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Heat Shock Protein 70 (Hsp70) as an Emerging Drug Target

https://doi.org/10.1021/jm100054f
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Surface‐Associated Heat Shock Proteins of Legionella pneumophila and Helicobacter pylori: Roles in Pathogenesis and Immunity
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The tetratricopeptide repeat: a structural motif mediating protein-protein interactions
inferredcites →https://doi.org/10.1002/anie.200802801openalex-snapshot
An Apoptosis‐Inducing Small Molecule That Binds to Heat Shock Protein 70
inferredcites →https://doi.org/10.1002/bip.21302openalex-snapshot
Hsp70 molecular chaperones and Parkinson's disease
inferredcites →https://doi.org/10.1002/cmdc.200600112openalex-snapshot
Hsp90 as a Target for Drug Development
inferredcites →https://doi.org/10.1002/jcp.1131openalex-snapshot
Hsp90: Chaperoning signal transduction
inferredcites →https://doi.org/10.1002/jnr.21721openalex-snapshot
Two motifs within the tau microtubule‐binding domain mediate its association with the hsc70 molecular chaperone
inferredcites →https://doi.org/10.1006/bbrc.1996.0103openalex-snapshot
T Cell Lymphoma in Transgenic Mice Expressing the HumanHsp70Gene
inferredcites →https://doi.org/10.1006/bbrc.1998.9775openalex-snapshot
Identification of a Binding Site on Hsc70 for the Immunosuppressant 15-Deoxyspergualin
inferredcites →https://doi.org/10.1006/bbrc.2001.5427openalex-snapshot
Heat Shock Proteins: Endogenous Modulators of Apoptotic Cell Death
inferredcites →https://doi.org/10.1006/excr.2000.4992openalex-snapshot
Heat-Shock Protein 70 Can Replace Viral Protein R of HIV-1 during Nuclear Import of the Viral Preintegration Complex
inferredcites →https://doi.org/10.1006/jmbi.1997.1072openalex-snapshot
The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system 1 1Edited by J.Karn
inferredcites →https://doi.org/10.1007/bf00335656openalex-snapshot
Pharmacokinetics of 15-deoxyspergualin studied in renal transplant patients receiving the drug during graft rejection
inferredcites →https://doi.org/10.1007/bf00873965openalex-snapshot
Phase II study of deoxyspergualin in metastatic breast cancer
inferredcites →https://doi.org/10.1007/s00018-004-4464-6openalex-snapshot
Hsp70 chaperones: Cellular functions and molecular mechanism
inferredcites →https://doi.org/10.1007/s00018-006-6192-6openalex-snapshot
The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones
inferredcites →https://doi.org/10.1007/s00018-008-7535-2openalex-snapshot
The BAG proteins: a ubiquitous family of chaperone regulators
inferredcites →https://doi.org/10.1007/s00109-007-0251-9openalex-snapshot
Celastrol inhibits polyglutamine aggregation and toxicity though induction of the heat shock response
inferredcites →https://doi.org/10.1007/s00280-009-1194-3openalex-snapshot
A novel, small molecule inhibitor of Hsc70/Hsp70 potentiates Hsp90 inhibitor induced apoptosis in HCT116 colon carcinoma cells
inferredcites →https://doi.org/10.1007/s10254-003-0021-1openalex-snapshot
Hsp70 and Hsp90—a relay team for protein folding
inferredcites →https://doi.org/10.1007/s12192-008-0064-yopenalex-snapshot
Polyamine compound deoxyspergualin inhibits heat shock protein-induced activation of immature dendritic cells
inferredcites →https://doi.org/10.1016/0042-6822(91)90033-8openalex-snapshot
Immunological evidence for the association between Simian Virus 40 115-kDa super T antigen and hsp70 proteins in rat, monkey, and human cells
inferredcites →https://doi.org/10.1016/j.ab.2007.08.020openalex-snapshot
High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK
inferredcites →https://doi.org/10.1016/j.ab.2007.12.009openalex-snapshot
Identification of small molecules that modify the protein folding activity of heat shock protein 70
inferredcites →https://doi.org/10.1016/j.bbrc.2004.10.037openalex-snapshot
A single amino acid substitution differentiates Hsp70-dependent effects on α-synuclein degradation and toxicity
inferredcites →https://doi.org/10.1016/j.bmc.2007.12.014openalex-snapshot
Pyrimidinone-peptoid hybrid molecules with distinct effects on molecular chaperone function and cell proliferation
inferredcites →https://doi.org/10.1016/j.bmcl.2007.11.027openalex-snapshot
Chemical modulators of heat shock protein 70 (Hsp70) by sequential, microwave-accelerated reactions on solid phase
inferredcites →https://doi.org/10.1016/j.bmcl.2009.04.062openalex-snapshot
Identification of Hsp70 modulators through modeling of the substrate binding domain
inferredcites →https://doi.org/10.1016/j.canlet.2006.12.038openalex-snapshot
Mortalin sensitizes human cancer cells to MKT-077-induced senescence
inferredcites →https://doi.org/10.1016/j.ccr.2008.08.002openalex-snapshot
Dual Targeting of HSC70 and HSP72 Inhibits HSP90 Function and Induces Tumor-Specific Apoptosis
inferredcites →https://doi.org/10.1016/j.cell.2006.04.014openalex-snapshot
Molecular Chaperones and Protein Quality Control
inferredcites →https://doi.org/10.1016/j.chembiol.2009.02.014openalex-snapshot
A Soluble Sulfogalactosyl Ceramide Mimic Promotes ΔF508 CFTR Escape from Endoplasmic Reticulum Associated Degradation
inferredcites →https://doi.org/10.1016/j.exger.2007.12.001openalex-snapshot
Nonenzymatic posttranslational protein modifications in ageing
inferredcites →https://doi.org/10.1016/j.febslet.2007.05.036openalex-snapshot
Molecular chaperones regulate p53 and suppress senescence programs
inferredcites →https://doi.org/10.1016/j.febslet.2007.05.039openalex-snapshot
The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions
inferredcites →https://doi.org/10.1016/j.febslet.2007.05.040openalex-snapshot
Inhibitors of the heat shock response: Biology and pharmacology
inferredcites →https://doi.org/10.1016/j.febslet.2009.04.011openalex-snapshot
HSP70 protects BCL2L12 and BCL2L12A from N‐terminal ubiquitination‐mediated proteasomal degradation
inferredcites →https://doi.org/10.1016/j.febslet.2009.09.047openalex-snapshot
Short peptides derived from the BAG‐1 C‐terminus inhibit the interaction between BAG‐1 and HSC70 and decrease breast cancer cell growth
inferredcites →https://doi.org/10.1016/j.imlet.2007.12.017openalex-snapshot
Innate immunity meets with cellular stress at the IKK complex: Regulation of the IKK complex by HSP70 and HSP90
inferredcites →https://doi.org/10.1016/j.intimp.2007.02.015openalex-snapshot
15-deoxyspergualin prevents mucosal injury by inhibiting production of TNF-α and down-regulating expression of MD-1 in a murine model of TNBS-induced colitis
inferredcites →https://doi.org/10.1016/j.jmb.2008.02.013openalex-snapshot
Structural Studies on the Co-chaperone Hop and Its Complexes with Hsp90
inferredcites →https://doi.org/10.1016/j.mad.2005.01.008openalex-snapshot
Proteasomal activity in brain differs between species and brain regions and changes with age
inferredcites →https://doi.org/10.1016/j.molcel.2007.08.022openalex-snapshot
Structural Basis of J Cochaperone Binding and Regulation of Hsp70
inferredcites →https://doi.org/10.1016/j.molcel.2009.09.023openalex-snapshot
A Small Molecule Inhibitor of Inducible Heat Shock Protein 70
inferredcites →https://doi.org/10.1016/j.nbd.2008.10.016openalex-snapshot
In vivo suppression of polyglutamine neurotoxicity by C-terminus of Hsp70-interacting protein (CHIP) supports an aggregation model of pathogenesis
inferredcites →https://doi.org/10.1016/j.pharmthera.2007.06.006openalex-snapshot
The role of amyloid β peptide 42 in Alzheimer's disease
inferredcites →https://doi.org/10.1016/j.tibs.2003.08.009openalex-snapshot
More than folding: localized functions of cytosolic chaperones
inferredcites →https://doi.org/10.1016/j.tins.2008.07.004openalex-snapshot
Polyglutamine neurodegeneration: protein misfolding revisited
inferredcites →https://doi.org/10.1016/j.transproceed.2004.12.289openalex-snapshot
Deoxyspergualin Prophylaxis With Tacrolimus Further Improves Long-Term Graft Survival in Living-Related Renal-Transplant Recipients Transfused With Donor-Specific Blood
inferredcites →https://doi.org/10.1016/j.virol.2005.05.004openalex-snapshot
Evidence for an association between heat shock protein 70 and the respiratory syncytial virus polymerase complex within lipid-raft membranes during virus infection
inferredcites →https://doi.org/10.1016/j.yexcr.2007.07.034openalex-snapshot
Modulation of polyglutamine inclusion formation by the Hsp70 chaperone machine
inferredcites →https://doi.org/10.1016/j.ymthe.2004.09.007openalex-snapshot
Hsp70 Gene Transfer by Adeno-associated Virus Inhibits MPTP-Induced Nigrostriatal Degeneration in the Mouse Model of Parkinson Disease
inferredcites →https://doi.org/10.1016/s0006-2952(98)00376-1openalex-snapshot
Selectivity of the molecular chaperone-specific immunosuppressive agent 15-deoxyspergualin
inferredcites →https://doi.org/10.1016/s0006-8993(02)04275-0openalex-snapshot
Overexpression of heat shock protein 70 in R6/2 Huntington’s disease mice has only modest effects on disease progression
inferredcites →https://doi.org/10.1016/s0008-6215(01)00209-9openalex-snapshot
The aglycone of sulfogalactolipids can alter the sulfate ester substitution position required for hsc70 recognition
inferredcites →https://doi.org/10.1016/s0014-5793(01)02435-8openalex-snapshot
Mutations in the interdomain linker region of DnaK abolish the chaperone action of the DnaK/DnaJ/GrpE system
inferredcites →https://doi.org/10.1016/s0014-5793(02)03570-6openalex-snapshot
HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor
inferredcites →https://doi.org/10.1016/s0014-5793(98)01242-3openalex-snapshot
Role of Hsp70 in regulation of stress‐kinase JNK: implications in apoptosis and aging
inferredcites →https://doi.org/10.1016/s0014-5793(99)01428-3openalex-snapshot
ATPase activity of the heat shock protein Hsp72 is dispensable for its effects on dephosphorylation of stress kinase JNK and on heat‐induced apoptosis
inferredcites →https://doi.org/10.1016/s0021-9258(17)37706-2openalex-snapshot
The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication.
inferredcites →https://doi.org/10.1016/s0092-8674(00)80830-2openalex-snapshot
Structure of TPR Domain–Peptide Complexes
inferredcites →https://doi.org/10.1016/s0167-4943(96)00745-5openalex-snapshot
Alterations in the chaperone activity of HSP70 in aging organisms
inferredcites →https://doi.org/10.1016/s0192-0561(99)00017-xopenalex-snapshot
Analysis of in vivo immunosuppressive and in vitro interaction with constitutive heat shock protein 70 activity of LF08-0299 (Tresperimus) and analogues
inferredcites →https://doi.org/10.1016/s0196-9781(02)00244-9openalex-snapshot
Development of novel antibacterial peptides that kill resistant isolates
inferredcites →https://doi.org/10.1016/s0952-7915(01)00297-7openalex-snapshot
Roles of heat-shock proteins in antigen presentation and cross-presentation
inferredcites →https://doi.org/10.1016/s0955-470x(96)80025-5openalex-snapshot
15-deoxyspergualin: Immunotherapy in solid organ and cellular transplantation
inferredcites →https://doi.org/10.1021/bi0012843openalex-snapshot
Interaction between Heat Shock Proteins and Antimicrobial Peptides
inferredcites →https://doi.org/10.1021/bi001643uopenalex-snapshot
Hsp70s Contain a Specific Sulfogalactolipid Binding Site. Differential Aglycone Influence on Sulfogalactosyl Ceramide Binding by Recombinant Prokaryotic and Eukaryotic Hsp70 Family Members
inferredcites →https://doi.org/10.1021/bi00175a027openalex-snapshot
Quantitation of the Interaction of the Immunosuppressant Deoxyspergualin and Analogs with Hsc70 and Hsp90
inferredcites →https://doi.org/10.1021/bi00252a031openalex-snapshot
ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain
inferredcites →https://doi.org/10.1021/bi002656aopenalex-snapshot
The Antibacterial Peptide Pyrrhocoricin Inhibits the ATPase Actions of DnaK and Prevents Chaperone-Assisted Protein Folding
inferredcites →https://doi.org/10.1021/bi800639zopenalex-snapshot
Structural and Functional Diversities between Members of the Human HSPB, HSPH, HSPA, and DNAJ Chaperone Families
inferredcites →https://doi.org/10.1021/bi972025popenalex-snapshot
Kinetic Characterization of the ATPase Cycle of the DnaK Molecular Chaperone
inferredcites →https://doi.org/10.1021/jm050347iopenalex-snapshot
Designer Antibacterial Peptides Kill Fluoroquinolone-Resistant Clinical Isolates
inferredcites →https://doi.org/10.1021/jm801627aopenalex-snapshot
Novel Adenosine-Derived Inhibitors of 70 kDa Heat Shock Protein, Discovered Through Structure-Based Design
inferredcites →https://doi.org/10.1021/jm980431gopenalex-snapshot
Structure−Immunosuppressive Activity Relationships of New Analogues of 15-Deoxyspergualin. 1. Structural Modifications of the Hydroxyglycine Moiety
inferredcites →https://doi.org/10.1021/jm991043xopenalex-snapshot
Structure−Immunosuppressive Activity Relationships of New Analogues of 15-Deoxyspergualin. 2. Structural Modifications of the Spermidine Moiety
inferredcites →https://doi.org/10.1023/a:1008336904585openalex-snapshot
Phase I trial of the selective mitochondrial toxin MKT 077 in chemo-resistant solid tumours
inferredcites →https://doi.org/10.1038/346623a0openalex-snapshot
Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
inferredcites →https://doi.org/10.1038/35019501openalex-snapshot
Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome
inferredcites →https://doi.org/10.1038/35019510openalex-snapshot
Negative regulation of the Apaf-1 apoptosome by Hsp70
inferredcites →https://doi.org/10.1038/35050618openalex-snapshot
The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
inferredcites →https://doi.org/10.1038/353726a0openalex-snapshot
Peptide-binding specificity of the molecular chaperone BiP
inferredcites →https://doi.org/10.1038/70532openalex-snapshot
Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
inferredcites →https://doi.org/10.1038/76819openalex-snapshot
Multistep mechanism of substrate binding determines chaperone activity of Hsp70.
inferredcites →https://doi.org/10.1038/89113openalex-snapshot
Overexpression of heat-shock proteins reduces survival of Mycobacterium tuberculosis in the chronic phase of infection
inferredcites →https://doi.org/10.1038/bjc.1996.334openalex-snapshot
Drug resistance against gemcitabine and topotecan mediated by constitutive hsp70 overexpression in vitro: implication of quercetin as sensitiser in chemotherapy
inferredcites →https://doi.org/10.1038/emboj.2009.383openalex-snapshot
Structure of clathrin coat with bound Hsc70 and auxilin: mechanism of Hsc70‐facilitated disassembly
inferredcites →https://doi.org/10.1038/nature08710openalex-snapshot
Hsp70 stabilizes lysosomes and reverts Niemann–Pick disease-associated lysosomal pathology
inferredcites →https://doi.org/10.1038/ncb0901-839openalex-snapshot
Heat-shock protein 70 antagonizes apoptosis-inducing factor
inferredcites →https://doi.org/10.1038/nchembio.2007.10openalex-snapshot
Selective compounds define Hsp90 as a major inhibitor of apoptosis in small-cell lung cancer
inferredcites →https://doi.org/10.1038/nrn2194openalex-snapshot
Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
inferredcites →https://doi.org/10.1038/sj.cdd.4401369openalex-snapshot
hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria
inferredcites →https://doi.org/10.1038/sj.emboj.7601970openalex-snapshot
Chaperones in control of protein disaggregation
inferredcites →https://doi.org/10.1038/sj.leu.2404463openalex-snapshot
Overexpression of the heat-shock protein 70 is associated to imatinib resistance in chronic myeloid leukemia
inferredcites →https://doi.org/10.1038/sj.onc.1207529openalex-snapshot
Molecular chaperones and the stress of oncogenesis
inferredcites →https://doi.org/10.1038/sj.onc.1208495openalex-snapshot
Increased expression of the major heat shock protein Hsp72 in human prostate carcinoma cells is dispensable for their viability but confers resistance to a variety of anticancer agents
inferredcites →https://doi.org/10.1042/bj20070084openalex-snapshot
Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions
inferredcites →https://doi.org/10.1042/bst0320617openalex-snapshot
Mechanism of substrate recognition by Hsp70 chaperones
inferredcites →https://doi.org/10.1046/j.1365-2567.2003.01725.xopenalex-snapshot
Facets of heat shock protein 70 show immunotherapeutic potential
inferredcites →https://doi.org/10.1046/j.1432-1033.2002.03119.xopenalex-snapshot
Identification of crucial residues for the antibacterial activity of the proline‐rich peptide, pyrrhocoricin
inferredcites →https://doi.org/10.1053/j.gastro.2009.01.070openalex-snapshot
Heat Shock Protein 70 Inhibits Apoptosis in Cancer Cells Through Simultaneous and Independent Mechanisms
inferredcites →https://doi.org/10.1073/pnas.042688099openalex-snapshot
Uncoating ATPase Hsc70 is recruited by invariant chain and controls the size of endocytic compartments
inferredcites →https://doi.org/10.1073/pnas.0506249102openalex-snapshot
Pharmacological induction of heat-shock proteins alleviates polyglutamine-mediated motor neuron disease
inferredcites →https://doi.org/10.1073/pnas.070047997openalex-snapshot
Bax degradation by the ubiquitin/proteasome-dependent pathway: Involvement in tumor survival and progression
inferredcites →https://doi.org/10.1073/pnas.0900746106openalex-snapshot
Identification of a consensus motif in substrates bound by a Type I Hsp40
inferredcites →https://doi.org/10.1073/pnas.0903503106openalex-snapshot
Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
inferredcites →https://doi.org/10.1073/pnas.140202897openalex-snapshot
Hsp70 and Hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils
inferredcites →https://doi.org/10.1073/pnas.1832245100openalex-snapshot
Chaperone-mediated in vitro assembly of Polyomavirus capsids
inferredcites →https://doi.org/10.1073/pnas.242720499openalex-snapshot
Chaperones increase association of tau protein with microtubules
inferredcites →https://doi.org/10.1073/pnas.89.15.7139openalex-snapshot
Partial loss of function mutations in DnaK, the Escherichia coli homologue of the 70-kDa heat shock proteins, affect highly conserved amino acids implicated in ATP binding and hydrolysis.
inferredcites →https://doi.org/10.1073/pnas.89.16.7290openalex-snapshot
An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins.
inferredcites →https://doi.org/10.1073/pnas.95.11.6108openalex-snapshot
Role of the J-domain in the cooperation of Hsp40 with Hsp70
inferredcites →https://doi.org/10.1073/pnas.96.10.5452openalex-snapshot
Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones
inferredcites →https://doi.org/10.1073/pnas.97.14.7871openalex-snapshot
Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2
inferredcites →https://doi.org/10.1073/pnas.97.4.1589openalex-snapshot
Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins
inferredcites →https://doi.org/10.1073/pnas.97.6.2898openalex-snapshot
Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease
inferredcites →https://doi.org/10.1074/jbc.272.14.9002openalex-snapshot
Ubiquitin-dependent Degradation of Certain Protein Substrates in Vitro Requires the Molecular Chaperone Hsc70
inferredcites →https://doi.org/10.1074/jbc.273.11.6373openalex-snapshot
Proteasome Inhibitors Activate Stress Kinases and Induce Hsp72
inferredcites →https://doi.org/10.1074/jbc.273.27.17147openalex-snapshot
Heat Shock Protein 72 Modulates Pathways of Stress-induced Apoptosis
inferredcites →https://doi.org/10.1074/jbc.274.29.20223openalex-snapshot
The Function of HSP72 in Suppression of c-Jun N-terminal Kinase Activation Can Be Dissociated from Its Role in Prevention of Protein Damage
inferredcites →https://doi.org/10.1074/jbc.275.12.8772openalex-snapshot
Chaperones Hsp70 and Hsp40 Suppress Aggregate Formation and Apoptosis in Cultured Neuronal Cells Expressing Truncated Androgen Receptor Protein with Expanded Polyglutamine Tract
inferredcites →https://doi.org/10.1074/jbc.m006632200openalex-snapshot
Suppression of Stress Kinase JNK Is Involved in HSP72-mediated Protection of Myogenic Cells from Transient Energy Deprivation
inferredcites →https://doi.org/10.1074/jbc.m006732200openalex-snapshot
The ATPase Domain of hsp70 Possesses a Unique Binding Specificity for 3′-Sulfogalactolipids
inferredcites →https://doi.org/10.1074/jbc.m008535200openalex-snapshot
Identification of an Inhibitor of hsc70-mediated Protein Translocation and ATP Hydrolysis
inferredcites →https://doi.org/10.1074/jbc.m104140200openalex-snapshot
Chaperone Suppression of Cellular Toxicity of Huntingtin Is Independent of Polyglutamine Aggregation
inferredcites →https://doi.org/10.1074/jbc.m109.057208openalex-snapshot
Facilitating Akt Clearance via Manipulation of Hsp70 Activity and Levels
inferredcites →https://doi.org/10.1074/jbc.m206566200openalex-snapshot
The Assembly and Intermolecular Properties of the hsp70-Hop-hsp90 Molecular Chaperone Complex
inferredcites →https://doi.org/10.1074/jbc.m212049200openalex-snapshot
Polyglutamine Expansion Induces a Protein-damaging Stress Connecting Heat Shock Protein 70 to the JNK Pathway
inferredcites →https://doi.org/10.1074/jbc.m305838200openalex-snapshot
CHIP-Hsc70 Complex Ubiquitinates Phosphorylated Tau and Enhances Cell Survival
inferredcites →https://doi.org/10.1074/jbc.m314130200openalex-snapshot
Multiple Domains of the Co-chaperone Hop Are Important for Hsp70 Binding
inferredcites →https://doi.org/10.1074/jbc.m404857200openalex-snapshot
Small Molecule Modulators of Endogenous and Co-chaperone-stimulated Hsp70 ATPase Activity
inferredcites →https://doi.org/10.1074/jbc.m409062200openalex-snapshot
Hsp70 and Hsp40 Chaperones Do Not Modulate Retinal Phenotype in SCA7 Mice
inferredcites →https://doi.org/10.1074/jbc.m412042200openalex-snapshot
Co-chaperone CHIP Associates with Expanded Polyglutamine Protein and Promotes Their Degradation by Proteasomes
inferredcites →https://doi.org/10.1074/jbc.m509497200openalex-snapshot
Hsp70 Inhibits Heat-induced Apoptosis Upstream of Mitochondria by Preventing Bax Translocation
inferredcites →https://doi.org/10.1074/jbc.m513728200openalex-snapshot
Distinct hsp70 Domains Mediate Apoptosis-inducing Factor Release and Nuclear Accumulation
inferredcites →https://doi.org/10.1074/jbc.m601603200openalex-snapshot
CHIP Protects from the Neurotoxicity of Expanded and Wild-type Ataxin-1 and Promotes Their Ubiquitination and Degradation
inferredcites →https://doi.org/10.1074/jbc.m602533200openalex-snapshot
Differential Effects of Mitochondrial Heat Shock Protein 60 and Related Molecular Chaperones to Prevent Intracellular β-Amyloid-induced Inhibition of Complex IV and Limit Apoptosis
inferredcites →https://doi.org/10.1074/jbc.m606192200openalex-snapshot
Heat Shock Proteins 70 and 90 Inhibit Early Stages of Amyloid β-(1–42) Aggregation in Vitro
inferredcites →https://doi.org/10.1074/jbc.m607667200openalex-snapshot
Fatty Acyl Benzamido Antibacterials Based on Inhibition of DnaK-catalyzed Protein Folding
inferredcites →https://doi.org/10.1074/jbc.m609020200openalex-snapshot
Allosteric Regulation of Hsp70 Chaperones Involves a Conserved Interdomain Linker
inferredcites →https://doi.org/10.1074/jbc.m706379200openalex-snapshot
BAG-1 Associates with Hsc70·Tau Complex and Regulates the Proteasomal Degradation of Tau Protein
inferredcites →https://doi.org/10.1074/jbc.m709447200openalex-snapshot
Tubocapsenolide A, a Novel Withanolide, Inhibits Proliferation and Induces Apoptosis in MDA-MB-231 Cells by Thiol Oxidation of Heat Shock Proteins
inferredcites →https://doi.org/10.1074/jbc.m710521200openalex-snapshot
Heat Shock Transcription Factor 1-activating Compounds Suppress Polyglutamine-induced Neurodegeneration through Induction of Multiple Molecular Chaperones
inferredcites →https://doi.org/10.1083/jcb.200410065openalex-snapshot
A foldable CFTRΔF508 biogenic intermediate accumulates upon inhibition of the Hsc70–CHIP E3 ubiquitin ligase
inferredcites →https://doi.org/10.1084/jem.20040531openalex-snapshot
Heat Shock Protein 70 Promotes Cell Survival by Inhibiting Lysosomal Membrane Permeabilization
inferredcites →https://doi.org/10.1089/107662900419429openalex-snapshot
Antibiotic Susceptibility of Escherichia coli dnaK and dnaJ Mutants
inferredcites →https://doi.org/10.1093/embo-reports/kve206openalex-snapshot
From the cradle to the grave: molecular chaperones that may choose between folding and degradation
inferredcites →https://doi.org/10.1093/emboj/18.6.1492openalex-snapshot
The Hdj‐2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
inferredcites →https://doi.org/10.1093/hmg/10.12.1307openalex-snapshot
Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease
inferredcites →https://doi.org/10.1093/hmg/10.14.1511openalex-snapshot
Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice
inferredcites →https://doi.org/10.1093/hmg/11.5.515openalex-snapshot
Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy
inferredcites →https://doi.org/10.1093/hmg/9.13.2009openalex-snapshot
Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity
inferredcites →https://doi.org/10.1093/hmg/ddh083openalex-snapshot
CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation
inferredcites →https://doi.org/10.1093/hmg/ddm030openalex-snapshot
CHIP and HSPs interact with β-APP in a proteasome-dependent manner and influence Aβ metabolism
inferredcites →https://doi.org/10.1097/00007890-199303000-00010openalex-snapshot
15-DEOXYSPERGUALIN “RESCUE THERAPY” FOR METHYLPREDNISOLONE-RESISTANT REJECTION OF RENAL TRANSPLANTS AS COMPARED WITH ANTI-T CELL MONOCLONAL ANTIBODY (OKT3)
inferredcites →https://doi.org/10.1097/01.asn.0000048716.42876.14openalex-snapshot
15-Deoxyspergualin in Patients with Refractory ANCA-Associated Systemic Vasculitis
inferredcites →https://doi.org/10.1099/mic.0.2007/009506-0openalex-snapshot
Role for dnaK locus in tolerance of multiple stresses in Staphylococcus aureus
inferredcites →https://doi.org/10.1101/gad.11.9.1098openalex-snapshot
DnaJ/hsp40 chaperone domain of SV40 large T antigen promotes efficient viral DNA replication.
inferredcites →https://doi.org/10.1101/gad.305405openalex-snapshot
Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms
inferredcites →https://doi.org/10.1111/j.1365-2249.2006.03231.xopenalex-snapshot
In vivoeffects of cyclic administration of 15-deoxyspergualin on leucocyte function in patients with Wegener's granulomatosis
inferredcites →https://doi.org/10.1111/j.1471-4159.2004.02713.xopenalex-snapshot
U‐box protein carboxyl terminus of Hsc70‐interacting protein (CHIP) mediates poly‐ubiquitylation preferentially on four‐repeat Tau and is involved in neurodegeneration of tauopathy
inferredcites →https://doi.org/10.1111/j.1471-4159.2009.06302.xopenalex-snapshot
The pathogenic mechanisms of polyglutamine diseases and current therapeutic strategies
inferredcites →https://doi.org/10.1111/j.1582-4934.2008.00575.xopenalex-snapshot
Synergistic promotion of breast cancer cells death by targeting molecular chaperone GRP78 and heat shock protein 70
inferredcites →https://doi.org/10.1111/j.1742-4658.2007.06019.xopenalex-snapshot
The viral SV40 T antigen cooperates with dj2 to enhance hsc70 chaperone function
inferredcites →https://doi.org/10.1111/j.1747-0285.2009.00869.xopenalex-snapshot
Small Molecule DnaK Modulators Targeting the β‐Domain
inferredcites →https://doi.org/10.1111/j.1749-6632.1993.tb35863.xopenalex-snapshot
15‐Deoxyspergualin: A Novel Immunosuppressive Drug with Clinical Potentiala
inferredcites →https://doi.org/10.1111/j.1749-6632.1993.tb35866.xopenalex-snapshot
A Member of the Hsp70 Family of Heat‐Shock Proteins Is a Putative Target for the Immunosuppressant 15‐Deoxyspergualin.
inferredcites →https://doi.org/10.1111/j.1749-6632.2000.tb05605.xopenalex-snapshot
Heat Shock Protein 70 Is Required for the Survival of Cancer Cells
inferredcites →https://doi.org/10.1124/mol.107.042697openalex-snapshot
OSU-03012 Stimulates PKR-Like Endoplasmic Reticulum-Dependent Increases in 70-kDa Heat Shock Protein Expression, Attenuating Its Lethal Actions in Transformed Cells
inferredcites →https://doi.org/10.1126/science.1067389openalex-snapshot
Chaperone Suppression of α-Synuclein Toxicity in a Drosophila Model for Parkinson's Disease
inferredcites →https://doi.org/10.1126/science.1132939openalex-snapshot
The Connectivity Map: Using Gene-Expression Signatures to Connect Small Molecules, Genes, and Disease
inferredcites →https://doi.org/10.1126/science.1411548openalex-snapshot
Interaction of the Immunosuppressant Deoxyspergualin with a Member of the Hsp70 Family of Heat Shock Proteins
inferredcites →https://doi.org/10.1126/science.272.5268.1606openalex-snapshot
Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK
inferredcites →https://doi.org/10.1126/science.2799391openalex-snapshot
A Role for a 70-Kilodalton Heat Shock Protein in Lysosomal Degradation of Intracellular Proteins
inferredcites →https://doi.org/10.1128/iai.01882-05openalex-snapshot
Stress Wars: the Direct Role of Host and Bacterial Molecular Chaperones in Bacterial Infection
inferredcites →https://doi.org/10.1128/iai.70.3.1631-1634.2002openalex-snapshot
Induction ofdnaKthrough Its Native Heat Shock Promoter Is Necessary for Intramacrophagic Replication ofBrucella suis
inferredcites →https://doi.org/10.1128/iai.72.3.1364-1373.2004openalex-snapshot
The DnaK/DnaJ Chaperone Machinery of Salmonella enterica Serovar Typhimurium Is Essential for Invasion of Epithelial Cells and Survival within Macrophages, Leading to Systemic Infection
inferredcites →https://doi.org/10.1128/jb.01655-06openalex-snapshot
Physiologic Effects of Forced Down-Regulation of dnaK and groEL Expression in Streptococcus mutans
inferredcites →https://doi.org/10.1128/jb.172.9.4827-4835.1990openalex-snapshot
Isolation and characterization of dnaJ null mutants of Escherichia coli
inferredcites →https://doi.org/10.1128/jvi.76.8.4096-4102.2002openalex-snapshot
Heat Shock Cognate Protein 70 Is Involved in Rotavirus Cell Entry
inferredcites →https://doi.org/10.1128/jvi.77.13.7254-7260.2003openalex-snapshot
Interaction of Rotaviruses with Hsc70 during Cell Entry Is Mediated by VP5
inferredcites →https://doi.org/10.1128/jvi.80.10.5086-5091.2006openalex-snapshot
Chaperone-Mediated In Vitro Disassembly of Polyoma- and Papillomaviruses
inferredcites →https://doi.org/10.1128/mcb.01041-08openalex-snapshot
Heat Shock Protein Hsp72 Controls Oncogene-Induced Senescence Pathways in Cancer Cells
inferredcites →https://doi.org/10.1128/mcb.19.4.2547openalex-snapshot
Protein-Damaging Stresses Activate c-Jun N-Terminal Kinase via Inhibition of Its Dephosphorylation: a Novel Pathway Controlled by HSP72
inferredcites →https://doi.org/10.1128/mcb.19.6.4535openalex-snapshot
Identification of CHIP, a Novel Tetratricopeptide Repeat-Containing Protein That Interacts with Heat Shock Proteins and Negatively Regulates Chaperone Functions
inferredcites →https://doi.org/10.1128/mcb.20.15.5749-5757.2000openalex-snapshot
Species-Specific Elements in the Large T-Antigen J Domain Are Required for Cellular Transformation and DNA Replication by Simian Virus 40
inferredcites →https://doi.org/10.1128/mcb.20.18.6826-6836.2000openalex-snapshot
Hsp72-Mediated Suppression of c-Jun N-Terminal Kinase Is Implicated in Development of Tolerance to Caspase-Independent Cell Death
inferredcites →https://doi.org/10.1128/mcb.22.10.3415-3424.2002openalex-snapshot
Hsp72 and Stress Kinase c-jun N-Terminal Kinase Regulate the Bid-Dependent Pathway in Tumor Necrosis Factor-Induced Apoptosis
inferredcites →https://doi.org/10.1146/annurev.biochem.70.1.603openalex-snapshot
Folding of Newly Translated Proteins In Vivo: The Role of Molecular Chaperones
inferredcites →https://doi.org/10.1152/ajpcell.00049.2003openalex-snapshot
HSP72 inhibits apoptosis-inducing factor release in ATP-depleted renal epithelial cells
inferredcites →https://doi.org/10.1158/0008-5472.can-05-3692openalex-snapshot
Targeting Heat Shock Response to Sensitize Cancer Cells to Proteasome and Hsp90 Inhibitors
inferredcites →https://doi.org/10.1158/0008-5472.can-06-1586openalex-snapshot
(−)−Epigallocatechin Gallate Overcomes Resistance to Etoposide-Induced Cell Death by Targeting the Molecular Chaperone Glucose-Regulated Protein 78
inferredcites →https://doi.org/10.1158/0008-5472.can-06-3796openalex-snapshot
High Levels of Heat Shock Protein Hsp72 in Cancer Cells Suppress Default Senescence Pathways
inferredcites →https://doi.org/10.1172/jci29715openalex-snapshot
The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins
inferredcites →https://doi.org/10.1177/153537020322800201openalex-snapshot
Regulation of Signaling Protein Function and Trafficking by the hsp90/hsp70-Based Chaperone Machinery
inferredcites →https://doi.org/10.1179/joc.2008.20.3.355openalex-snapshot
Epigallocatechin-3-Gallate Suppressed the Over-Expression of HSP 70 and MDR1 Induced by Heat Shock in SGC 7901
inferredcites →https://doi.org/10.1182/blood-2004-01-0081openalex-snapshot
Heat-shock protein 70 exerts opposing effects on Vpr-dependent and Vpr-independent HIV-1 replication in macrophages
inferredcites →https://doi.org/10.1182/blood-2006-08-040634openalex-snapshot
Hsp72 up-regulates Epstein-Barr virus EBNALP coactivation with EBNA2
inferredcites →https://doi.org/10.1186/1471-2180-3-16openalex-snapshot
Effects of disruption of heat shock genes on susceptibility of Escherichia coli to fluoroquinolones
showing the first 200 of 231 · page through all 231

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4652831openalex-extracted
Enhancement Biohydrogen Production from Lignocellulosic Biomass in Non-Polyhydroxybutyrate-Producing Clostridium Acetobutylicum Atcc 824 by Phasin Gene Introduction
inferred← citeshttps://doi.org/10.2139/ssrn.4775041openalex-extracted
Synthesis, Cytotoxic Evaluation, and in Silico Studies of Some New Benzimidazole and Benzothiazole Derivatives as Potential Dual Inhibitors of Hsp70 and Foxm1
inferred← citeshttps://doi.org/10.1002/1873-3468.12913openalex-snapshot
Peptide fragments of Hsp70 modulate its chaperone activity and sensitize tumor cells to anti‐cancer drugs
inferred← citeshttps://doi.org/10.1002/9783527659685.ch23openalex-snapshot
Targeting HSP70 to Fight Cancer and Bad Bugs: One and the Same Battle?
inferred← citeshttps://doi.org/10.1002/adfm.202212085openalex-snapshot
A Biodegradable Antigen Nanocapsule Promotes Anti‐Tumor Immunity via the cGAS‐STING Pathway
inferred← citeshttps://doi.org/10.1002/ange.1777033openalex-snapshot
Reengineering Protease Inhibitors to Disrupt Hsp70 Chaperone Function
inferred← citeshttps://doi.org/10.1002/anie.1777033openalex-snapshot
Reengineering Protease Inhibitors to Disrupt Hsp70 Chaperone Function
inferred← citeshttps://doi.org/10.1002/aro2.70032openalex-snapshot
Reduction of Ribonucleotide Reductase Subunit RRM2 Potentially Impairs Gut Function of Woody Breast Broilers
inferred← citeshttps://doi.org/10.1002/cbic.201100524openalex-snapshot
Inhibition of Heat Shock Transcription Factor Binding by a Linear Polyamide Binding in an Unusual 1:1 Mode
inferred← citeshttps://doi.org/10.1002/cbin.12164openalex-snapshot
Expression and localization of apelin and apelin receptor protein in the oviduct of letrozole‐induced hyperandrogenized mice
inferred← citeshttps://doi.org/10.1002/inm3.70022openalex-snapshot
Targeting GRP78 and the Proteostasis Network to Break the Therapeutic Ceiling in Neuroendocrine Prostate Cancer
inferred← citeshttps://doi.org/10.1002/jat.2845openalex-snapshot
Cellular‐signaling pathways unveil the carcinogenic potential of chemicals
inferred← citeshttps://doi.org/10.1002/jat.70149openalex-snapshot
High Environmental Ammonia Causes Induction in the Expression of Heat Shock Factor 1, Heat Shock Protein 70, and 90 Genes in Different Tissues of Air‐Breathing Stinging Catfish ( Heteropneustes fossilis )
inferred← citeshttps://doi.org/10.1002/prca.201300097openalex-snapshot
Intestinal proteomics in pig models of necrotising enterocolitis, short bowel syndrome and intrauterine growth restriction
inferred← citeshttps://doi.org/10.1002/pro.70575openalex-snapshot
ATP modulates holdase activity of fungal and human 110‐kilodalton heat shock proteins to promote protein folding
inferred← citeshttps://doi.org/10.1002/pros.23239openalex-snapshot
A Novel Class of Hsp90 C-Terminal Modulators Have Pre-Clinical Efficacy in Prostate Tumor Cells Without Induction of a Heat Shock Response
inferred← citeshttps://doi.org/10.1002/prot.24731openalex-snapshot
Common functionally important motions of the nucleotide‐binding domain of H sp70
inferred← citeshttps://doi.org/10.1002/slct.202404047openalex-snapshot
Malaria Prophylactics Through Heat Shock Protein 70x Chaperone Inhibition by Alkaloids of Polyalthia longifolia : An I n Silico Investigation
inferred← citeshttps://doi.org/10.1007/7355_2015_88openalex-snapshot
Allosteric Inhibitors of Hsp70: Drugging the Second Chaperone of Tumorigenesis
inferred← citeshttps://doi.org/10.1007/7355_2015_90openalex-snapshot
The Effect of Structure and Mechanism of the Hsp70 Chaperone on the Ability to Identify Chemical Modulators and Therapeutics
inferred← citeshttps://doi.org/10.1007/7355_2015_96openalex-snapshot
Evaluating Dual Hsp90 and Hsp70 Inhibition as a Cancer Therapy
inferred← citeshttps://doi.org/10.1007/7355_2026_190openalex-snapshot
The Role of Molecular Chaperones in Tau Proteostasis: Potential Therapeutic Opportunities in Tauopathies
inferred← citeshttps://doi.org/10.1007/7515_2020_20openalex-snapshot
Heat Shock Proteins and Pain
inferred← citeshttps://doi.org/10.1007/978-1-0716-4213-9_9openalex-snapshot
Prediction of the Stability of Protein Substructures Using AI/ML Techniques
inferred← citeshttps://doi.org/10.1007/978-1-4939-7477-1_6openalex-snapshot
Fluorescent-Linked Enzyme Chemoproteomic Strategy (FLECS) for Identifying HSP70 Inhibitors
inferred← citeshttps://doi.org/10.1007/978-3-030-03952-3_13openalex-snapshot
IER5 Is a p53-Regulated Activator of HSF1 That Contributes to Promotion of Cancer
inferred← citeshttps://doi.org/10.1007/978-3-030-03952-3_14openalex-snapshot
Heat Shock Proteins in Digestive Tract Cancer: Molecular Mechanism and Therapeutic Potential
inferred← citeshttps://doi.org/10.1007/978-3-030-46943-6_21openalex-snapshot
Review on Regulation of Heat Shock Protein 70 During Radiotherapy in Cancer Patients
inferred← citeshttps://doi.org/10.1007/978-3-030-78397-6_2openalex-snapshot
General Structural and Functional Features of Molecular Chaperones
inferred← citeshttps://doi.org/10.1007/978-3-030-78397-6_9openalex-snapshot
Heat Shock Proteins as Targets for Novel Antimalarial Drug Discovery
inferred← citeshttps://doi.org/10.1007/978-3-319-17211-8_10openalex-snapshot
New Indications for HSP90 and HSP70 Inhibitors as Antiviral Drugs
inferred← citeshttps://doi.org/10.1007/978-3-319-23449-6_4openalex-snapshot
Managing the Adaptive Proteostatic Landscape: Restoring Resilience in Alpha-1 Antitrypsin Deficiency
inferred← citeshttps://doi.org/10.1007/978-3-319-89551-2_19openalex-snapshot
Suppression of HSP70 Expression by Quercetin and Its Therapeutic Potential Against Cancer
inferred← citeshttps://doi.org/10.1007/978-3-642-28175-4_4openalex-snapshot
Targeting Conserved Pathways as a Strategy for Novel Drug Development: Disabling the Cellular Stress Response
inferred← citeshttps://doi.org/10.1007/978-94-007-3027-4_14openalex-snapshot
Many Faces of Mortalin and Tid1
inferred← citeshttps://doi.org/10.1007/978-94-007-7192-5_7openalex-snapshot
Molecular-Genetic Testing in Hepatocellular Carcinoma and Its Premalignant Conditions
inferred← citeshttps://doi.org/10.1007/978-94-007-7438-4_2openalex-snapshot
General Structural and Functional Features of Molecular Chaperones
inferred← citeshttps://doi.org/10.1007/978-94-017-9421-3_10openalex-snapshot
The Hsp70 Family of Heat Shock Proteins in Tumorigenesis: From Molecular Mechanisms to Therapeutic Opportunities
inferred← citeshttps://doi.org/10.1007/978-981-95-6099-8_6openalex-snapshot
Ubiquitin-Proteasome System in the Cellular Proteostasis
inferred← citeshttps://doi.org/10.1007/s00018-014-1622-3openalex-snapshot
Gold nanoparticles induce nuclear damage in breast cancer cells, which is further amplified by hyperthermia
inferred← citeshttps://doi.org/10.1007/s00018-019-03302-2openalex-snapshot
Targeting Hsp70 facilitated protein quality control for treatment of polyglutamine diseases
inferred← citeshttps://doi.org/10.1007/s00203-016-1246-0openalex-snapshot
The Rab1 in host cells modulates Brucella intracellular survival and binds to Brucella DnaK protein
inferred← citeshttps://doi.org/10.1007/s00300-022-03006-7openalex-snapshot
Can heat shock protein 70 (HSP70) serve as biomarkers in Antarctica for future ocean acidification, warming and salinity stress?
inferred← citeshttps://doi.org/10.1007/s00396-012-2629-7openalex-snapshot
Synthesis and characterization of pH-responsive diblock copolymers with cadaverine side groups
inferred← citeshttps://doi.org/10.1007/s10162-014-0491-7openalex-snapshot
Heat Shock Protein-Mediated Protection Against Cisplatin-Induced Hair Cell Death
inferred← citeshttps://doi.org/10.1007/s10266-026-01530-0openalex-snapshot
Fibroblast stress responses to 3D-spheroid culture and thermal challenge, and stem-cell secretome-mediated repair: an exploratory in vitro investigation
inferred← citeshttps://doi.org/10.1007/s10353-015-0317-9openalex-snapshot
Significant relationship between preoperative serum concentration of anti-heat shock protein 70 antibody and postoperative morbidity in patients with esophageal cancer
inferred← citeshttps://doi.org/10.1007/s10517-024-06075-2openalex-snapshot
Association between Polymorphisms of Heat Shock Protein HSPA5 and Risk of Type 2 Diabetes Mellitus
inferred← citeshttps://doi.org/10.1007/s10787-025-01754-6openalex-snapshot
Chaperone-mediated autophagy, heat shock protein 70, and serotonin: novel targets of beta-hydroxybutyrate in HFFD/LPS-induced sporadic Alzheimer’s disease model
inferred← citeshttps://doi.org/10.1007/s11064-016-2084-9openalex-snapshot
Targeting of Heat Shock Protein HSPA6 (HSP70B′) to the Periphery of Nuclear Speckles is Disrupted by a Transcription Inhibitor Following Thermal Stress in Human Neuronal Cells
inferred← citeshttps://doi.org/10.1007/s11270-018-3920-0openalex-snapshot
HSP70 as a Biomarker: an Excellent Tool in Environmental Contamination Analysis—a Review
inferred← citeshttps://doi.org/10.1007/s11356-019-07203-6openalex-snapshot
Histopatology and HSP70 analysis of the midgut of Rhinocricus padbergi (Diplopoda) in the evaluation of the toxicity of two new metallic-insecticides
inferred← citeshttps://doi.org/10.1007/s11626-024-00924-0openalex-snapshot
HSP70 protects PC12 cells against TBHP-induced apoptosis and oxidative stress by activating the Nrf2/HO-1 signaling pathway
inferred← citeshttps://doi.org/10.1007/s12011-018-1622-5openalex-snapshot
Borax Alleviates Copper-Induced Renal Injury via Inhibiting the DNA Damage and Apoptosis in Rainbow Trout
inferred← citeshttps://doi.org/10.1007/s12013-023-01213-5openalex-snapshot
Glycolytic enzymes in non-glycolytic web: functional analysis of the key players
inferred← citeshttps://doi.org/10.1007/s12185-011-0964-yopenalex-snapshot
Apoptosis induced by ZnPcH1-based photodynamic therapy in Jurkat cells and HEL cells
inferred← citeshttps://doi.org/10.1007/s12192-011-0295-1openalex-snapshot
Phage display biopanning identifies the translation initiation and elongation factors (IF1α-3 and eIF-3) as components of Hsp70–peptide complexes in breast tumour cells
inferred← citeshttps://doi.org/10.1007/s12192-011-0307-1openalex-snapshot
Visualization and functional analysis of the oligomeric states of Escherichia coli heat shock protein 70 (Hsp70/DnaK)
inferred← citeshttps://doi.org/10.1007/s12192-013-0459-2openalex-snapshot
Stress-induced localization of HSPA6 (HSP70B′) and HSPA1A (HSP70-1) proteins to centrioles in human neuronal cells
inferred← citeshttps://doi.org/10.1007/s12192-015-0589-9openalex-snapshot
HSP70 inhibits stress-induced cardiomyocyte apoptosis by competitively binding to FAF1
inferred← citeshttps://doi.org/10.1007/s12192-015-0608-xopenalex-snapshot
Identification and expression analysis of a heat-shock protein 70 gene in Polycelis sp.
inferred← citeshttps://doi.org/10.1007/s12192-016-0676-6openalex-snapshot
The human HSP70 family of chaperones: where do we stand?
inferred← citeshttps://doi.org/10.1007/s12192-016-0752-yopenalex-snapshot
A disulfide-bonded DnaK dimer is maintained in an ATP-bound state
inferred← citeshttps://doi.org/10.1007/s12192-018-0900-7openalex-snapshot
Characterizing functional differences in sea anemone Hsp70 isoforms using budding yeast
inferred← citeshttps://doi.org/10.1007/s12192-020-01068-2openalex-snapshot
Autophagy and Hsp70 activation alleviate oral epithelial cell death induced by food-derived hypertonicity
inferred← citeshttps://doi.org/10.1007/s12192-020-01088-yopenalex-snapshot
Stress-induced changes in CARF expression determine cell fate to death, survival, or malignant transformation
inferred← citeshttps://doi.org/10.1007/s12192-023-01376-3openalex-snapshot
N-Acetylcysteine may exert hepatoprotective effect by regulating Meteorin-Like levels in Adriamycin-induced liver injury
inferred← citeshttps://doi.org/10.1007/s12355-024-01509-7openalex-snapshot
Genome-Wide Expression Profiling of Cytochrome P450 Genes in Response to the Oxidative Stress in Saccharum spp.
inferred← citeshttps://doi.org/10.1007/s13277-012-0585-yopenalex-snapshot
Apoptin selectively induces the apoptosis of tumor cells by suppressing the transcription of HSP70
inferred← citeshttps://doi.org/10.1007/s13311-013-0186-5openalex-snapshot
Opportunities and Challenges for Molecular Chaperone Modulation to Treat Protein-Conformational Brain Diseases
inferred← citeshttps://doi.org/10.1007/s13311-021-01114-6openalex-snapshot
Heat Shock Protein 70 as a Sex-Skewed Regulator of α-Synucleinopathy
inferred← citeshttps://doi.org/10.1007/s13562-024-00875-3openalex-snapshot
Identifying miRNAs and target genes associated with Allicin synthesis in Allium species
inferred← citeshttps://doi.org/10.1007/s40242-013-2193-9openalex-snapshot
Synthesis and characterization of pH-Responsive block copolymers with primary amine groups
inferred← citeshttps://doi.org/10.1007/s41666-023-00138-1openalex-snapshot
Clinical Feature Ranking Based on Ensemble Machine Learning Reveals Top Survival Factors for Glioblastoma Multiforme
inferred← citeshttps://doi.org/10.1007/s43538-024-00325-7openalex-snapshot
Conformational Dynamics of Hsp90 and Hsp70 Chaperones in Treating Neurodegenerative Diseases: Insights from the Drosophila Model
inferred← citeshttps://doi.org/10.1016/b978-0-08-099420-8.00004-3openalex-snapshot
Step IIIb: The Drug-Like Chemical Diversity Pool: Diverse and Targeted Compound Collections
inferred← citeshttps://doi.org/10.1016/b978-0-12-385883-2.00003-5openalex-snapshot
Protein Quality Control in Neurodegenerative Disease
inferred← citeshttps://doi.org/10.1016/b978-0-12-396521-9.00009-7openalex-snapshot
Exploiting Cancer Dependence on Molecular Chaperones
inferred← citeshttps://doi.org/10.1016/b978-0-12-397927-8.00015-4openalex-snapshot
HSP90 Inhibitors for Cancer Therapy and Overcoming Drug Resistance
inferred← citeshttps://doi.org/10.1016/b978-0-12-800186-8.00002-xopenalex-snapshot
Targeting the Protein Quality Control (PQC) Machinery
inferred← citeshttps://doi.org/10.1016/b978-0-12-801944-3.00002-3openalex-snapshot
Targeting the Protein Quality Control (PQC) Machinery
inferred← citeshttps://doi.org/10.1016/b978-0-12-817613-9.00009-2openalex-snapshot
Autocatakinesis systems in drug discovery
inferred← citeshttps://doi.org/10.1016/bs.apcsb.2026.06.010openalex-snapshot
Marine-derived molecular chaperones: Emerging therapeutic agents for neurodegenerative diseases
inferred← citeshttps://doi.org/10.1016/bs.irn.2016.03.001openalex-snapshot
Promoting Neuronal Tolerance of Diabetic Stress
inferred← citeshttps://doi.org/10.1016/j.antiviral.2017.08.005openalex-snapshot
An RNA polymerase II-driven Ebola virus minigenome system as an advanced tool for antiviral drug screening
inferred← citeshttps://doi.org/10.1016/j.apsb.2018.05.011openalex-snapshot
Gold nanorods together with HSP inhibitor-VER-155008 micelles for colon cancer mild-temperature photothermal therapy
inferred← citeshttps://doi.org/10.1016/j.apsb.2020.01.018openalex-snapshot
Modulation of protein fate decision by small molecules: targeting molecular chaperone machinery
inferred← citeshttps://doi.org/10.1016/j.bbagen.2019.129458openalex-snapshot
HSPA1A conformational mutants reveal a conserved structural unit in Hsp70 proteins
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2016.05.015openalex-snapshot
Ste20-like kinase, SLK, activates the heat shock factor 1 – Hsp70 pathway
inferred← citeshttps://doi.org/10.1016/j.bbapap.2018.09.001openalex-snapshot
Genetic analysis of Hsp70 phosphorylation sites reveals a role in Candida albicans cell and colony morphogenesis
inferred← citeshttps://doi.org/10.1016/j.bbr.2022.114204openalex-snapshot
Targeting α-synuclein post-translational modifications in Parkinson’s disease
inferred← citeshttps://doi.org/10.1016/j.bbrc.2012.07.088openalex-snapshot
MiR-30c: A novel regulator of salt tolerance in tilapia
inferred← citeshttps://doi.org/10.1016/j.bcmd.2016.04.011openalex-snapshot
Transgenic sickle cell trait mice do not exhibit abnormal thermoregulatory and stress responses to heat shock exposure
inferred← citeshttps://doi.org/10.1016/j.biomaterials.2013.12.077openalex-snapshot
Tumor-suppressive effect of a telomerase-derived peptide by inhibiting hypoxia-induced HIF-1α-VEGF signaling axis
inferred← citeshttps://doi.org/10.1016/j.biortech.2024.130355openalex-snapshot
Positive effect of phasin in biohydrogen production of non polyhydroxybutyrate-producing Clostridium acetobutylicum ATCC 824
inferred← citeshttps://doi.org/10.1016/j.bmc.2012.12.008openalex-snapshot
Binding partners for curcumin in human schwannoma cells: Biologic Implications
inferred← citeshttps://doi.org/10.1016/j.bmc.2020.115710openalex-snapshot
Analogs of nitrofuran antibiotics are potent GroEL/ES inhibitor pro-drugs
inferred← citeshttps://doi.org/10.1016/j.bmc.2026.118682openalex-snapshot
Discovery of Hsp70 inhibitors for allosteric dissociation of the Hsp70/BAG3 complex via structure-based de novo design
inferred← citeshttps://doi.org/10.1016/j.bmcl.2011.02.079openalex-snapshot
Improved synthesis of 15-deoxyspergualin analogs using the Ugi multi-component reaction
inferred← citeshttps://doi.org/10.1016/j.bmcl.2013.03.035openalex-snapshot
Structure-based design of HSPA5 inhibitors: From peptide to small molecule inhibitors
inferred← citeshttps://doi.org/10.1016/j.bmcl.2013.12.100openalex-snapshot
A biochemical screen for GroEL/GroES inhibitors
inferred← citeshttps://doi.org/10.1016/j.bmcl.2015.11.032openalex-snapshot
Mitochondrial drug targets in neurodegenerative diseases
inferred← citeshttps://doi.org/10.1016/j.bmcl.2019.04.034openalex-snapshot
Dual-targeting GroEL/ES chaperonin and protein tyrosine phosphatase B (PtpB) inhibitors: A polypharmacology strategy for treating Mycobacterium tuberculosis infections
inferred← citeshttps://doi.org/10.1016/j.bmcl.2020.126954openalex-snapshot
Neutral analogs of the heat shock protein 70 (Hsp70) inhibitor, JG-98
inferred← citeshttps://doi.org/10.1016/j.bmcl.2025.130401openalex-snapshot
Design, synthesis, and anticancer evaluation of benzimidazole and benzothiazole derivatives targeting Hsp70 and FoxM1
inferred← citeshttps://doi.org/10.1016/j.canlet.2011.08.019openalex-snapshot
Human DNAJ in cancer and stem cells
inferred← citeshttps://doi.org/10.1016/j.canlet.2011.09.043openalex-snapshot
Targeting heat shock factor 1 with a triazole nucleoside analog to elicit potent anticancer activity on drug-resistant pancreatic cancer
inferred← citeshttps://doi.org/10.1016/j.canlet.2013.07.023openalex-snapshot
Hsp70 inhibition induces myeloma cell death via the intracellular accumulation of immunoglobulin and the generation of proteotoxic stress
inferred← citeshttps://doi.org/10.1016/j.celrep.2021.108726openalex-snapshot
Gain-of-function p53 protein transferred via small extracellular vesicles promotes conversion of fibroblasts to a cancer-associated phenotype
inferred← citeshttps://doi.org/10.1016/j.chembiol.2010.12.010openalex-snapshot
Chemical Screens against a Reconstituted Multiprotein Complex: Myricetin Blocks DnaJ Regulation of DnaK through an Allosteric Mechanism
inferred← citeshttps://doi.org/10.1016/j.chembiol.2012.07.026openalex-snapshot
Cysteine Reactivity Distinguishes Redox Sensing by the Heat-Inducible and Constitutive Forms of Heat Shock Protein 70
inferred← citeshttps://doi.org/10.1016/j.chembiol.2014.10.016openalex-snapshot
Identification of an Allosteric Small-Molecule Inhibitor Selective for the Inducible Form of Heat Shock Protein 70
inferred← citeshttps://doi.org/10.1016/j.chembiol.2015.02.004openalex-snapshot
A Small Molecule Inhibitor of ATPase Activity of HSP70 Induces Apoptosis and Has Antitumor Activities
inferred← citeshttps://doi.org/10.1016/j.chembiol.2016.04.014openalex-snapshot
Stabilizing the Hsp70-Tau Complex Promotes Turnover in Models of Tauopathy
inferred← citeshttps://doi.org/10.1016/j.chembiol.2018.06.010openalex-snapshot
Subcellular Hsp70 Inhibitors Promote Cancer Cell Death via Different Mechanisms
inferred← citeshttps://doi.org/10.1016/j.chembiol.2018.10.004openalex-snapshot
When Small Molecules Are Like Real Estate: It’s All about Location, Location, Location
inferred← citeshttps://doi.org/10.1016/j.chembiol.2021.11.004openalex-snapshot
An allosteric inhibitor of bacterial Hsp70 chaperone potentiates antibiotics and mitigates resistance
inferred← citeshttps://doi.org/10.1016/j.chembiol.2022.06.006openalex-snapshot
A campaign targeting a conserved Hsp70 binding site uncovers how subcellular localization is linked to distinct biological activities
inferred← citeshttps://doi.org/10.1016/j.compbiolchem.2017.05.011openalex-snapshot
Pharmacophore modeling, virtual screening and molecular docking of ATPase inhibitors of HSP70
inferred← citeshttps://doi.org/10.1016/j.csag.2025.100082openalex-snapshot
The impacts of climate change on livestock: An interdisciplinary, scoping review of health, production, and adaptation strategies
inferred← citeshttps://doi.org/10.1016/j.cstres.2024.02.002openalex-snapshot
The dance of proteostasis and metabolism: Unveiling the caloristatic controlling switch
inferred← citeshttps://doi.org/10.1016/j.drudis.2011.09.016openalex-snapshot
Targeting heat shock response pathways to treat pancreatic cancer
inferred← citeshttps://doi.org/10.1016/j.ejcb.2018.01.001openalex-snapshot
Understanding organellar protein folding capacities and assessing their pharmacological modulation by small molecules
inferred← citeshttps://doi.org/10.1016/j.ejmech.2020.112762openalex-snapshot
2-substituted benzothiazoles as antiproliferative agents: Novel insights on structure-activity relationships
inferred← citeshttps://doi.org/10.1016/j.ejmech.2025.118188openalex-snapshot
Potential next generation targets for antibacterial agent's discovery and development
inferred← citeshttps://doi.org/10.1016/j.expneurol.2025.115284openalex-snapshot
Heat shock proteins in cerebral ischemia-reperfusion injury: Mechanisms and therapeutic implications
inferred← citeshttps://doi.org/10.1016/j.fct.2013.12.024openalex-snapshot
Ferulic acid: Pharmacological and toxicological aspects
inferred← citeshttps://doi.org/10.1016/j.fct.2017.02.028openalex-snapshot
New insights into the ameliorative effects of ferulic acid in pathophysiological conditions
inferred← citeshttps://doi.org/10.1016/j.fob.2015.09.001openalex-snapshot
Decreasing or increasing heat shock protein 72 exacerbates or attenuates heat‐induced cell death, respectively, in rat hypothalamic cells
inferred← citeshttps://doi.org/10.1016/j.fochms.2020.100001openalex-snapshot
Differentially expressed marker genes and glycogen levels in pectoralis major of Ross308 broilers with wooden breast syndrome indicates stress, inflammation and hypoxic conditions
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2012.01.004openalex-snapshot
Geranylgeranylacetone protects mice against morphine-induced hyperlocomotion, rewarding effect, and withdrawal syndrome
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2014.08.012openalex-snapshot
Regulation of protein turnover by heat shock proteins
inferred← citeshttps://doi.org/10.1016/j.fsirep.2022.100079openalex-snapshot
Effects of elevated temperature on 8-OHdG expression in the American oyster (Crassostrea virginica): Induction of oxidative stress biomarkers, cellular apoptosis, DNA damage and γH2AX signaling pathways
inferred← citeshttps://doi.org/10.1016/j.genrep.2016.09.003openalex-snapshot
Computational study of some amoebicidal phytochemicals against heat shock protein of Naegleria fowleri
inferred← citeshttps://doi.org/10.1016/j.heliyon.2021.e08070openalex-snapshot
Short and long-term effect of reproduction on mitochondrial dynamics and autophagy in rats
inferred← citeshttps://doi.org/10.1016/j.heliyon.2025.e42487openalex-snapshot
Immunoproteomic approach identifies a putative virulence chaperone DnaK protein as a candidate diagnostic marker and therapeutic target for Pythium insidiosum infection
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2017.02.004openalex-snapshot
The dissociation of the Hsp60/pro-Caspase-3 complex by bis(pyridyl)oxadiazole copper complex ( CubipyOXA ) leads to cell death in NCI-H292 cancer cells
inferred← citeshttps://doi.org/10.1016/j.jmb.2011.07.001openalex-snapshot
The Four Hydrophobic Residues on the Hsp70 Inter-Domain Linker Have Two Distinct Roles
inferred← citeshttps://doi.org/10.1016/j.jmb.2015.04.010openalex-snapshot
Mutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions
inferred← citeshttps://doi.org/10.1016/j.jobcr.2022.07.009openalex-snapshot
Expression and bioinformatics analyses show HSP70 complements BCL2 action in oral carcinogenesis
inferred← citeshttps://doi.org/10.1016/j.jprot.2013.01.030openalex-snapshot
Chemical proteomics reveals HSP70 1A as a target for the anticancer diterpene oridonin in Jurkat cells
inferred← citeshttps://doi.org/10.1016/j.jprot.2015.05.037openalex-snapshot
Quantitative proteomic analysis of paired colorectal cancer and non-tumorigenic tissues reveals signature proteins and perturbed pathways involved in CRC progression and metastasis
inferred← citeshttps://doi.org/10.1016/j.jprot.2016.06.019openalex-snapshot
Determination of the interactome of non-structural protein12 from highly pathogenic porcine reproductive and respiratory syndrome virus with host cellular proteins using high throughput proteomics and identification of HSP70 as a cellular factor for virus replication
inferred← citeshttps://doi.org/10.1016/j.jprot.2024.105087openalex-snapshot
Proteomic analysis of the mucus of the photosynthetic sea slug Elysia crispata
inferred← citeshttps://doi.org/10.1016/j.jss.2010.09.040openalex-snapshot
Heat Shock Protein 70 Expression Following Hepatic Radiofrequency Ablation is Affected by Adjacent Vasculature
inferred← citeshttps://doi.org/10.1016/j.jtherbio.2025.104236openalex-snapshot
Effects of heat stress on plasminogen activator related in milk protein in bovine mammary epithelial cells and mid lactating Holstein cow milk
inferred← citeshttps://doi.org/10.1016/j.lfs.2025.123563openalex-snapshot
Critical role of microRNAs in cellular quality control during brain aging and neurological disorders: Interplay between autophagy and proteostasis
inferred← citeshttps://doi.org/10.1016/j.marpolbul.2018.07.066openalex-snapshot
Highly polluted life history and acute heat stress, a hazardous mix for blue mussels
inferred← citeshttps://doi.org/10.1016/j.microb.2024.100151openalex-snapshot
A comprehensive review on latent role of stress proteins in antibiotic resistance
inferred← citeshttps://doi.org/10.1016/j.neuint.2017.08.013openalex-snapshot
Alterations in the E3 ligases Parkin and CHIP result in unique metabolic signaling defects and mitochondrial quality control issues
inferred← citeshttps://doi.org/10.1016/j.npep.2013.06.002openalex-snapshot
Amyloid-β25–35 induces a permanent phosphorylation of HSF-1, but a transitory and inflammation-independent overexpression of Hsp-70 in C6 astrocytoma cells
inferred← citeshttps://doi.org/10.1016/j.npep.2014.04.006openalex-snapshot
17-AAG improves cognitive process and increases heat shock protein response in a model lesion with Aβ25–35
inferred← citeshttps://doi.org/10.1016/j.nutres.2024.01.014openalex-snapshot
Ginger alleviates mechanical hypersensitivity and anxio-depressive behavior in rats with diabetic neuropathy through beneficial actions on gut microbiome composition, mitochondria, and neuroimmune cells of colon and spinal cord
inferred← citeshttps://doi.org/10.1016/j.pharmthera.2020.107684openalex-snapshot
The role of the brain renin-angiotensin system (RAS) in mild traumatic brain injury (TBI)
inferred← citeshttps://doi.org/10.1016/j.phrs.2022.106173openalex-snapshot
New insights into the role and therapeutic potential of HSP70 in diabetes
inferred← citeshttps://doi.org/10.1016/j.plantsci.2014.12.012openalex-snapshot
Erianthus arundinaceus HSP70 (EaHSP70) overexpression increases drought and salinity tolerance in sugarcane (Saccharum spp. hybrid)
inferred← citeshttps://doi.org/10.1016/j.plaphy.2024.109226openalex-snapshot
HIP is involved in NaCl and endoplasmic reticulum stress resistance in Arabidopsis
inferred← citeshttps://doi.org/10.1016/j.procbio.2020.12.016openalex-snapshot
Cloning, prokaryotic expression, and functional characterization of a novel 70-kDa heat shock protein (DnaK) from Bacillus persicus
inferred← citeshttps://doi.org/10.1016/j.psj.2025.106290openalex-snapshot
Establishing an experimental challenge model in broiler chickens exposed to multiple mild stressors of cyclic elevated ambient temperature, feed withdrawal, and coccidiosis infection
inferred← citeshttps://doi.org/10.1016/j.rvsc.2023.105057openalex-snapshot
Review: The role of heat shock proteins in chicken: Insights into stress adaptation and health
inferred← citeshttps://doi.org/10.1016/j.talo.2023.100265openalex-snapshot
Intracellular metal enhanced fluorescence utilizing gold nanoparticles embedded in hydrogel droplets for sensitive protein detection in cells
inferred← citeshttps://doi.org/10.1016/j.tips.2011.11.001openalex-snapshot
Heat shock response and insulin-associated neurodegeneration
inferred← citeshttps://doi.org/10.1016/j.virol.2021.08.002openalex-snapshot
Targeting conserved co-opted host factors to block virus replication: Using allosteric inhibitors of the cytosolic Hsp70s to interfere with tomato bushy stunt virus replication
inferred← citeshttps://doi.org/10.1016/j.vpoa.2019.100014openalex-snapshot
Trypanosoma vivax infection in sheep: Different patterns of virulence and pathogenicity associated with differentially expressed proteomes
inferred← citeshttps://doi.org/10.1016/j.yexcr.2024.114393openalex-snapshot
The effect of cancer cell-derived exosomal proteins on macrophage polarization: An in-depth review
inferred← citeshttps://doi.org/10.1016/j.yexmp.2012.09.001openalex-snapshot
HSP27 expression in primary colorectal cancers is dependent on mutation of KRAS and PI3K/AKT activation status and is independent of TP53
inferred← citeshttps://doi.org/10.1016/j.ygyno.2012.04.048openalex-snapshot
Green tea for ovarian cancer prevention and treatment: A systematic review of the in vitro, in vivo and epidemiological studies
inferred← citeshttps://doi.org/10.1017/erm.2012.10openalex-snapshot
Features of protein–protein interactions that translate into potent inhibitors: topology, surface area and affinity
inferred← citeshttps://doi.org/10.1021/acs.accounts.8b00036openalex-snapshot
Protein–Protein Interactions in the Molecular Chaperone Network
inferred← citeshttps://doi.org/10.1021/acs.biochem.5b00459openalex-snapshot
A Rational Design Strategy for the Selective Activity Enhancement of a Molecular Chaperone toward a Target Substrate
inferred← citeshttps://doi.org/10.1021/acs.bioconjchem.6b00305openalex-snapshot
Identification of Targets of the HIF-1 Inhibitor IDF-11774 Using Alkyne-Conjugated Photoaffinity Probes
inferred← citeshttps://doi.org/10.1021/acs.jcim.5b00755openalex-snapshot
Probing Allosteric Inhibition Mechanisms of the Hsp70 Chaperone Proteins Using Molecular Dynamics Simulations and Analysis of the Residue Interaction Networks
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.1c01342openalex-snapshot
Inhibitor Combinations Reveal Wiring of the Proteostasis Network in Prostate Cancer Cells
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.1c01897openalex-snapshot
Proteostasis Regulators in Cystic Fibrosis: Current Development and Future Perspectives
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.6b01613openalex-snapshot
Ugi Reaction-Derived α-Acyl Aminocarboxamides Bind to Phosphatidylinositol 3-Kinase-Related Kinases, Inhibit HSF1-Dependent Heat Shock Response, and Induce Apoptosis in Multiple Myeloma Cells
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.8b00583openalex-snapshot
Exploration of Benzothiazole Rhodacyanines as Allosteric Inhibitors of Protein–Protein Interactions with Heat Shock Protein 70 (Hsp70)
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.8b00989openalex-snapshot
Sulfonamido-2-arylbenzoxazole GroEL/ES Inhibitors as Potent Antibacterials against Methicillin-Resistant Staphylococcus aureus (MRSA)
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.8b01293openalex-snapshot
Hydroxybiphenylamide GroEL/ES Inhibitors Are Potent Antibacterials against Planktonic and Biofilm Forms of Staphylococcus aureus
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.9b01400openalex-snapshot
α‑Synuclein Dimers as Potent Inhibitors of Fibrillization
inferred← citeshttps://doi.org/10.1021/acscentsci.9b00467openalex-snapshot
Enhancement of the Anti-Aggregation Activity of a Molecular Chaperone Using a Rationally Designed Post-Translational Modification
inferred← citeshttps://doi.org/10.1021/acschembio.3c00589openalex-snapshot
Combined In-Solution Fragment Screening and Crystallographic Binding-Mode Analysis with a Two-Domain Hsp70 Construct
inferred← citeshttps://doi.org/10.1021/acschembio.5b00740openalex-snapshot
Transportable, Chemical Genetic Methodology for the Small Molecule-Mediated Inhibition of Heat Shock Factor 1
inferred← citeshttps://doi.org/10.1021/acschembio.8b00712openalex-snapshot
A Local Allosteric Network in Heat Shock Protein 70 (Hsp70) Links Inhibitor Binding to Enzyme Activity and Distal Protein–Protein Interactions
inferred← citeshttps://doi.org/10.1021/acschemneuro.5b00165openalex-snapshot
Modulating Molecular Chaperones Improves Mitochondrial Bioenergetics and Decreases the Inflammatory Transcriptome in Diabetic Sensory Neurons
inferred← citeshttps://doi.org/10.1021/acschemneuro.9b00105openalex-snapshot
HSP90 Inhibitor, NVP-AUY922, Improves Myelination in Vitro and Supports the Maintenance of Myelinated Axons in Neuropathic Mice
inferred← citeshttps://doi.org/10.1021/acsinfecdis.7b00231openalex-snapshot
Targeting the Proteostasis Network for Mycobacterial Drug Discovery
inferred← citeshttps://doi.org/10.1021/acsnano.6b03874openalex-snapshot
Selectively Sensitizing Malignant Cells to Photothermal Therapy Using a CD44-Targeting Heat Shock Protein 72 Depletion Nanosystem
inferred← citeshttps://doi.org/10.1021/acsomega.5c05832openalex-snapshot
Unraveling the Molecular Inhibition and Conformational Changes of Hsp70 and Hsc70 Induced by VER-155008, a Competitive ATPase Inhibitor through Molecular Dynamics Simulations and Principal Component Analysis
inferred← citeshttps://doi.org/10.1021/bi2018078openalex-snapshot
Hsp70 Alters Tau Function and Aggregation in an Isoform Specific Manner
inferred← citeshttps://doi.org/10.1021/bi500004qopenalex-snapshot
Conformational Changes in Human Hsp70 Induced by High Hydrostatic Pressure Produce Oligomers with ATPase Activity but without Chaperone Activity
inferred← citeshttps://doi.org/10.1021/cb100105copenalex-snapshot
Natural Products as Chemical Probes
inferred← citeshttps://doi.org/10.1021/cb200308eopenalex-snapshot
Caught in the Act: Covalent Cross-Linking Captures Activator–Coactivator Interactions in Vivo
inferred← citeshttps://doi.org/10.1021/cb300166popenalex-snapshot
Pharmacological Tuning of Heat Shock Protein 70 Modulates Polyglutamine Toxicity and Aggregation
inferred← citeshttps://doi.org/10.1021/cb500256uopenalex-snapshot
Affinity Purification Probes of Potential Use To Investigate the Endogenous Hsp70 Interactome in Cancer
inferred← citeshttps://doi.org/10.1021/cn300210gopenalex-snapshot
Synthesis and Initial Evaluation of YM-08, a Blood-Brain Barrier Permeable Derivative of the Heat Shock Protein 70 (Hsp70) Inhibitor MKT-077, Which Reduces Tau Levels
inferred← citeshttps://doi.org/10.1021/jacsau.6c00173openalex-snapshot
ProMol_Func: A Structure-Free Deep Learning Model for Virtual Screening
inferred← citeshttps://doi.org/10.1021/jm100342zopenalex-snapshot
ATPases as Drug Targets: Insights from Heat Shock Proteins 70 and 90
inferred← citeshttps://doi.org/10.1021/jm3015926openalex-snapshot
Target- and Mechanism-Based Therapeutics for Neurodegenerative Diseases: Strength in Numbers
inferred← citeshttps://doi.org/10.1021/jm401551nopenalex-snapshot
Heat Shock Protein 70 Inhibitors. 1. 2,5′-Thiodipyrimidine and 5-(Phenylthio)pyrimidine Acrylamides as Irreversible Binders to an Allosteric Site on Heat Shock Protein 70
inferred← citeshttps://doi.org/10.1021/jm401552yopenalex-snapshot
Heat Shock Protein 70 Inhibitors. 2. 2,5′-Thiodipyrimidines, 5-(Phenylthio)pyrimidines, 2-(Pyridin-3-ylthio)pyrimidines, and 3-(Phenylthio)pyridines as Reversible Binders to an Allosteric Site on Heat Shock Protein 70
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