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Chaperone function and mechanism of small heat-shock proteins
131/131 checkable references clean · checked 2026-07-24
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
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The 131 checked references that resolve
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Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA
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<i>Synechocystis</i>
HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding
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Hsp12 Is an Intrinsically Unstructured Stress Protein that Folds upon Membrane Association and Modulates Membrane Function
resolves10.1074/jbc.273.18.11032
The Small Heat-shock Protein IbpB from Escherichia coli Stabilizes Stress-denatured Proteins for Subsequent Refolding by a Multichaperone Network
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Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation
resolves10.1093/emboj/16.3.659
A small heat shock protein stably binds heat‐denatured model substrates and can maintain a substrate in a folding‐competent state
resolves10.1093/emboj/16.2.221
Binding of non‐native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
resolves10.1074/jbc.M710400200
A Mutant Small Heat Shock Protein with Increased Thylakoid Association Provides an Elevated Resistance Against UV-B Damage in Synechocystis 6803
resolves10.1007/s00299-012-1262-8
ZmHSP16.9, a cytosolic class I small heat shock protein in maize (Zea mays), confers heat tolerance in transgenic tobacco
resolves10.1007/s00294-007-0140-3
The heterologous overexpression of hsp23, a small heat-shock protein gene from Trichoderma virens, confers thermotolerance to T. harzianum
resolves10.1007/s10529-011-0769-3
Overexpression of a chloroplast-localized small heat shock protein OsHSP26 confers enhanced tolerance against oxidative and heat stresses in tall fescue
resolves10.1016/j.bbrc.2005.12.086
The intertidal copepod Tigriopus japonicus small heat shock protein 20 gene (Hsp20) enhances thermotolerance of transformed Escherichia coli
resolves10.1073/pnas.94.20.10967
Expression of a gene encoding a 16.9-kDa heat-shock protein, Oshsp16.9, in
<i>Escherichia coli</i>
enhances thermotolerance
resolves10.1111/j.1574-6968.2000.tb09009.x
Small heat shock proteins, IbpA and IbpB, are involved in resistances to heat and superoxide stresses in<i>Escherichia coli</i>
resolves10.1083/jcb.109.1.7
Heat shock resistance conferred by expression of the human HSP27 gene in rodent cells.
resolves10.1038/sj.cdd.4400847
Overexpression of murine small heat shock protein HSP25 interferes with chondrocyte differentiation and decreases cell adhesion
resolves10.1152/ajplung.00453.2006
Overexpression of human Hsp27 inhibits serum-induced proliferation in airway smooth muscle myocytes and confers resistance to hydrogen peroxide cytotoxicity
resolves10.1074/jbc.C400357200
Decreased Lifespan in the Absence of Expression of the Mitochondrial Small Heat Shock Protein Hsp22 in Drosophila
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Overexpression of Wild-Type Heat Shock Protein 27 and a Nonphosphorylatable Heat Shock Protein 27 Mutant Protects Against Ischemia/Reperfusion Injury in a Transgenic Mouse Model
resolves10.1074/jbc.M112.368324
Phenotype of Cardiomyopathy in Cardiac-specific Heat Shock Protein B8 K141N Transgenic Mouse
resolves10.1093/hmg/7.3.471
Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA
resolves10.1038/1765
A missense mutation in the αB-crystallin chaperone gene causes a desmin-related myopathy
resolves10.1038/ng1328
Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy
resolves10.1038/ng1354
Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy
resolves10.1038/nsb722
resolves10.1074/jbc.M406319200
A Dual Role for the N-terminal Region of Mycobacterium tuberculosis Hsp16.3 in Self-oligomerization and Binding Denaturing Substrate Proteins
resolves10.1074/jbc.M802946200
Insights into Small Heat Shock Protein and Substrate Structure during Chaperone Action Derived from Hydrogen/Deuterium Exchange and Mass Spectrometry
resolves10.1016/S0167-4838(97)00145-3
A spectroscopic study of glycated bovine α-crystallin: investigation of flexibility of the C-terminal extension, chaperone activity and evidence for diglycation
resolves10.1016/S0141-8130(98)00017-8
NMR spectroscopy of α-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins
resolves10.1016/j.tibs.2011.11.005
Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions
resolves10.1016/j.jmb.2012.05.017
Structural Studies on the Oligomeric Transition of a Small Heat Shock Protein, StHsp14.0
resolves10.1016/j.str.2012.11.015
Nonequivalence Observed for the 16-Meric Structure of a Small Heat Shock Protein, SpHsp16.0, from Schizosaccharomyces pombe
resolves10.1016/S0014-5793(98)00917-X
<i>Caenorhabditis elegans</i> small heat‐shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone‐like activity
resolves10.1016/j.jmb.2013.02.011
An Unusual Dimeric Small Heat Shock Protein Provides Insight into the Mechanism of This Class of Chaperones
resolves10.1074/jbc.272.19.12847
Unique Structural Features of a Novel Class of Small Heat Shock Proteins
resolves10.1074/jbc.271.12.7218
Mycobacterium tuberculosis 16-kDa Antigen (Hsp16.3) Functions as an Oligomeric Structure in Vitro to Suppress Thermal Aggregation
resolves10.1110/ps.8.1.174
The <i>mycobacterium tuberculosis</i> small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: Conformational flexibility and molecular chaperone activity
resolves10.1016/S0022-2836(02)00311-X
Monodisperse Hsp16.3 Nonamer Exhibits Dynamic Dissociation and Reassociation, with the Nonamer Dissociation Prerequisite for Chaperone-like Activity
resolves10.1016/j.jmb.2005.01.029
The Essential Role of the Flexible Termini in the Temperature-responsiveness of the Oligomeric State and Chaperone-like Activity for the Polydisperse Small Heat Shock Protein IbpB from Escherichia coli
resolves10.1042/BJ20071120
The dramatically increased chaperone activity of small heat-shock protein IbpB is retained for an extended period of time after the stress condition is removed
resolves10.1016/j.bbrc.2005.07.065
Small heat-shock proteins function in the insoluble protein complex
resolves10.1074/jbc.M113.501817
In Vivo Substrate Diversity and Preference of Small Heat Shock Protein IbpB as Revealed by Using a Genetically Incorporated Photo-cross-linker
resolves10.1074/jbc.M113.450437
Small Heat Shock Protein IbpB Acts as a Robust Chaperone in Living Cells by Hierarchically Activating Its Multi-type Substrate-binding Residues
resolves10.1016/S0923-2508(98)80301-X
The 16-kDa α-crystallin-like protein of Mycobacterium bovis BCG is produced under conditions of oxygen deficiency and is associated with ribosomes
resolves10.2174/138920312799277875
The Role of Intrinsically Disordered Regions in the Structure and Functioning of Small Heat Shock Proteins
resolves10.1128/MMBR.66.1.64-93.2002
α-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone Network
resolves10.1016/j.cellsig.2013.07.027
The potential role of small heat shock proteins in mitochondria
resolves10.1016/S0021-9258(18)54039-4
Structural and functional similarities of bovine alpha-crystallin and mouse small heat-shock protein. A family of chaperones.
resolves10.1073/pnas.0914773107
Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation
resolves10.1371/journal.pbio.1001346
Small Heat Shock Proteins Potentiate Amyloid Dissolution by Protein Disaggregases from Yeast and Humans
resolves10.1016/j.jbiosc.2012.08.001
Small heat shock protein AgsA: An effective stabilizer of enzyme activities
resolves10.1074/jbc.271.18.10449
Conformational Properties of Substrate Proteins Bound to a Molecular Chaperone α-Crystallin
resolves10.1016/S0014-5793(02)02884-3
Suppression of DTT‐induced aggregation of abrin by αA‐ and αB‐crystallins: a model aggregation assay for α‐crystallin chaperone activity in vitro<sup>1</sup>
resolves10.1074/jbc.272.39.24646
Structure-Function Studies on Small Heat Shock Protein Oligomeric Assembly and Interaction with Unfolded Polypeptides
resolves10.1074/jbc.273.16.9415
Interactions of Chaperone α-Crystallin with the Molten Globule State of Xylose Reductase
resolves10.1016/S0022-2836(02)00144-4
The Interaction of the Molecular Chaperone α-Crystallin with Unfolding α-Lactalbumin: A Structural and Kinetic Spectroscopic Study
resolves10.1016/S0167-4838(00)00109-6
The small heat-shock chaperone protein, α-crystallin, does not recognise stable molten globule states of cytosolic proteins
resolves10.1074/jbc.272.44.27722
The Interaction of the Molecular Chaperone, α-Crystallin, with Molten Globule States of Bovine α-Lactalbumin
resolves10.1074/jbc.274.47.33209
Insight into the Secondary Structure of Non-native Proteins Bound to a Molecular Chaperone α-Crystallin
resolves10.1042/bj3540079
The molecular chaperone α-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of α-lactalbumin
resolves10.1074/jbc.M310684200
The Identity of Proteins Associated with a Small Heat Shock Protein during Heat Stress in Vivo Indicates That These Chaperones Protect a Wide Range of Cellular Functions
resolves10.1038/nature03239
Interaction network containing conserved and essential protein complexes in Escherichia coli
resolves10.1139/G07-114
The recent evolution of a pseudogene: diversity and divergence of a mitochondria-localized small heat shock protein in<i>Arabidopsis thaliana</i>
resolves10.1073/pnas.96.25.14394
Chloroplast small heat shock proteins: Evidence for atypical evolution of an organelle-localized protein
resolves10.1016/j.biocel.2012.03.009
Small heat shock protein expression and functions during development
resolves10.1016/S0022-2836(03)00018-4
Mycobacterium tuberculosis Hsp16.3 Nonamers are Assembled and Re-assembled via Trimer and Hexamer Intermediates
resolves10.1093/bioinformatics/16.11.1023
Biochemical systems analysis of genome-wide expression data
resolves10.1073/pnas.95.3.1004
ATP-enhanced molecular chaperone functions of the small heat shock protein human αB crystallin
resolves10.1104/pp.120.2.521
Heterologous Expression of a Plant Small Heat-Shock Protein Enhances <i>Escherichia coli</i>Viability under Heat and Cold Stress1
resolves10.18388/abp.2009_2516
Role of Escherichia coli heat shock proteins IbpA and IbpB in protection of alcohol dehydrogenase AdhE against heat inactivation in the presence of oxygen.
resolves10.1099/00221287-148-6-1757
The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock
resolves10.1016/j.chembiol.2012.04.007
Dissecting Heterogeneous Molecular Chaperone Complexes Using a Mass Spectrum Deconvolution Approach
resolves10.1074/jbc.M311104200
Interactions between Small Heat Shock Protein Subunits and Substrate in Small Heat Shock Protein-Substrate Complexes
resolves10.1073/pnas.0910126107
Quaternary dynamics and plasticity underlie small heat shock protein chaperone function
resolves10.1007/BF01674432
Comparison of the homologous carboxy-terminal domain and tail of α-crystallin and small heat shock protein
resolves10.1074/jbc.M607677200
The N-terminal Arm of Small Heat Shock Proteins Is Important for Both Chaperone Activity and Substrate Specificity
resolves10.1021/bi061471m
N- and C-Terminal Motifs in Human αB Crystallin Play an Important Role in the Recognition, Selection, and Solubilization of Substrates
resolves10.1074/jbc.M111.273847
Importance of N- and C-terminal Regions of IbpA, Escherichia coli Small Heat Shock Protein, for Chaperone Function and Oligomerization
resolves10.1046/j.1432-1033.2002.03049.x
A critical motif for oligomerization and chaperone activity of bacterial α‐heat shock proteins
resolves10.1016/j.bbrc.2006.08.036
Identification of bis-ANS binding sites in Mycobacterium tuberculosis small heat shock protein Hsp16.3: Evidences for a two-step substrate-binding mechanism
resolves10.1007/s12192-012-0360-4
Probing the transient interaction between the small heat-shock protein Hsp21 and a model substrate protein using crosslinking mass spectrometry
resolves10.1016/j.abb.2011.06.014
Biochemical characterization of small heat shock protein HspB8 (Hsp22)–Bag3 interaction
resolves10.1006/bbrc.1997.7460
Functional Elements in Molecular Chaperone α-Crystallin: Identification of Binding Sites in αB-Crystallin
resolves10.1074/jbc.273.25.15474
Identification of 1,1′-Bi(4-anilino)naphthalene-5,5′-disulfonic Acid Binding Sequences in α-Crystallin
resolves10.1134/S0006297906130141
Identification of a highly conserved pro-gly doublet in non-animal small heat shock proteins and characterization of its structural and functional roles in Mycobacterium tuberculosis Hsp 16.3
resolves10.1074/jbc.M404455200
Mutants in a Small Heat Shock Protein That Affect the Oligomeric State
resolves10.1016/S0022-2836(03)00356-5
Structural and Functional Defects Caused by Point Mutations in the α-Crystallin Domain of a Bacterial α-Heat Shock Protein
resolves10.1002/prot.21762
Role of the IXI/V motif in oligomer assembly and function of StHsp14.0, a small heat shock protein from the acidothermophilic archaeon, <i>Sulfolobus tokodaii</i> strain 7
resolves10.1371/journal.pone.0001046
Site-Directed Mutations in the C-Terminal Extension of Human αB-Crystallin Affect Chaperone Function and Block Amyloid Fibril Formation
resolves10.1074/jbc.M109211200
The R116C Mutation in αA-crystallin Diminishes Its Protective Ability against Stress-induced Lens Epithelial Cell Apoptosis
resolves10.1074/jbc.274.34.24137
Structural and Functional Consequences of the Mutation of a Conserved Arginine Residue in αA and αB Crystallins
resolves10.1073/pnas.0401900101
Desmin-related cardiomyopathy in transgenic mice: A cardiac amyloidosis
resolves10.1073/pnas.0902177106
Substrate binding site flexibility of the small heat shock protein molecular chaperones
resolves10.1073/pnas.172226299
Addition of a photocrosslinking amino acid to the genetic code of
<i>Escherichia</i>
<i>coli</i>
resolves10.1074/jbc.271.45.28558
Effects of Site-directed Mutations on the Chaperone-like Activity of αB-Crystallin
resolves10.1111/j.1432-1033.1995.834zz.x
The Mutation Asp69→Ser Affects the Chaperone‐Like Activity of αA‐Crystallin
resolves10.1074/jbc.M303587200
Refolding of Substrates Bound to Small Hsps Relies on a Disaggregation Reaction Mediated Most Efficiently by ClpB/DnaK
resolves10.1016/j.bbrc.2004.02.053
Temperature-dependent subunit exchange and chaperone-like activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis
resolves10.1074/jbc.M205594200
Subunit Exchange, Conformational Stability, and Chaperone-like Function of the Small Heat Shock Protein 16.5 fromMethanococcus jannaschii
resolves10.1016/j.jmb.2005.05.034
The Activation Mechanism of Hsp26 does not Require Dissociation of the Oligomer
resolves10.1016/j.molcel.2007.11.025
Activation of the Chaperone Hsp26 Is Controlled by the Rearrangement of Its Thermosensor Domain
resolves10.1074/jbc.M109.074088
Mechanistic Differences between Two Conserved Classes of Small Heat Shock Proteins Found in the Plant Cytosol
resolves10.1074/jbc.272.38.23559
Chaperone-like Activity and Temperature-induced Structural Changes of α-Crystallin
resolves10.1046/j.1432-1033.2003.03928.x
Some properties of human small heat shock protein Hsp20 (HspB6)
resolves10.1161/CIRCULATIONAHA.110.013847
H11 Kinase/Heat Shock Protein 22 Deletion Impairs Both Nuclear and Mitochondrial Functions of STAT3 and Accelerates the Transition Into Heart Failure on Cardiac Overload
resolves10.1073/pnas.1308898110
Regulated structural transitions unleash the chaperone activity of αB-crystallin
The 3 references without a DOI — listed, not checked
no DOI — not checkedde Jong WW, Leunissen JA, Voorter CE. Evolution of the alpha-crystallin/small heat-shock protein family. Mol Biol Evol, 1993, 10: 103-126.
no DOI — not checkedRichards EH, Hickey E, Weber L, Master JR. Effect of overexpression of the small heat shock protein HSP27 on the heat and drug sensitivities of human testis tumor cells. Cancer Res, 1996, 56: 2446-2451.
no DOI — not checkedLee SY EcoProDB databases. (http://eecoli.kaist.ac.kr/main.html) 2013.
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