On the public citation graph

Protein folding in the cell

https://doi.org/10.1038/355033a0
0 signed · 4166 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/j.1460-2075.1985.tb03806.xopenalex-snapshot
SV40 T antigen and the exocytotic pathway.
inferredcites →https://doi.org/10.1002/j.1460-2075.1985.tb03837.xopenalex-snapshot
Actin gene mutations in Drosophila; heat shock activation in the indirect flight muscles
inferredcites →https://doi.org/10.1002/j.1460-2075.1985.tb04056.xopenalex-snapshot
Involvement of ATP in the nuclear and nucleolar functions of the 70 kd heat shock protein.
inferredcites →https://doi.org/10.1002/j.1460-2075.1987.tb04843.xopenalex-snapshot
Complementary DNA for human T‐cell cyclophilin.
inferredcites →https://doi.org/10.1002/j.1460-2075.1988.tb02923.xopenalex-snapshot
Unfolding and refolding of a purified precursor protein during import into isolated mitochondria.
inferredcites →https://doi.org/10.1002/j.1460-2075.1988.tb03144.xopenalex-snapshot
Seventy‐kilodalton heat shock proteins and an additional component from reticulocyte lysate stimulate import of M13 procoat protein into microsomes.
inferredcites →https://doi.org/10.1002/j.1460-2075.1989.tb03529.xopenalex-snapshot
Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides.
inferredcites →https://doi.org/10.1002/j.1460-2075.1989.tb08411.xopenalex-snapshot
Three pure chaperone proteins of Escherichia coli‐‐SecB, trigger factor and GroEL‐‐form soluble complexes with precursor proteins in vitro.
inferredcites →https://doi.org/10.1002/j.1460-2075.1989.tb08517.xopenalex-snapshot
Effects of mutations in heat‐shock genes groES and groEL on protein export in Escherichia coli.
inferredcites →https://doi.org/10.1002/j.1460-2075.1990.tb07403.xopenalex-snapshot
The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta‐lactamase precursor.
inferredcites →https://doi.org/10.1002/j.1460-2075.1990.tb07561.xopenalex-snapshot
Cotranslational glycosylation of proteins in systems depleted of protein disulphide isomerase.
inferredcites →https://doi.org/10.1002/j.1460-2075.1990.tb07880.xopenalex-snapshot
A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein.
inferredcites →https://doi.org/10.1002/j.1460-2075.1991.tb08044.xopenalex-snapshot
A hypothetical model for the peptide binding domain of hsp70 based on the peptide binding domain of HLA.
inferredcites →https://doi.org/10.1002/prot.340060202openalex-snapshot
The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure
inferredcites →https://doi.org/10.1007/bf00216688openalex-snapshot
Which came first, MHC class I or class II?
inferredcites →https://doi.org/10.1007/bf00331858openalex-snapshot
Genes involved in the control of nuclear fusion during the sexual cycle of Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1016/0022-2836(79)90502-3openalex-snapshot
Purification and properties of groE, a host protein involved in bacteriophage assembly
inferredcites →https://doi.org/10.1016/0022-2836(82)90308-4openalex-snapshot
Interactions of mouse immunoglobulin chains within Xenopus oocytes
inferredcites →https://doi.org/10.1016/0022-2836(88)90555-4openalex-snapshot
Scaffolding protein regulates the polymerization of P22 coat subunits into icosahedral shells in vitro
inferredcites →https://doi.org/10.1016/0079-6107(87)90011-3openalex-snapshot
Folding and association of proteins
inferredcites →https://doi.org/10.1016/0092-8674(77)90305-1openalex-snapshot
Induction of two transformation-sensitive membrane polypeptides in normal fibroblasts by a block in glycoprotein synthesis or glucose deprivation
inferredcites →https://doi.org/10.1016/0092-8674(81)90055-6openalex-snapshot
The specific interaction of the Rous sarcoma virus transforming protein, pp60src, with two cellular proteins
inferredcites →https://doi.org/10.1016/0092-8674(86)90074-7openalex-snapshot
Correlation of competence for export with lack of tertiary structure of the mature species: A study in vivo of maltose-binding protein in E. coli
inferredcites →https://doi.org/10.1016/0092-8674(86)90076-0openalex-snapshot
Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport
inferredcites →https://doi.org/10.1016/0092-8674(86)90532-5openalex-snapshot
Uncoating ATPase is a member of the 70 kilodalton family of stress proteins
inferredcites →https://doi.org/10.1016/0092-8674(86)90693-8openalex-snapshot
Speculations on the functions of the major heat shock and glucose-regulated proteins
inferredcites →https://doi.org/10.1016/0092-8674(86)90746-4openalex-snapshot
An hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein
inferredcites →https://doi.org/10.1016/0092-8674(86)90852-4openalex-snapshot
Enzymatic recycling of clathrin from coated vesicles
inferredcites →https://doi.org/10.1016/0092-8674(88)90115-8openalex-snapshot
ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle
inferredcites →https://doi.org/10.1016/0092-8674(88)90120-1openalex-snapshot
Glycosylation site binding protein, a component of oligosaccharyl transferase, is highly similar to three other 57 kd luminal proteins of the ER
inferredcites →https://doi.org/10.1016/0092-8674(88)90122-5openalex-snapshot
A movable and regulable inactivation function within the steroid binding domain of the glucocorticoid receptor
inferredcites →https://doi.org/10.1016/0092-8674(88)90389-3openalex-snapshot
The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein
inferredcites →https://doi.org/10.1016/0092-8674(88)90458-8openalex-snapshot
Protein unfolding and the energetics of protein translocation across biological membranes
inferredcites →https://doi.org/10.1016/0092-8674(89)90005-6openalex-snapshot
Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells
inferredcites →https://doi.org/10.1016/0092-8674(89)90043-3openalex-snapshot
Protein disulfide isomerase: Multiple roles in the modification of nascent secretory proteins
inferredcites →https://doi.org/10.1016/0092-8674(89)90058-5openalex-snapshot
KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene
inferredcites →https://doi.org/10.1016/0092-8674(89)90059-7openalex-snapshot
S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP
inferredcites →https://doi.org/10.1016/0092-8674(90)90263-eopenalex-snapshot
Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis
inferredcites →https://doi.org/10.1016/0092-8674(90)90268-jopenalex-snapshot
The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner
inferredcites →https://doi.org/10.1016/0092-8674(90)90437-jopenalex-snapshot
How do polypeptides cross the mitochondrial membranes?
inferredcites →https://doi.org/10.1016/0092-8674(90)90488-zopenalex-snapshot
Stress proteins in biology and medicine
inferredcites →https://doi.org/10.1016/0092-8674(91)90156-sopenalex-snapshot
The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins
inferredcites →https://doi.org/10.1016/0167-5699(87)90861-9openalex-snapshot
The role of immunoglobulin heavy chain binding protein
inferredcites →https://doi.org/10.1016/0968-0004(84)90152-xopenalex-snapshot
Native disulphide bond formation in protein biosynthesis: evidence for the role of protein disulphide isomerase
inferredcites →https://doi.org/10.1016/0968-0004(87)90011-9openalex-snapshot
Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells
inferredcites →https://doi.org/10.1016/0968-0004(89)90067-4openalex-snapshot
How does protein folding get started?
inferredcites →https://doi.org/10.1016/0968-0004(89)90168-0openalex-snapshot
Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures
inferredcites →https://doi.org/10.1016/0968-0004(90)90019-8openalex-snapshot
Peptide sequences that target cytosolic proteins for lysosomal proteolysis
inferredcites →https://doi.org/10.1016/0968-0004(91)90055-zopenalex-snapshot
Is hsp70 the cellular thermometer?
inferredcites →https://doi.org/10.1016/s0021-9258(17)39211-6openalex-snapshot
ATP catalyzes the sequestration of clathrin during enzymatic uncoating.
inferredcites →https://doi.org/10.1016/s0021-9258(17)43091-2openalex-snapshot
Biochemical characterization of the 94- and 78-kilodalton glucose-regulated proteins in hamster fibroblasts.
inferredcites →https://doi.org/10.1016/s0021-9258(18)47496-0openalex-snapshot
ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94).
inferredcites →https://doi.org/10.1016/s0021-9258(18)47769-1openalex-snapshot
The role of protein structure in the mitochondrial import pathway. Unfolding of mitochondrially bound precursors is required for membrane translocation.
inferredcites →https://doi.org/10.1016/s0021-9258(18)61274-8openalex-snapshot
T3-p28 is a protein associated with the delta and epsilon chains of the T cell receptor-T3 antigen complex during biosynthesis.
inferredcites →https://doi.org/10.1016/s0021-9258(18)67256-4openalex-snapshot
Purification and properties of the groES morphogenetic protein of Escherichia coli.
inferredcites →https://doi.org/10.1016/s0021-9258(18)68238-9openalex-snapshot
Cyclosporin A-binding protein (cyclophilin) of Neurospora crassa. One gene codes for both the cytosolic and mitochondrial forms.
inferredcites →https://doi.org/10.1016/s0021-9258(18)68402-9openalex-snapshot
Association and dissociation of the murine T cell receptor associated protein (TRAP). Early events in the biosynthesis of a multisubunit receptor.
inferredcites →https://doi.org/10.1016/s0021-9258(18)89471-6openalex-snapshot
Structure and assembly of the endoplasmic reticulum. The synthesis of three major endoplasmic reticulum proteins during lipopolysaccharide-induced differentiation of murine lymphocytes.
inferredcites →https://doi.org/10.1016/s0021-9258(18)98800-9openalex-snapshot
Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese
inferredcites →https://doi.org/10.1016/s0021-9258(18)99078-2openalex-snapshot
A novel secreted cyclophilin-like protein (SCYLP)
inferredcites →https://doi.org/10.1016/s0021-9258(18)99079-4openalex-snapshot
S-cyclophilin. New member of the cyclophilin family associated with the secretory pathway
inferredcites →https://doi.org/10.1016/s0021-9258(19)38489-3openalex-snapshot
Mapping the HSP90 binding region of the glucocorticoid receptor.
inferredcites →https://doi.org/10.1016/s0021-9258(19)38742-3openalex-snapshot
Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex.
inferredcites →https://doi.org/10.1016/s0021-9258(19)40163-4openalex-snapshot
ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase.
inferredcites →https://doi.org/10.1016/s0021-9258(19)47115-9openalex-snapshot
Identification, characterization, and purification of two mammalian stress proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein
inferredcites →https://doi.org/10.1016/s0021-9258(19)47184-6openalex-snapshot
Direct evidence that the glucocorticoid receptor binds to hsp90 at or near the termination of receptor translation in vitro
inferredcites →https://doi.org/10.1016/s0021-9258(19)67740-9openalex-snapshot
The 90-kDa heat shock protein (hsp-90) possesses an ATP binding site and autophosphorylating activity.
inferredcites →https://doi.org/10.1016/s0021-9258(19)67821-xopenalex-snapshot
Localization of the 90-kDa heat shock protein-binding site within the hormone-binding domain of the glucocorticoid receptor by peptide competition
inferredcites →https://doi.org/10.1016/s0021-9258(19)67841-5openalex-snapshot
Catalysis of protein folding by cyclophilins from different species
inferredcites →https://doi.org/10.1016/s0021-9258(19)75848-7openalex-snapshot
The ATPase core of a clathrin uncoating protein.
inferredcites →https://doi.org/10.1016/s0022-2836(77)80200-3openalex-snapshot
The protein data bank: A computer-based archival file for macromolecular structures
inferredcites →https://doi.org/10.1016/s0091-679x(08)61171-1openalex-snapshot
Chapter 7 Protein Folding and Intracellular Transport: Evaluation of Conformational Changes in Nascent Exocytotic Proteins
inferredcites →https://doi.org/10.1016/s0092-8674(85)80031-3openalex-snapshot
Production of abnormal proteins in E. coli stimulates transcription of ion and other heat shock genes
inferredcites →https://doi.org/10.1021/bi00220a020openalex-snapshot
GroE facilitates refolding of citrate synthase by suppressing aggregation
inferredcites →https://doi.org/10.1021/bi00226a009openalex-snapshot
Two distinct forms of peptidylprolyl-cis-trans-isomerase are expressed separately in periplasmic and cytoplasmic compartments of Escherichia coli cells
inferredcites →https://doi.org/10.1021/bi00244a001openalex-snapshot
The chaperonin GroEL binds a polypeptide in an .alpha.-helical conformation
inferredcites →https://doi.org/10.1021/bi00388a001openalex-snapshot
In vivo cross-linking of protein disulfide isomerase to immunoglobulins
inferredcites →https://doi.org/10.1021/bi00461a001openalex-snapshot
The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell
inferredcites →https://doi.org/10.1021/bi00468a001openalex-snapshot
Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymes
inferredcites →https://doi.org/10.1021/bi00476a003openalex-snapshot
Chaperonin-facilitated refolding of ribulose bisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are potassium dependent
inferredcites →https://doi.org/10.1038/275416a0openalex-snapshot
Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA
inferredcites →https://doi.org/10.1038/289366a0openalex-snapshot
Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
inferredcites →https://doi.org/10.1038/306387a0openalex-snapshot
Immunoglobulin heavy chain binding protein
inferredcites →https://doi.org/10.1038/317267a0openalex-snapshot
Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin
inferredcites →https://doi.org/10.1038/322209a0openalex-snapshot
Cell biology: An unfolding story of protein translocation
inferredcites →https://doi.org/10.1038/322228a0openalex-snapshot
Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
inferredcites →https://doi.org/10.1038/329268a0openalex-snapshot
Catalysis of protein folding by prolyl isomerase
inferredcites →https://doi.org/10.1038/329506a0openalex-snapshot
Structure of the human class I histocompatibility antigen, HLA-A2
inferredcites →https://doi.org/10.1038/332462a0openalex-snapshot
The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
inferredcites →https://doi.org/10.1038/332800a0openalex-snapshot
A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
inferredcites →https://doi.org/10.1038/332805a0openalex-snapshot
70K heat shock related proteins stimulate protein translocation into microsomes
inferredcites →https://doi.org/10.1038/333330a0openalex-snapshot
Homologous plant and bacterial proteins chaperone oligomeric protein assembly
inferredcites →https://doi.org/10.1038/335649a0openalex-snapshot
Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes
inferredcites →https://doi.org/10.1038/336254a0openalex-snapshot
Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein
inferredcites →https://doi.org/10.1038/337044a0openalex-snapshot
GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
inferredcites →https://doi.org/10.1038/337620a0openalex-snapshot
Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
inferredcites →https://doi.org/10.1038/337655a0openalex-snapshot
Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor
inferredcites →https://doi.org/10.1038/338067a0openalex-snapshot
The ninaA gene required for visual transduction in Drosophila encodes a homologue of cyclosporin A-binding protein
inferredcites →https://doi.org/10.1038/341125a0openalex-snapshot
Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
inferredcites →https://doi.org/10.1038/342224a0openalex-snapshot
Chaperones, paperones
inferredcites →https://doi.org/10.1038/342248a0openalex-snapshot
Crystal structure of chaperone protein PapD reveals an immunoglobulin fold
inferredcites →https://doi.org/10.1038/342451a0openalex-snapshot
Demonstration by genetic suppression of interaction of GroE products with many proteins
inferredcites →https://doi.org/10.1038/342884a0openalex-snapshot
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
inferredcites →https://doi.org/10.1038/342953a0openalex-snapshot
Sensitivity to cyclosporin A is mediated by cyclophilin in Neurospora crassa and Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1038/344882a0openalex-snapshot
Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli
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/10.1038/348137a0openalex-snapshot
Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
inferredcites →https://doi.org/10.1038/348166a0openalex-snapshot
Reduced levels of hsp90 compromise steroid receptor action in vivo
inferredcites →https://doi.org/10.1038/348339a0openalex-snapshot
(Mg–ATP)-dependent self-assembly of molecular chaperone GroEL
inferredcites →https://doi.org/10.1038/348455a0openalex-snapshot
The mitochondrial chaperonin hsp60 is required for its own assembly
inferredcites →https://doi.org/10.1038/350165a0openalex-snapshot
Function of DnaJ and DnaK as chaperones in origin-specific DNA binding by RepA
inferredcites →https://doi.org/10.1038/352036a0openalex-snapshot
Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
inferredcites →https://doi.org/10.1038/353321a0openalex-snapshot
The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation
inferredcites →https://doi.org/10.1042/bj2700001openalex-snapshot
Protein folding
inferredcites →https://doi.org/10.1042/bst0160096openalex-snapshot
Protein disulphide-isomerase: a homologue of thioredoxin implicated in the biosynthesis of secretory proteins
inferredcites →https://doi.org/10.1073/pnas.47.9.1309openalex-snapshot
THE KINETICS OF FORMATION OF NATIVE RIBONUCLEASE DURING OXIDATION OF THE REDUCED POLYPEPTIDE CHAIN
inferredcites →https://doi.org/10.1073/pnas.73.10.3651openalex-snapshot
A mutant of Saccharomyces cerevisiae defective for nuclear fusion.
inferredcites →https://doi.org/10.1073/pnas.80.21.6431openalex-snapshot
The dnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system.
inferredcites →https://doi.org/10.1073/pnas.81.3.848openalex-snapshot
Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous.
inferredcites →https://doi.org/10.1073/pnas.84.12.4156openalex-snapshot
SSC1, a member of the 70-kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth.
inferredcites →https://doi.org/10.1073/pnas.85.18.6632openalex-snapshot
Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage lambda DNA replication.
inferredcites →https://doi.org/10.1073/pnas.86.14.5390openalex-snapshot
Drosophila ninaA gene encodes an eye-specific cyclophilin (cyclosporine A binding protein).
inferredcites →https://doi.org/10.1073/pnas.86.20.7805openalex-snapshot
A member of the Hsp70 family is localized in mitochondria and resembles Escherichia coli DnaK.
inferredcites →https://doi.org/10.1073/pnas.87.11.4028openalex-snapshot
Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: a periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A.
inferredcites →https://doi.org/10.1073/pnas.87.19.7683openalex-snapshot
Identification of a groES-like chaperonin in mitochondria that facilitates protein folding.
inferredcites →https://doi.org/10.1073/pnas.87.3.1159openalex-snapshot
An essential member of the HSP70 gene family of Saccharomyces cerevisiae is homologous to immunoglobulin heavy chain binding protein.
inferredcites →https://doi.org/10.1073/pnas.87.5.1749openalex-snapshot
Hsp70 proteins, similar to Escherichia coli DnaK, in chloroplasts and mitochondria of Euglena gracilis.
inferredcites →https://doi.org/10.1073/pnas.88.10.4453openalex-snapshot
Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast.
inferredcites →https://doi.org/10.1073/pnas.88.11.5041openalex-snapshot
Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein.
inferredcites →https://doi.org/10.1073/pnas.88.15.6677openalex-snapshot
Molecular cloning of a membrane-associated human FK506- and rapamycin-binding protein, FKBP-13.
inferredcites →https://doi.org/10.1073/pnas.88.2.537openalex-snapshot
Evolution of the major histocompatibility complex: molecular cloning of major histocompatibility complex class I from the amphibian Xenopus.
inferredcites →https://doi.org/10.1073/pnas.88.3.1029openalex-snapshot
FKB1 encodes a nonessential FK 506-binding protein in Saccharomyces cerevisiae and contains regions suggesting homology to the cyclophilins.
inferredcites →https://doi.org/10.1073/pnas.88.5.1903openalex-snapshot
Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence.
inferredcites →https://doi.org/10.1073/pnas.88.5.1948openalex-snapshot
FK 506-binding protein proline rotamase is a target for the immunosuppressive agent FK 506 in Saccharomyces cerevisiae.
inferredcites →https://doi.org/10.1073/pnas.88.7.2874openalex-snapshot
Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.
inferredcites →https://doi.org/10.1083/jcb.102.5.1558openalex-snapshot
Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas.
inferredcites →https://doi.org/10.1083/jcb.103.4.1179openalex-snapshot
Assembly of influenza hemagglutinin trimers and its role in intracellular transport.
inferredcites →https://doi.org/10.1083/jcb.104.3.761openalex-snapshot
Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein.
inferredcites →https://doi.org/10.1083/jcb.105.6.2665openalex-snapshot
The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins.
inferredcites →https://doi.org/10.1083/jcb.105.6.2905openalex-snapshot
Translocation in yeast and mammalian cells: not all signal sequences are functionally equivalent.
inferredcites →https://doi.org/10.1083/jcb.107.6.2051openalex-snapshot
70-kD heat shock-related protein is one of at least two distinct cytosolic factors stimulating protein import into mitochondria.
inferredcites →https://doi.org/10.1083/jcb.108.6.2117openalex-snapshot
Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP).
inferredcites →https://doi.org/10.1083/jcb.109.5.1947openalex-snapshot
Mutational analysis of the human HSP70 protein: distinct domains for nucleolar localization and adenosine triphosphate binding.
inferredcites →https://doi.org/10.1083/jcb.109.6.2641openalex-snapshot
Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast.
inferredcites →https://doi.org/10.1083/jcb.109.6.2665openalex-snapshot
A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein.
inferredcites →https://doi.org/10.1083/jcb.109.6.3273openalex-snapshot
Intracellular maturation and transport of the SV5 type II glycoprotein hemagglutinin-neuraminidase: specific and transient association with GRP78-BiP in the endoplasmic reticulum and extensive internalization from the cell surface.
inferredcites →https://doi.org/10.1083/jcb.110.6.1885openalex-snapshot
Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast.
inferredcites →https://doi.org/10.1083/jcb.111.3.829openalex-snapshot
Immunoglobulin heavy chain and binding protein complexes are dissociated in vivo by light chain addition.
inferredcites →https://doi.org/10.1083/jcb.112.6.1099openalex-snapshot
Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules.
inferredcites →https://doi.org/10.1083/jcb.113.5.1125openalex-snapshot
BIP associates with newly synthesized subunits of the mouse muscle nicotinic receptor.
inferredcites →https://doi.org/10.1083/jcb.99.2.723openalex-snapshot
An enzyme that removes clathrin coats: purification of an uncoating ATPase.
inferredcites →https://doi.org/10.1089/dna.1988.7.261openalex-snapshot
pl Bl5: A cDNA Clone of the Rat mRNA Encoding Cyclophilin
inferredcites →https://doi.org/10.1093/nar/18.6.1643openalex-snapshot
A second cyclophilin-related gene inSaccharomyces cerevisiae
inferredcites →https://doi.org/10.1101/gad.3.8.1226openalex-snapshot
Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation.
inferredcites →https://doi.org/10.1105/tpc.1.12.1223openalex-snapshot
Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone.
inferredcites →https://doi.org/10.1111/j.1365-2958.1991.tb01821.xopenalex-snapshot
Molecular chaperones and protein translocation across the Escherichia coli inner membrane
inferredcites →https://doi.org/10.1111/j.1365-2958.1991.tb01907.xopenalex-snapshot
Filnmentous phage assembly
inferredcites →https://doi.org/10.1126/science.1702904openalex-snapshot
Chemistry and Biology of the Immunophilins and Their Immunosuppressive Ligands
inferredcites →https://doi.org/10.1126/science.1709301openalex-snapshot
Solution Structure of FKBP, a Rotamase Enzyme and Receptor for FK506 and Rapamycin
inferredcites →https://doi.org/10.1126/science.1709302openalex-snapshot
Atomic Structure of FKBP-FK506, an Immunophilin-Immunosuppressant Complex
inferredcites →https://doi.org/10.1126/science.181.4096.223openalex-snapshot
Principles that Govern the Folding of Protein Chains
inferredcites →https://doi.org/10.1126/science.2188360openalex-snapshot
Interaction of Hsp 70 with Newly Synthesized Proteins: Implications for Protein Folding and Assembly
inferredcites →https://doi.org/10.1126/science.2255910openalex-snapshot
Isotope-Edited NMR of Cyclosporin a Bound to Cyclophilin: Evidence for a Trans 9,10 Amide Bond
inferredcites →https://doi.org/10.1126/science.2406905openalex-snapshot
Protein Sorting to Mitochondria: Evolutionary Conservations of Folding and Assembly
inferredcites →https://doi.org/10.1126/science.250.4983.954openalex-snapshot
Molecular Chaperones: The Plant Connection
inferredcites →https://doi.org/10.1126/science.2756425openalex-snapshot
Peptide Binding and Release by Proteins Implicated as Catalysts of Protein Assembly
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/10.1126/science.3083508openalex-snapshot
Abnormal Proteins Serve as Eukaryotic Stress Signals and Trigger the Activation of Heat Shock Genes
inferredcites →https://doi.org/10.1128/jb.171.3.1379-1385.1989openalex-snapshot
The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
inferredcites →https://doi.org/10.1128/mcb.11.7.3484openalex-snapshot
An Endoplasmic Reticulum-Specific Cyclophilin
inferredcites →https://doi.org/10.1128/mcb.4.12.2697openalex-snapshot
Myristic Acid Is Attached to the Transforming Protein of Rous Sarcoma Virus During or Immediately After Synthesis and Is Present in Both Soluble and Membrane-Bound Forms of the Protein
inferredcites →https://doi.org/10.1128/mcb.7.12.4414openalex-snapshot
A Normal Mitochondrial Protein is Selectively Synthesized and Accumulated During Heat Shock in Tetrahymena Thermophila
inferredcites →https://doi.org/10.1128/mcb.7.7.2568-2577.1987openalex-snapshot
Complex Interactions Among Members of an Essential Subfamily of hsp70 Genes in Saccharomyces Cerevisiae
inferredcites →https://doi.org/10.1128/mcb.8.1.371openalex-snapshot
A Highly Evolutionarily Conserved Mitochondrial Protein Is Structurally Related to the Protein Encoded by the Escherichia coli groEL Gene
inferredcites →https://doi.org/10.1128/mcb.8.3.1206openalex-snapshot
Purification of complexes of nuclear oncogene p53 with rat and Escherichia coli heat shock proteins: in vitro dissociation of hsc70 and dnaK from murine p53 by ATP.
inferredcites →https://doi.org/10.1128/mcb.9.11.5163openalex-snapshot
Molecular Cloning of mtp70, a Mitochondrial Member of the hsp70 Family
inferredcites →https://doi.org/10.1128/mcb.9.7.3000openalex-snapshot
SSC1, an essential member of the yeast HSP70 multigene family, encodes a mitochondrial protein.
inferredcites →https://doi.org/10.1128/mcb.9.7.3000-3008.1989openalex-snapshot
SSC1, an Essential Member of the Yeast HSP70 Multigene Family, Encodes a Mitochondrial Protein
inferredcites →https://doi.org/10.1146/annurev.bi.54.070185.001321openalex-snapshot
THIOREDOXIN
inferredcites →https://doi.org/10.1146/annurev.bi.55.070186.005443openalex-snapshot
THE HEAT-SHOCK RESPONSE
inferredcites →https://doi.org/10.1146/annurev.bi.59.070190.003215openalex-snapshot
INTERMEDIATES IN THE FOLDING REACTIONS OF SMALL PROTEINS
inferredcites →https://doi.org/10.1146/annurev.cb.05.110189.000245openalex-snapshot
Control of Protein Exit from the Endoplasmic Reticulum
inferredcites →https://doi.org/10.1146/annurev.cb.06.110190.001013openalex-snapshot
Chaperone Function: The Assembly of Ribulose Bisphosphate Carboxylase-Oxygenase
inferredcites →https://doi.org/10.1146/annurev.ge.22.120188.000453openalex-snapshot
THE MECHANISM OF CONSERVATIVE SITE-SPECIFIC RECOMBINATION
inferredcites →https://doi.org/10.1152/ajpcell.1986.250.1.c1openalex-snapshot
Stress protein systems of mammalian cells
inferredcites →https://doi.org/10.1242/jcs.86.1.217openalex-snapshot
Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin
inferredcites →https://doi.org/10.1242/jcs.91.1.61openalex-snapshot
Identification of a set of calcium-binding proteins in reticuloplasm, the luminal content of the endoplasmic reticulum
inferredcites →https://doi.org/10.3109/10409238509085135openalex-snapshot
The Heat Shock Respons
inferredcites →https://doi.org/10.4049/jimmunol.114.2_part_1.655openalex-snapshot
Heavy Chain-Producing Variants of a Mouse Myeloma Cell Line

What points at this work

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

inferred← citeshttps://doi.org/10.2478/jofnem-2023-0009zenodo-depositor-declared
Effect of Vicia sativa L. on Motility, Mortality and Expression Levels of hsp Genes in J2 Stage of Meloidogyne hapla
inferred← citeshttps://doi.org/10.1001/archsurg.134.11.1248openalex-snapshot
Expression Patterns of Heat Shock Proteins in Lungs of Neonates With Congenital Diaphragmatic Hernia
inferred← citeshttps://doi.org/10.1001/archsurg.1995.01430120014002openalex-snapshot
Induction of Heat Shock Protein 72 Prevents Neutrophil-Mediated Human Endothelial Cell Necrosis
inferred← citeshttps://doi.org/10.1002/(sici)1096-9101(1997)20:4<451::aid-lsm12>3.0.co;2-eopenalex-snapshot
Helium-neon laser irradiation is not a stressful treatment: A study on heat-shock protein (HSP70) level
inferred← citeshttps://doi.org/10.1002/(sici)1096-987x(200006)21:8<626::aid-jcc4>3.0.co;2-popenalex-snapshot
Peptide models XXIII. Conformational model for polar side-chain containing amino acid residues: A comprehensive analysis of RHF, DFT, and MP2 properties of HCO-L-SER-NH2
inferred← citeshttps://doi.org/10.1002/(sici)1096-9896(199608)179:4<409::aid-path602>3.0.co;2-eopenalex-snapshot
IMMUNOCYTOCHEMICAL EXPRESSION OF THE 70 kD HEAT SHOCK PROTEIN IN ISCHAEMIC BOWEL DISEASE
inferred← citeshttps://doi.org/10.1002/(sici)1096-9896(199802)184:2<212::aid-path996>3.0.co;2-zopenalex-snapshot
The retention of abnormal type I procollagen and correlated expression of HSP 47 in fibroblasts from a patient with lethal osteogenesis imperfecta
inferred← citeshttps://doi.org/10.1002/(sici)1097-0029(20000515)49:4<329::aid-jemt2>3.0.co;2-hopenalex-snapshot
Roles of molecular chaperones in pancreatic secretion and their involvement in intestinal absorption
inferred← citeshttps://doi.org/10.1002/(sici)1097-0061(199607)12:9<849::aid-yea985>3.0.co;2-zopenalex-snapshot
Identification and characterization of cytosolic Hansenula polymorpha proteins belonging to the Hsp70 protein family
inferred← citeshttps://doi.org/10.1002/(sici)1097-0061(19960930)12:12<1229::aid-yea15>3.0.co;2-hopenalex-snapshot
N-glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast
inferred← citeshttps://doi.org/10.1002/(sici)1097-0061(19970330)13:4<337::aid-yea98>3.0.co;2-kopenalex-snapshot
Enhancement of Protein Secretion in Saccharomyces cerevisiae by Overproduction of Sso Protein, a Late‐acting Component of the Secretory Machinery
inferred← citeshttps://doi.org/10.1002/(sici)1097-0061(19970915)13:11<1009::aid-yea157>3.0.co;2-kopenalex-snapshot
Accumulation of Misfolded Protein Aggregates Leads to the Formation of Russell Body-like Dilated Endoplasmic Reticulum in Yeast
inferred← citeshttps://doi.org/10.1002/(sici)1097-0061(199710)13:13<1211::aid-yea168>3.0.co;2-8openalex-snapshot
Inducible Membranes in Yeast: Relation to the Unfolded-Protein-Response Pathway
inferred← citeshttps://doi.org/10.1002/(sici)1097-0061(1998100)14:14<1285::aid-yea329>3.0.co;2-0openalex-snapshot
Characterization of deletion mutations in the carboxy-terminal peptide-binding domain of the Kar2 protein inSaccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1002/(sici)1097-0134(199601)24:1<1::aid-prot1>3.0.co;2-oopenalex-snapshot
Helical fold prediction for the cyclin box
inferred← citeshttps://doi.org/10.1002/(sici)1097-0134(199606)25:2<237::aid-prot9>3.0.co;2-eopenalex-snapshot
Protein structure and the sequential structure of mRNA: α-Helix and β-sheet signals at the nucleotide level
inferred← citeshttps://doi.org/10.1002/(sici)1097-0134(199608)25:4<517::aid-prot13>3.0.co;2-kopenalex-snapshot
Expression and crystallization of the yeast Hsp82 chaperone, and preliminary x-ray diffraction studies of the amino-terminal domain
inferred← citeshttps://doi.org/10.1002/(sici)1097-0177(199702)208:2<227::aid-aja10>3.0.co;2-0openalex-snapshot
Induction of Hsp72 and transient nuclear localization of Hsp73 and Hsp72 correlate with the acquisition and loss of thermotolerance in postimplantation rat embryos
inferred← citeshttps://doi.org/10.1002/(sici)1097-0215(19960410)66:2<234::aid-ijc16>3.0.co;2-copenalex-snapshot
Primary monoclonal and secondary polyclonal growth of colon neoplastic lesions in C3H/HeN→BALB/c chimeric mice treated with 1,2-dimethylhydrazine: Immunohistochemical detection of C3H strain-specific antigen and simple sequence length polymorphism analysis of DNA
inferred← citeshttps://doi.org/10.1002/(sici)1097-0215(19980529)76:5<639::aid-ijc5>3.0.co;2-ropenalex-snapshot
Selective down-regulation of human papillomavirus transcription by 2-deoxyglucose
inferred← citeshttps://doi.org/10.1002/(sici)1097-0290(19960920)51:6<691::aid-bit7>3.0.co;2-copenalex-snapshot
Endoplasmic reticulum protein expression in recombinant NS0 myelomas grown in batch culture
inferred← citeshttps://doi.org/10.1002/(sici)1097-4547(19961215)46:6<652::aid-jnr2>3.0.co;2-eopenalex-snapshot
Intracellular localization of heat shock mRNAs (hsc70 and hsp70) to neural cell bodies and processes in the control and hyperthermic rabbit brain
inferred← citeshttps://doi.org/10.1002/(sici)1097-4547(19990101)55:1<36::aid-jnr5>3.0.co;2-eopenalex-snapshot
Ca2 and Mg2 selectively induce aggregates of PHF‐tau but not normal human tau
inferred← citeshttps://doi.org/10.1002/(sici)1097-4644(199608)62:2<223::aid-jcb10>3.0.co;2-mopenalex-snapshot
Connecting nuclear architecture and genomic function
inferred← citeshttps://doi.org/10.1002/(sici)1097-4644(19970701)66:1<98::aid-jcb11>3.0.co;2-9openalex-snapshot
Intracellular distribution of heat-induced stress glycoproteins
inferred← citeshttps://doi.org/10.1002/(sici)1097-4644(19980315)68:4<436::aid-jcb4>3.0.co;2-ropenalex-snapshot
Elevated expression of PDI family proteins during differentiation of mouse F9 teratocarcinoma cells
inferred← citeshttps://doi.org/10.1002/(sici)1097-4644(19980401)69:1<30::aid-jcb4>3.0.co;2-wopenalex-snapshot
Calreticulin associates with stress proteins: Implications for chaperone function during heat stress
inferred← citeshttps://doi.org/10.1002/(sici)1097-4644(19981101)71:2<216::aid-jcb7>3.0.co;2-yopenalex-snapshot
Role of the pro-α2(I) COOH-terminal region in assembly of type I collagen: Truncation of the last 10 amino acid residues of pro-α2(I) chain prevents assembly of type I collagen heterotrimer
inferred← citeshttps://doi.org/10.1002/(sici)1097-4644(19981101)71:2<233::aid-jcb8>3.0.co;2-wopenalex-snapshot
Role of the pro-α2(I) COOH-terminal region in assembly of type I collagen: Disruption of two intramolecular disulfide bonds in pro-α2(I) blocks assembly of type I collagen
inferred← citeshttps://doi.org/10.1002/(sici)1097-4644(19990315)72:4<558::aid-jcb11>3.0.co;2-xopenalex-snapshot
Heat-induced expression of MHC-linked HSP70 genes in lymphocytes varies at the single-cell level
inferred← citeshttps://doi.org/10.1002/(sici)1097-4644(19991201)75:3<446::aid-jcb10>3.0.co;2-iopenalex-snapshot
Secretion of glycosylation site mutants can be rescued by the signal/pro sequence of tissue plasminogen activator
inferred← citeshttps://doi.org/10.1002/(sici)1097-4644(19991201)75:3<446::aid-jcb10>3.3.co;2-9openalex-snapshot
Secretion of glycosylation site mutants can be rescued by the signal/pro sequence of tissue plasminogen activator
inferred← citeshttps://doi.org/10.1002/(sici)1097-4644(19991215)75:4<610::aid-jcb7>3.0.co;2-8openalex-snapshot
Involvement of p42/p44 mitogen-activated protein kinase in prostaglandin f2?-stimulated induction of heat shock protein 27 in osteoblasts
inferred← citeshttps://doi.org/10.1002/(sici)1097-4644(20000615)77:4<615::aid-jcb9>3.0.co;2-mopenalex-snapshot
Stable expression of functional CBP70 lectin during heat shock
inferred← citeshttps://doi.org/10.1002/(sici)1097-4652(199602)166:2<332::aid-jcp11>3.0.co;2-dopenalex-snapshot
Enhancement of stress-induced synthesis of hsp27 and αB crystallin by modulators of the arachidonic acid cascade
inferred← citeshttps://doi.org/10.1002/(sici)1097-4652(199608)168:2<248::aid-jcp3>3.0.co;2-popenalex-snapshot
Intracellular location of cysteine transport activity correlates with productive processing of antigen disulfide
inferred← citeshttps://doi.org/10.1002/(sici)1097-4652(199701)170:1<19::aid-jcp3>3.0.co;2-oopenalex-snapshot
Inhibition of colony formation of NIH 3T3 cells by the expression of the small molecular weight heat shock protein HSP27: Involvement of its phosphorylation and aggregation at the C-terminal region
inferred← citeshttps://doi.org/10.1002/(sici)1097-4652(199702)170:2<130::aid-jcp4>3.0.co;2-popenalex-snapshot
Tissue-specific differences in heat shock protein hsc70 and hsp70 in the control and hyperthermic rabbit
inferred← citeshttps://doi.org/10.1002/(sici)1097-4652(199707)172:1<44::aid-jcp5>3.0.co;2-dopenalex-snapshot
Distribution of HSP70, protein kinase C, and spectrin is altered in lymphocytes during a fever-like hyperthermia exposure
inferred← citeshttps://doi.org/10.1002/(sici)1097-4652(199811)177:2<282::aid-jcp10>3.0.co;2-copenalex-snapshot
Down-regulation of epidermal growth factor receptor-signaling pathway by binding of GRP78/BiP to the receptor under glucose-starved stress conditions
inferred← citeshttps://doi.org/10.1002/(sici)1097-4652(199901)178:1<93::aid-jcp12>3.0.co;2-uopenalex-snapshot
An ethanol-sensitive variant of the PC12 neuronal cell line: Sensitivity to alcohol is associated with increased cell adhesion and decreased glucose accumulation
inferred← citeshttps://doi.org/10.1002/(sici)1098-0997(1999)7:1/2<80::aid-idog15>3.0.co;2-mopenalex-snapshot
Heat shock protein-based therapeutic strategies against human immunodeficiency virus type 1 infection
inferred← citeshttps://doi.org/10.1002/(sici)1099-0496(199810)26:17+<146::aid-ppul6>3.0.co;2-5openalex-snapshot
Symposium Session Summaries: Sessions 13.4 to 18.4
inferred← citeshttps://doi.org/10.1002/(sici)1099-1352(199812)11:1/6<25::aid-jmr384>3.0.co;2-topenalex-snapshot
Reactivation of glyceraldehyde-3-phosphate dehydrogenase using conjugates of monoclonal antibodies with polyelectrolyte complexes. An attempt to make an artificial chaperone
inferred← citeshttps://doi.org/10.1002/(sici)1520-6408(1997)21:3<223::aid-dvg5>3.0.co;2-9openalex-snapshot
Molecular characterization of a heat shock cognate cDNA of zebrafish, hsc70, and developmental expression of the corresponding transcripts
inferred← citeshttps://doi.org/10.1002/(sici)1520-6408(1998)23:2<104::aid-dvg2>3.0.co;2-aopenalex-snapshot
A homologue of the calcium-binding disulfide isomerase CaBP1 is expressed in the developing CNS ofDrosophila melanogaster
inferred← citeshttps://doi.org/10.1002/(sici)1521-1878(199807)20:7<546::aid-bies5>3.0.co;2-iopenalex-snapshot
Assembly, sorting, and exit of oligomeric proteins from the endoplasmic reticulum
inferred← citeshttps://doi.org/10.1002/(sici)1521-3757(19980403)110:7<908::aid-ange908>3.0.co;2-0openalex-snapshot
Proteinfaltung aus theoretischer und experimenteller Sicht
inferred← citeshttps://doi.org/10.1002/(sici)1521-4141(199903)29:03<845::aid-immu845>3.0.co;2-xopenalex-snapshot
Distinction between processing of normal and mutant complement C3 within human skin fibroblasts
inferred← citeshttps://doi.org/10.1002/(sici)1522-2683(19990201)20:2<409::aid-elps409>3.0.co;2-nopenalex-snapshot
Stathmin interaction with HSC70 family proteins
inferred← citeshttps://doi.org/10.1002/0471140864.ps0509s10openalex-snapshot
Overview of Protein Expression by Mammalian Cells
inferred← citeshttps://doi.org/10.1002/0471143030.cb0503s00openalex-snapshot
Determination of Molecular Size by Zonal Sedimentation Analysis on Sucrose Density Gradients
inferred← citeshttps://doi.org/10.1002/0471143030.cb1501s03openalex-snapshot
Overview of Protein Trafficking in the Secretory and Endocytic Pathways
inferred← citeshttps://doi.org/10.1002/047120918x.emb1228openalex-snapshot
Protein FoldingIn Vivo
inferred← citeshttps://doi.org/10.1002/0471250570.spi095openalex-snapshot
Protein Processing, Processing in the Endoplasmic Reticulum and G olgi Network
inferred← citeshttps://doi.org/10.1002/0471250589.ebt197openalex-snapshot
Secretion from Animal Cells
inferred← citeshttps://doi.org/10.1002/0471266949.bmc234openalex-snapshot
Antimalarials
inferred← citeshttps://doi.org/10.1002/1097-0185(20010201)262:2<213::aid-ar1031>3.0.co;2-wopenalex-snapshot
Constitutive expression of the 27-kDa heat-shock protein in neurons and satellite cells in the peripheral nervous system of the rat
inferred← citeshttps://doi.org/10.1002/1097-0215(20001115)88:4<535::aid-ijc4>3.0.co;2-vopenalex-snapshot
Identification of differentially expressed genes in human melanoma cells with acquired resistance to various antineoplastic drugs
inferred← citeshttps://doi.org/10.1002/1098-1128(200011)20:6<452::aid-med2>3.0.co;2-6openalex-snapshot
Immunophilins: Switched on protein binding domains?
inferred← citeshttps://doi.org/10.1002/1439-7633(20010803)2:7/8<505::aid-cbic505>3.0.co;2-topenalex-snapshot
Sorting of Preproteins into Mitochondria
inferred← citeshttps://doi.org/10.1002/1521-3757(20020402)114:7<1142::aid-ange1142>3.0.co;2-topenalex-snapshot
Molekulare Chaperone: zelluläre Maschinen für die Proteinfaltung
inferred← citeshttps://doi.org/10.1002/1521-3773(20020402)41:7<1098::aid-anie1098>3.0.co;2-9openalex-snapshot
Molecular Chaperones—Cellular Machines for Protein Folding
inferred← citeshttps://doi.org/10.1002/1522-2683(200011)21:17<3785::aid-elps3785>3.0.co;2-2openalex-snapshot
Human ERp29: Isolation, primary structural characterisation and two-dimensional gel mapping
inferred← citeshttps://doi.org/10.1002/1522-2683(200101)22:1<155::aid-elps155>3.0.co;2-lopenalex-snapshot
Identification of a phosphoprotein that is downregulated in immortalized human fibroblasts
inferred← citeshttps://doi.org/10.1002/1529-0131(200101)44:1<96::aid-anr13>3.0.co;2-#openalex-snapshot
Nitric oxide regulates mitochondrial respiration and functions of articular chondrocytes
inferred← citeshttps://doi.org/10.1002/1873-3468.13161openalex-snapshot
Unconventional RNA ‐binding proteins: an uncharted zone in RNA biology
inferred← citeshttps://doi.org/10.1002/1873-3468.14548openalex-snapshot
miR ‐4734 conditionally suppresses ER stress‐associated proinflammatory responses
inferred← citeshttps://doi.org/10.1002/2211-5463.13022openalex-snapshot
Prefoldin subunit 6 of Plasmodium falciparum binds merozoite surface protein-1.
inferred← citeshttps://doi.org/10.1002/9780470015902.a0005721.pub2openalex-snapshot
Protein Folding and Chaperones
inferred← citeshttps://doi.org/10.1002/9780470141649.ch7openalex-snapshot
Monte Carlo Approaches to the Protein Folding Problem
inferred← citeshttps://doi.org/10.1002/9780470511459.ch6openalex-snapshot
The Protein as a Supermolecule: The Architecture of a (βα)8Barrel
inferred← citeshttps://doi.org/10.1002/9780470514658.ch13openalex-snapshot
Primitive Vertebrate Immunity: What is the Evolutionary Derivation of Molecules that Define the Adaptive Immune System?
inferred← citeshttps://doi.org/10.1002/9780470751541.ch32openalex-snapshot
New Approaches
inferred← citeshttps://doi.org/10.1002/9780470939932.ch13openalex-snapshot
Refolding of Inclusion Body Proteins fromE. coli
inferred← citeshttps://doi.org/10.1002/9780470987070.ch16openalex-snapshot
Pharmacology and the Use of Immunosuppressive Agents After Hematopoietic Cell Transplantation
inferred← citeshttps://doi.org/10.1002/9781118222942.refsopenalex-snapshot
References
inferred← citeshttps://doi.org/10.1002/9781118523063.ch12openalex-snapshot
Amyloid‐Like Fibrils: Origin, Structure, Properties, and Potential Technological Applications
inferred← citeshttps://doi.org/10.1002/9781118530009.ch11openalex-snapshot
Distinction of Coexisting Protein Conformations by Capillary Electrophoresis
inferred← citeshttps://doi.org/10.1002/9781119075738.ch10openalex-snapshot
Emerging Applications of Dynamic Covalent Chemistry from Macro‐ to Nanoscopic Length Scales
inferred← citeshttps://doi.org/10.1002/9781119949091.ch17openalex-snapshot
Responses of Poultry to Environmental Challenges
inferred← citeshttps://doi.org/10.1002/9783527610754.sf15openalex-snapshot
Chaperone Function in Vitro
inferred← citeshttps://doi.org/10.1002/9783527610754.sf19openalex-snapshot
Protein Folding in the Endoplasmic Reticulum
inferred← citeshttps://doi.org/10.1002/9783527615971.ch3openalex-snapshot
Subunit Assembly of Oligomeric Enzymes
inferred← citeshttps://doi.org/10.1002/9783527616091.ch17openalex-snapshot
On the Correlation of Protein Structure with Local Sequence Patterns
inferred← citeshttps://doi.org/10.1002/9783527619498.ch36openalex-snapshot
Studying Protein Folding in Vivo
inferred← citeshttps://doi.org/10.1002/9783527619498.ch38openalex-snapshot
Analysis of Chaperone Function in Vitro
inferred← citeshttps://doi.org/10.1002/9783527619498.ch49openalex-snapshot
Protein Folding in the Endoplasmic Reticulum Via the Hsp70 Family
inferred← citeshttps://doi.org/10.1002/9783527620838.ch17openalex-snapshot
Genetic Engineering of Animal Cells
inferred← citeshttps://doi.org/10.1002/9783527620869.ch2openalex-snapshot
Sequence and Structure of Proteins
inferred← citeshttps://doi.org/10.1002/9783527620890.ch12openalex-snapshot
Cyclosporins: Recent Developments in Biosynthesis, Pharmacology and Biology, and Clinical Applications
inferred← citeshttps://doi.org/10.1002/9783527620890.ch7openalex-snapshot
Peptide Antibiotics
inferred← citeshttps://doi.org/10.1002/9783527620999.ch12gopenalex-snapshot
Cyclosporins: Recent Developments in Biosynthesis, Pharmacology and Biology, and Clinical Applications
inferred← citeshttps://doi.org/10.1002/9783527620999.ch17aopenalex-snapshot
Genetic Engineering of Animal Cells
inferred← citeshttps://doi.org/10.1002/9783527620999.ch2dopenalex-snapshot
Sequence and Structure of Proteins
inferred← citeshttps://doi.org/10.1002/9783527620999.ch7gopenalex-snapshot
Peptide Antibiotics
inferred← citeshttps://doi.org/10.1002/9783527631001.ch1openalex-snapshot
Kräfte in der Biologie
inferred← citeshttps://doi.org/10.1002/9783527675265.ch15openalex-snapshot
Adaptation and Mitigation Strategies of Plant Under Drought and High‐Temperature Stress
inferred← citeshttps://doi.org/10.1002/adhm.202101633openalex-snapshot
A Biomimetic Nonantibiotic Nanoplatform for Low‐Temperature Photothermal Treatment of Urinary Tract Infections Caused by Uropathogenic Escherichia coli
inferred← citeshttps://doi.org/10.1002/adhm.202102821openalex-snapshot
Biomimetic Metal−Organic Frameworks as Targeted Vehicles to Enhance Osteogenesis
inferred← citeshttps://doi.org/10.1002/adma.201501558openalex-snapshot
Adaptable Hydrogel Networks with Reversible Linkages for Tissue Engineering
inferred← citeshttps://doi.org/10.1002/adma.201806024openalex-snapshot
A Biomimetic Non‐Antibiotic Approach to Eradicate Drug‐Resistant Infections
inferred← citeshttps://doi.org/10.1002/aic.690430225openalex-snapshot
Molecular thermodynamics of heat‐induced protein unfolding in aqueous media
inferred← citeshttps://doi.org/10.1002/ana.410320619openalex-snapshot
Expression of 65‐kd heat shock proteins in the inflammatory myopathies
inferred← citeshttps://doi.org/10.1002/ange.19941061404openalex-snapshot
Über Peptidyl‐Prolyl‐cis/trans‐Isomerasen und ihre Effektoren
inferred← citeshttps://doi.org/10.1002/ange.201310249openalex-snapshot
Mechanistic Insights into the Interface‐Directed Transformation of Thiols into Disulfides and Molecular Hydrogen by Visible‐Light Irradiation of Quantum Dots
inferred← citeshttps://doi.org/10.1002/ange.201805695openalex-snapshot
Enantioseparation of Au20(PP3)4Cl4 Clusters with Intrinsically Chiral Cores
inferred← citeshttps://doi.org/10.1002/anie.199414151openalex-snapshot
Peptidyl‐Prolyl cis/trans Isomerases and Their Effectors
inferred← citeshttps://doi.org/10.1002/anie.201310249openalex-snapshot
Mechanistic Insights into the Interface‐Directed Transformation of Thiols into Disulfides and Molecular Hydrogen by Visible‐Light Irradiation of Quantum Dots
inferred← citeshttps://doi.org/10.1002/anie.201805695openalex-snapshot
Enantioseparation of Au 20 (PP 3 ) 4 Cl 4 Clusters with Intrinsically Chiral Cores
inferred← citeshttps://doi.org/10.1002/ar.10023openalex-snapshot
Transient occurrence of 27 kDa heat‐shock protein in the terminal tubule cells during postnatal development of the rat submandibular gland
inferred← citeshttps://doi.org/10.1002/ar.10070openalex-snapshot
Calnexin is associated with and induced by overexpressed human complement protein C2
inferred← citeshttps://doi.org/10.1002/asi.22974openalex-snapshot
A bibliometric study of highly cited reviews in the S cience C itation I ndex expanded™
inferred← citeshttps://doi.org/10.1002/bies.950140807openalex-snapshot
Membrane protein insertion into the endoplasmic reticulum ‐ another channel tunnel?
inferred← citeshttps://doi.org/10.1002/bies.950140912openalex-snapshot
Roots: Assembly of a complex bacteriophage in vitro
inferred← citeshttps://doi.org/10.1002/bies.950160916openalex-snapshot
Molecular chaperones in cellular protein folding
inferred← citeshttps://doi.org/10.1002/bies.950171209openalex-snapshot
Developmental regulation of αβ T cell antigen receptor assembly in immature CD4+CD8+ thymocytes
inferred← citeshttps://doi.org/10.1002/bies.950190409openalex-snapshot
Variable peroxisomal and mitochondrial targeting of alanine: Glyoxylate aminotransferase in mammalian evolution and disease
inferred← citeshttps://doi.org/10.1002/biof.5520090107openalex-snapshot
ATP‐sensitive association of mortalin with the IL‐1 receptor type I
inferred← citeshttps://doi.org/10.1002/bip.10221openalex-snapshot
Assembly of the 30S ribosomal subunit
inferred← citeshttps://doi.org/10.1002/bip.360360303openalex-snapshot
Specific interaction between cyclophilin and cyclic peptides
inferred← citeshttps://doi.org/10.1002/bit.10206openalex-snapshot
Induction of protein aggregation in an early secretory compartment by elevation of expression level
inferred← citeshttps://doi.org/10.1002/bit.10445openalex-snapshot
Endoplasmic reticulum signaling as a determinant of recombinant protein expression
inferred← citeshttps://doi.org/10.1002/bit.10517openalex-snapshot
Stability of protein production from recombinant mammalian cells
inferred← citeshttps://doi.org/10.1002/bit.20403openalex-snapshot
eIF2α phosphorylation, stress perception, and the shutdown of global protein synthesis in cultured CHO cells
inferred← citeshttps://doi.org/10.1002/bit.20762openalex-snapshot
Enhancement of protein secretion in Pichia pastoris by overexpression of protein disulfide isomerase
inferred← citeshttps://doi.org/10.1002/biuz.200410256openalex-snapshot
Stress im Boden: Früherkennung ökotoxikologischer Effekte durch Biomarker
inferred← citeshttps://doi.org/10.1002/bmc.1245openalex-snapshot
Purification of the 90 kDa heat shock protein (hsp90) and simultaneous purification of hsp70/hsc70, hsp90 and hsp96 from mammalian tissues and cells using thiophilic interaction chromatography
inferred← citeshttps://doi.org/10.1002/cbf.290100309openalex-snapshot
Targeting signals for protein import into peroxisomes
inferred← citeshttps://doi.org/10.1002/cbic.200400036openalex-snapshot
Key Players Involved in Bacterial Disulfide‐Bond Formation
inferred← citeshttps://doi.org/10.1002/cbic.201800782openalex-snapshot
A Fluorogenic AggTag Method Based on Halo‐ and SNAP‐Tags to Simultaneously Detect Aggregation of Two Proteins in Live Cells
inferred← citeshttps://doi.org/10.1002/cbic.202300149openalex-snapshot
Hydrogels with Reversible Crosslinks for Improved Localised Stem Cell Retention: A Review
inferred← citeshttps://doi.org/10.1002/cbic.70457openalex-snapshot
Enzyme‐Inspired Design of Redox‐Active Molecules for Promotion of Oxidative Protein Folding
inferred← citeshttps://doi.org/10.1002/celc.201801533openalex-snapshot
Enhanced Li‐Ion‐Storage Performance of MoS2 through Multistage Structural Design
inferred← citeshttps://doi.org/10.1002/cpdd.1openalex-snapshot
Pharmacokinetics and Safety of Migalastat HCl and Effects on Agalsidase Activity in Healthy Volunteers
inferred← citeshttps://doi.org/10.1002/cphy.c130007openalex-snapshot
Molecular Biology of Freezing Tolerance
inferred← citeshttps://doi.org/10.1002/cphy.cp140115openalex-snapshot
The ER –Golgi Membrane System: Compartmental Organization and Protein Traffic
inferred← citeshttps://doi.org/10.1002/cyto.a.22595openalex-snapshot
Prostaglandin E synthase interacts with inducible heat shock protein 70 after heat stress in bovine primary dermal fibroblast cells
inferred← citeshttps://doi.org/10.1002/dvdy.461openalex-snapshot
Disruption of Trip11 in cranial neural crest cells is associated with increased ER and Golgi stress contributing to skull defects in mice
inferred← citeshttps://doi.org/10.1002/dvg.1020140204openalex-snapshot
Development and tissue‐specific distribution of mouse small heat shock protein hsp25
inferred← citeshttps://doi.org/10.1002/dvg.1020140205openalex-snapshot
Tissue‐specific expression of heat shock proteins of the mouse in the absence of stress
inferred← citeshttps://doi.org/10.1002/dvg.1020140209openalex-snapshot
Changes in heat shock protein synthesis and heat sensitivity during mouse thymocyte development
inferred← citeshttps://doi.org/10.1002/dvg.1020160110openalex-snapshot
Tumor suppression in Drosophila is causally related to the function of the lethal(2)tumorous imaginal discs gene, a dnaJ homolog
inferred← citeshttps://doi.org/10.1002/eji.1830240139openalex-snapshot
Early events in the assembly of major histocompatibility complex class II heterotrimers from their free subunits
inferred← citeshttps://doi.org/10.1002/eji.1830240704openalex-snapshot
Peptide transporter‐independent, stress protein‐mediated endosomal processing of endogenous protein antigens for major histocompatibility complex class I presentation
inferred← citeshttps://doi.org/10.1002/eji.1830261220openalex-snapshot
Heat shock increases antigenic peptide generation but decreases antigen presentation
inferred← citeshttps://doi.org/10.1002/eji.1830261229openalex-snapshot
Defective antigen processing correlates with a low level of intracellular glutathione
inferred← citeshttps://doi.org/10.1002/eji.201444461openalex-snapshot
A RIDDle solved: Why an intact IRE1α/XBP‐1 signaling relay is key for humoral immune responses
inferred← citeshttps://doi.org/10.1002/elps.1150150161openalex-snapshot
Purification and identification of tyrosine‐phosphorylated proteins from B lymphocytes stimulated through the antigen receptor
inferred← citeshttps://doi.org/10.1002/elps.1150150166openalex-snapshot
The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin exhibit strikingly different levels in quiescent keratinocytes as compared to their proliferating normal and transformed counterparts: cDNA cloning and expression of calnexin
inferred← citeshttps://doi.org/10.1002/elps.1150170431openalex-snapshot
Identification of stress proteins in endothelial cells
inferred← citeshttps://doi.org/10.1002/elps.1150171109openalex-snapshot
Analysis of chaperonin‐containing TCP‐1 subunits in the human keratinocyte two‐dimensional protein database: Further characterisation of antibodies to individual subunits
inferred← citeshttps://doi.org/10.1002/elps.1150171114openalex-snapshot
Tumor suppressor p53 gene forms multiple isoforms: Evidence for single lucus origin and cytoplasmic complex formation with heat shock proteins
inferred← citeshttps://doi.org/10.1002/elps.1150171118openalex-snapshot
Expression and divalent cation binding properties of the novel chemotactic inflammatory protein psoriasin
inferred← citeshttps://doi.org/10.1002/elps.1150181424openalex-snapshot
Biogenesis of lipoprotein(a) in human and animal hepatocytes
inferred← citeshttps://doi.org/10.1002/elps.1150190531openalex-snapshot
Divergent and common groups of proteins in glands of venomous snakes
inferred← citeshttps://doi.org/10.1002/etc.5620130805openalex-snapshot
SPECIFIC CROSS-REACTIVITY OF ANTIBODIES RAISED AGAINST TWO MAJOR STRESS PROTEINS, STRESS 70 AND CHAPERONIN 60, IN DIVERSE SPECIES
inferred← citeshttps://doi.org/10.1002/etc.5620150810openalex-snapshot
ACCUMULATION OF HSP70 IN JUVENILE AND ADULT RAINBOW TROUT GILL EXPOSED TO METAL-CONTAMINATED WATER AND/OR DIET
inferred← citeshttps://doi.org/10.1002/etc.5620161127openalex-snapshot
STRESS PROTEINS HSP60 AND HSP70 IN THREE SPECIES OF AMPHIPODS EXPOSED TO CADMIUM, DIAZINON, DIELDRIN AND FLUORANTHENE
inferred← citeshttps://doi.org/10.1002/etc.5620171115openalex-snapshot
Validation of hsp70 stress gene expression as a marker of metal effects in Deroceras reticulatum (pulmonata): Correlation with demographic parameters
inferred← citeshttps://doi.org/10.1002/hep.1840180636openalex-snapshot
Stress proteins: Is their application in clinical medicine on the horizon?
inferred← citeshttps://doi.org/10.1002/hep.22430openalex-snapshot
“Toxic memory” via chaperone modification is a potential mechanism for rapid mallory-denk body reinduction
inferred← citeshttps://doi.org/10.1002/hep.510240635openalex-snapshot
Molecular Pathogenesis of Liver Disease in α1–Antitrypsin Deficiency
inferred← citeshttps://doi.org/10.1002/humu.1380010602openalex-snapshot
Molecular genetics of the LDL receptor gene in familial hypercholesterolemia
inferred← citeshttps://doi.org/10.1002/ijc.11659openalex-snapshot
Dynamic and intracellular trafficking of P‐glycoprotein‐EGFP fusion protein: Implications in multidrug resistance in cancer
inferred← citeshttps://doi.org/10.1002/ijc.2910560224openalex-snapshot
Immunoselection of GRP94/endoplasmin from a KNRK cell‐specific λGTLL library using antibodies directed against a putative heparanase amino‐terminal peptide
inferred← citeshttps://doi.org/10.1002/ijc.2910560319openalex-snapshot
Expression of the 100‐kDa glucose‐regulated protein (grp100/endoplasmin) is associated with tumorigenicity in a model of rat colon adenocarcinoma
inferred← citeshttps://doi.org/10.1002/iub.2331openalex-snapshot
Anterior gradient 2 promotes tumorigenesis through upregulation of CCAAT‐enhancer binding protein beta and hypoxia‐inducible factor‐2α and subsequent secretion of interleukin‐6, interleukin‐8, and vascular endothelial growth factor in the Caki‐1 clear cell renal cell carcinoma cell line
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1992.tb05323.xopenalex-snapshot
A 22 bp cis‐acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1992.tb05434.xopenalex-snapshot
Interaction of heat‐shock protein 70 with p53 translated in vitro: evidence for interaction with dimeric p53 and for a role in the regulation of p53 conformation.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1992.tb05581.xopenalex-snapshot
Chaperonin‐mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1992.tb05582.xopenalex-snapshot
Function in protein folding of TRiC, a cytosolic ring complex containing TCP‐1 and structurally related subunits.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1992.tb05584.xopenalex-snapshot
Role of ATP in the intramitochondrial sorting of cytochrome c1 and the adenine nucleotide translocator.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1993.tb05683.xopenalex-snapshot
Recognition of the Xenopus ribosomal core promoter by the transcription factor xUBF involves multiple HMG box domains and leads to an xUBF interdomain interaction.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1993.tb05729.xopenalex-snapshot
A novel multicopy suppressor of a groEL mutation includes two nested open reading frames transcribed from different promoters.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1993.tb05863.xopenalex-snapshot
Membrane glycoprotein folding, oligomerization and intracellular transport: effects of dithiothreitol in living cells.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1993.tb05952.xopenalex-snapshot
One member of a gro‐ESL‐like chaperonin multigene family in Bradyrhizobium japonicum is co‐regulated with symbiotic nitrogen fixation genes.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1993.tb05983.xopenalex-snapshot
Tumor rejection antigen gp96/grp94 is an ATPase: implications for protein folding and antigen presentation.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1993.tb05984.xopenalex-snapshot
Novel proteins associated with MHC class I antigens in cells expressing the adenovirus protein E3/19K.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1993.tb06054.xopenalex-snapshot
The heat shock cognate protein from Dictyostelium affects actin polymerization through interaction with the actin‐binding protein cap32/34.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1993.tb06097.xopenalex-snapshot
DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat‐induced protein damage.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06251.xopenalex-snapshot
RNA annealing activities in HeLa nuclei.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06306.xopenalex-snapshot
A role for calnexin (IP90) in the assembly of class II MHC molecules.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06308.xopenalex-snapshot
Antibody fragments from a ‘single pot’ phage display library as immunochemical reagents.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06338.xopenalex-snapshot
Association with BiP and aggregation of class II MHC molecules synthesized in the absence of invariant chain.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06339.xopenalex-snapshot
Chaperone activity of alpha‐crystallins modulates intermediate filament assembly.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06371.xopenalex-snapshot
Stch encodes the ‘ATPase core’ of a microsomal stress 70 protein.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06433.xopenalex-snapshot
The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06618.xopenalex-snapshot
Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha‐lactalbumin.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06670.xopenalex-snapshot
Folding of firefly luciferase during translation in a cell‐free system.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06843.xopenalex-snapshot
Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06940.xopenalex-snapshot
Immunophilins interact with calcineurin in the absence of exogenous immunosuppressive ligands.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06954.xopenalex-snapshot
Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1995.tb00150.xopenalex-snapshot
Soluble constituents of the ER lumen are required for GPI anchoring of a model protein.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1995.tb00177.xopenalex-snapshot
A ribosome‐associated peptidyl‐prolyl cis/trans isomerase identified as the trigger factor.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1995.tb00290.xopenalex-snapshot
Trigger factor is involved in GroEL‐dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1995.tb00291.xopenalex-snapshot
In vivo reactivation of heat‐denatured protein in the endoplasmic reticulum of yeast.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1995.tb07092.xopenalex-snapshot
In vivo iodination of a misfolded proinsulin reveals co‐localized signals for Bip binding and for degradation in the ER.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1995.tb07120.xopenalex-snapshot
Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1995.tb07221.xopenalex-snapshot
39 kDa receptor‐associated protein is an ER resident protein and molecular chaperone for LDL receptor‐related protein.
showing the first 200 of 3977
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.