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The expanding small heat-shock protein family, and structure predictions of the conserved “α-crystallin domain”
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/dvg.1020140109openalex-snapshot
hsp23 and hsp26 exhibit distinct spatial and temporal patterns of constitutive expression in Drosophila adults
inferredcites →https://doi.org/10.1002/dvg.1020140204openalex-snapshot
Development and tissue‐specific distribution of mouse small heat shock protein hsp25
inferredcites →https://doi.org/10.1002/j.1460-2075.1994.tb06339.xopenalex-snapshot
Chaperone activity of alpha‐crystallins modulates intermediate filament assembly.
inferredcites →https://doi.org/10.1002/prot.340200303openalex-snapshot
Conservation and prediction of solvent accessibility in protein families
inferredcites →https://doi.org/10.1006/exer.1994.1089openalex-snapshot
A Partial cDNA Sequence Corrects the Human αA-Crystallin Primary Structure
inferredcites →https://doi.org/10.1006/jmbi.1993.1413openalex-snapshot
Prediction of Protein Secondary Structure at Better than 70% Accuracy
inferredcites →https://doi.org/10.1007/978-3-642-73163-1_31openalex-snapshot
Developmental Expression of Heat Shock Proteins in Higher Plants
inferredcites →https://doi.org/10.1007/bf00016072openalex-snapshot
Alfalfa heat shock genes are differentially expressed during somatic embryogenesis
inferredcites →https://doi.org/10.1007/bf00019209openalex-snapshot
Two rice (Oryza sativa) full-length cDNA clones encoding low-molecular-weight heat-shock proteins
inferredcites →https://doi.org/10.1007/bf00019220openalex-snapshot
An Arabidopsis thaliana cDNA clone encoding a 17.6 kDa class II heat shock protein
inferredcites →https://doi.org/10.1007/bf00027074openalex-snapshot
Developmental and environmental concurrent expression of sunflower dry-seed-stored low-molecular-weight heat-shock protein and Lea mRNAs
inferredcites →https://doi.org/10.1007/bf00039500openalex-snapshot
Nucleotide sequence of a Triticum aestivum cDNA clone which is homologous to the 26 kDa chloroplast-localized heat shock protein gene of maize
inferredcites →https://doi.org/10.1007/bf00160214openalex-snapshot
Phylogeny of the ?-crystallin-related heat-shock proteins
inferredcites →https://doi.org/10.1007/bf00260655openalex-snapshot
Analysis of conserved domains identifies a unique structural feature of a chloroplast heat shock protein
inferredcites →https://doi.org/10.1007/bf01674432openalex-snapshot
Comparison of the homologous carboxy-terminal domain and tail of α-crystallin and small heat shock protein
inferredcites →https://doi.org/10.1016/0014-4835(74)90071-2openalex-snapshot
Circular dichroism and optical rotatory dispersion of the aggregates of purified polypeptides of alpha-crystallin
inferredcites →https://doi.org/10.1016/0014-4835(91)90119-yopenalex-snapshot
Truncation of α A-crystallin from the human lens
inferredcites →https://doi.org/10.1016/0014-4835(92)90014-jopenalex-snapshot
Crystallin gene expression in the process of lentoidogenesis in cultures of chicken lens epithelial cells
inferredcites →https://doi.org/10.1016/0014-5793(85)81102-9openalex-snapshot
Domain structure and evolution in α‐crystallins and small heat‐shock proteins
inferredcites →https://doi.org/10.1016/0014-5793(92)81386-zopenalex-snapshot
Identification by 1H NMR spectroscopy of flexible C‐terminal extensions in bovine lens α‐crystallin
inferredcites →https://doi.org/10.1016/0022-2836(83)90041-4openalex-snapshot
Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure
inferredcites →https://doi.org/10.1016/0022-2836(88)90300-2openalex-snapshot
Nucleotide sequence analysis of soybean small heat shock protein genes belonging to two different multigene families
inferredcites →https://doi.org/10.1016/0092-8674(83)90299-4openalex-snapshot
Accumulation of a specific subset of D. melanogaster heat shock mRNAs in normal development without heat shock
inferredcites →https://doi.org/10.1016/0166-6851(86)90021-6openalex-snapshot
Sequence and expression of a major egg antigen from Schistosoma mansoni. Homologies to heat shock proteins and alpha-crystallins
inferredcites →https://doi.org/10.1016/0166-6851(92)90073-sopenalex-snapshot
A stage-specific calcium-binding protein expressed in eggs of Schistosoma mansoni
inferredcites →https://doi.org/10.1016/0166-6851(93)90102-4openalex-snapshot
Cloning of a cDNA encoding an egg antigen homologue from Schistosoma mansoni
inferredcites →https://doi.org/10.1016/0166-6851(93)90168-wopenalex-snapshot
The expression of a small heat shock protein homologue is developmentally regulated in Nippostrongylus brasiliensis
inferredcites →https://doi.org/10.1016/0167-4838(91)90146-qopenalex-snapshot
Immunoreactive αA crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method
inferredcites →https://doi.org/10.1016/0168-9452(94)90054-xopenalex-snapshot
Isolation, sequence and expression of a cDNA encoding a Class I heat shock protein (HSP17.2) in maize
inferredcites →https://doi.org/10.1016/0305-0491(86)90223-3openalex-snapshot
Isolation and characterization of a 29,000 Dalton protein from ascidian (Halocynthia roretzi) body wall muscle
inferredcites →https://doi.org/10.1016/0378-1119(93)90574-mopenalex-snapshot
Cloning of the mouse hsp25 gene and an extremely conserved hsp25 pseudogene
inferredcites →https://doi.org/10.1016/0378-1119(93)90575-nopenalex-snapshot
Structure and organisation of a murine gene encoding small heat-shock protein Hsp25
inferredcites →https://doi.org/10.1016/0968-0004(94)90065-5openalex-snapshot
The biology of heat shock proteins and molecular chaperones
inferredcites →https://doi.org/10.1016/b978-1-4832-3211-9.50009-7openalex-snapshot
Evolution of Protein Molecules
inferredcites →https://doi.org/10.1016/s0006-291x(89)80215-3openalex-snapshot
αB subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissues
inferredcites →https://doi.org/10.1016/s0021-9258(17)36606-1openalex-snapshot
Purification and characterization of a 20-kDa protein that is highly homologous to alpha B crystallin.
inferredcites →https://doi.org/10.1016/s0021-9258(17)37131-4openalex-snapshot
Differential estrogenic regulation of small M(r) heat shock protein expression in osteoblasts.
inferredcites →https://doi.org/10.1016/s0021-9258(18)53882-5openalex-snapshot
Small heat shock proteins are molecular chaperones.
inferredcites →https://doi.org/10.1016/s0021-9258(18)54039-4openalex-snapshot
Structural and functional similarities of bovine alpha-crystallin and mouse small heat-shock protein. A family of chaperones.
inferredcites →https://doi.org/10.1016/s0021-9258(18)60691-xopenalex-snapshot
Dogfish alpha-crystallin sequences. Comparison with small heat shock proteins and Schistosoma egg antigen.
inferredcites →https://doi.org/10.1017/cbo9780511622434.009openalex-snapshot
Structure and organization
inferredcites →https://doi.org/10.1038/368032a0openalex-snapshot
2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans
inferredcites →https://doi.org/10.1073/pnas.79.7.2360openalex-snapshot
Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin.
inferredcites →https://doi.org/10.1073/pnas.88.9.3652openalex-snapshot
Alpha B-crystallin is a small heat shock protein.
inferredcites →https://doi.org/10.1073/pnas.89.21.10449openalex-snapshot
Alpha-crystallin can function as a molecular chaperone.
inferredcites →https://doi.org/10.1083/jcb.109.1.7openalex-snapshot
Heat shock resistance conferred by expression of the human HSP27 gene in rodent cells.
inferredcites →https://doi.org/10.1083/jcb.114.2.255openalex-snapshot
A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein.
inferredcites →https://doi.org/10.1093/bioinformatics/10.1.53openalex-snapshot
PHD-an automatic mail server for protein secondary structure prediction
inferredcites →https://doi.org/10.1093/nar/14.10.4127openalex-snapshot
Sequence and organization of genes encoding the human 27 kDa heat shock protein
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a123665openalex-snapshot
αB-Crystallin in Skeletal Muscle: Purification and Localization1
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a124046openalex-snapshot
Structure of 29-kDa Protein from Ascidian(Halocynthia roretzi) Body Wall Muscle1
inferredcites →https://doi.org/10.1093/oxfordjournals.molbev.a039992openalex-snapshot
Evolution of the alpha-crystallin/small heat-shock protein family.
inferredcites →https://doi.org/10.1093/oxfordjournals.molbev.a040454openalex-snapshot
The neighbor-joining method: a new method for reconstructing phylogenetic trees.
inferredcites →https://doi.org/10.1101/087969427.26.335openalex-snapshot
14 Expression and Function of the Low-molecular-weight Heat Shock Proteins
inferredcites →https://doi.org/10.1104/pp.100.4.1772openalex-snapshot
Structure and Light-Induced Expression of a Small Heat-Shock Protein Gene of Pharbitis nil
inferredcites →https://doi.org/10.1104/pp.93.4.1626openalex-snapshot
Heat Shock Proteins and Their mRNAs in Dry and Early Imbibing Embryos of Wheat
inferredcites →https://doi.org/10.1111/j.1365-3040.1990.tb01299.xopenalex-snapshot
Heat shock proteins in Sorghum bicolor and Pennisetum americanum. II. Stored RNA in sorghum seed and its relationship to heat shock protein synthesis during germination
inferredcites →https://doi.org/10.1111/j.1432-1033.1984.tb08167.xopenalex-snapshot
Primary structures of the α‐crystallin A chains of twenty‐eight mammalian species, chicken and frog
inferredcites →https://doi.org/10.1111/j.1432-1033.1993.tb18032.xopenalex-snapshot
Analysis of the resistance to heat and hydrogen peroxide stresses in COS cells transiently expressing wild type or deletion mutants of the Drosophila 27‐kDa heat‐shock protein
inferredcites →https://doi.org/10.1111/j.1432-1033.1994.00001.xopenalex-snapshot
Structure and Modifications of the Junior Chaperone α‐Crystallin
inferredcites →https://doi.org/10.1126/science.155.3760.279openalex-snapshot
Construction of Phylogenetic Trees
inferredcites →https://doi.org/10.1126/science.3511530openalex-snapshot
An Ancient Developmental Induction: Heat-Shock Proteins Induced in Sporulation and Oogenesis
inferredcites →https://doi.org/10.1128/jb.170.12.5919-5921.1988openalex-snapshot
A protein antigen of Mycobacterium leprae is related to a family of small heat shock proteins
inferredcites →https://doi.org/10.1128/jb.174.21.6938-6947.1992openalex-snapshot
Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli
inferredcites →https://doi.org/10.1128/jb.174.4.1352-1359.1992openalex-snapshot
The 14,000-molecular-weight antigen of Mycobacterium tuberculosis is related to the alpha-crystallin family of low-molecular-weight heat shock proteins
inferredcites →https://doi.org/10.1128/jb.175.11.3394-3400.1993openalex-snapshot
Sequence and molecular characterization of a DNA region encoding a small heat shock protein of Clostridium acetobutylicum
inferredcites →https://doi.org/10.1128/jb.175.22.7479-7482.1993openalex-snapshot
Heat shock and development induce synthesis of a low-molecular-weight stress-responsive protein in the myxobacterium Stigmatella aurantiaca
inferredcites →https://doi.org/10.1128/jb.175.3.905-908.1993openalex-snapshot
Purification and characterization of SP21, a development-specific protein of the myxobacterium Stigmatella aurantiaca
inferredcites →https://doi.org/10.1128/mcb.13.1.238openalex-snapshot
Localization of Small Heat Shock Proteins to the Higher Plant Endomembrane System
inferredcites →https://doi.org/10.1128/mcb.7.3.973openalex-snapshot
The ovarian, ecdysterone, and heat-shock-responsive promoters of the Drosophila melanogaster hsp27 gene react very differently to perturbations of DNA sequence.
inferredcites →https://doi.org/10.1128/mcb.7.3.973-981.1987openalex-snapshot
The Ovarian, Ecdysterone, and Heat-Shock-Responsive Promoters of the Drosophila melanogaster hsp27 Gene React Very Differently to Perturbations of DNA Sequence
inferredcites →https://doi.org/10.1128/mcb.9.11.5265openalex-snapshot
hsp26 of Saccharomyces cerevisiae is related to the superfamily of small heat shock proteins but is without a demonstrable function.
inferredcites →https://doi.org/10.1128/mcb.9.11.5265-5271.1989openalex-snapshot
hsp26 of Saccharomyces cerevisiae Is Related to the Superfamily of Small Heat Shock Proteins but Is without a Demonstrable Function
inferredcites →https://doi.org/10.1128/mcb.9.3.1298openalex-snapshot
Cytoplasmic Heat Shock Granules Are Formed from Precursor Particles and Are Associated with a Specific Set of mRNAs
inferredcites →https://doi.org/10.1139/g89-126openalex-snapshot
Structure, organization, and expression of the 16-kDa heat shock gene family of Caenorhabditis elegans
inferredcites →https://doi.org/10.1139/g90-012openalex-snapshot
Characterization of expressed meiotic prophase repeat transcript clones of Lilium: meiosis-specific expression, relatedness, and affinities to small heat shock protein genes
inferredcites →https://doi.org/10.1146/annurev.arplant.42.1.579openalex-snapshot
The Roles Of Heat Shock Proteins In Plants
inferredcites →https://doi.org/10.1146/annurev.bb.17.060188.000403openalex-snapshot
Eye Lens Proteins and Transparency: From Light Transmission Theory to Solution X-Ray Structural Analysis
inferredcites →https://doi.org/10.1146/annurev.bi.57.070188.002403openalex-snapshot
LENS CRYSTALLINS: THE EVOLUTION AND EXPRESSION OF PROTEINS FOR A HIGHLY SPECIALIZED TISSUE
inferredcites →https://doi.org/10.1146/annurev.bi.62.070193.002025openalex-snapshot
MOLECULAR CHAPERONE FUNCTIONS OF HEAT-SHOCK PROTEINS
inferredcites →https://doi.org/10.1146/annurev.ge.22.120188.003215openalex-snapshot
THE HEAT-SHOCK PROTEINS
inferredcites →https://doi.org/10.1146/annurev.pp.42.060191.003051openalex-snapshot
The Roles of Heat Shock Proteins in Plants
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.4772706openalex-extracted
Unraveling the Existence of Different Oligomeric Forms of E. Coli Small Heat-Shock Protein Ibpb Under Heat Stress and the Most Functional Oligomers with Respect to Holding Chaperone Activity
inferred← citeshttps://doi.org/10.1002/1873-3468.15019openalex-snapshot
Two new oligomers of E. coli small heat‐shock protein IbpB identified under heat stress exhibit maximum holding chaperone activity
inferred← citeshttps://doi.org/10.1002/2211-5463.12726openalex-snapshot
Functional and structural characterization of HspB1/Hsp27 from Chinese hamster ovary cells
inferred← citeshttps://doi.org/10.1002/9781118063903.ch1openalex-snapshot
Intrinsically Disordered Chaperones and Neurodegeneration
inferred← citeshttps://doi.org/10.1002/9781119004813.ch71openalex-snapshot
Small Heat Shock Proteins in Bacteria
inferred← citeshttps://doi.org/10.1002/9783527619498.ch57openalex-snapshot
Small Heat Shock Proteins: Dynamic Players in the Folding Game
inferred← citeshttps://doi.org/10.1002/adfm.202315509openalex-snapshot
Protein‐Based Controllable Nanoarchitectonics for Desired Applications
inferred← citeshttps://doi.org/10.1002/ana.106openalex-snapshot
Abnormal desmin protein in myofibrillar myopathies caused by desmin gene mutations
inferred← citeshttps://doi.org/10.1002/bip.20716openalex-snapshot
Structure, stability, and chaperone function of αA‐crystallin: Role of N‐terminal region
inferred← citeshttps://doi.org/10.1002/jcb.20445openalex-snapshot
Endoplasmic reticulum stress induces the phosphorylation of small heat shock protein, Hsp27
inferred← citeshttps://doi.org/10.1002/jnr.21231openalex-snapshot
Structure, function, property, and role in neurologic diseases and other diseases of the sHsp22
inferred← citeshttps://doi.org/10.1002/mc.23133openalex-snapshot
Heat shock protein beta 3 (HSPB3) is an unfavorable molecular biomarker in colorectal adenocarcinoma
inferred← citeshttps://doi.org/10.1002/pro.761openalex-snapshot
Roles of the N‐ and C‐terminal sequences in Hsp27 self‐association and chaperone activity
inferred← citeshttps://doi.org/10.1002/prot.22132openalex-snapshot
Characterization of a sHsp of Schizosaccharomyces pombe, SpHsp15.8, and the implication of its functional mechanism by comparison with another sHsp, SpHsp16.0
inferred← citeshttps://doi.org/10.1002/prot.22261openalex-snapshot
Chaperone action of a versatile small heat shock protein from Methanococcoides burtonii, a cold adapted archaeon
inferred← citeshttps://doi.org/10.1002/ps.7941openalex-snapshot
Sequential expression of small heat shock proteins contributing to the cold response of Haemaphysalis longicornis ( Acari: Ixodidae )
inferred← citeshttps://doi.org/10.1002/tox.22772openalex-snapshot
Small heat shock protein genes of the green algae Closterium ehrenbergii: Cloning and differential expression under heat and heavy metal stresses
inferred← citeshttps://doi.org/10.1006/abbi.1999.1177openalex-snapshot
Evidence for a Novel Set of Small Heat-Shock Proteins That Associates with the Mitochondria of Murine PC12 Cells and Protects NADH:Ubiquinone Oxidoreductase from Heat and Oxidative Stress
inferred← citeshttps://doi.org/10.1006/bbrc.1998.8699openalex-snapshot
Phosphorylation of αB-Crystallin and HSP27 Is Induced by Similar Stressors in HeLa Cells
inferred← citeshttps://doi.org/10.1006/bbrc.2001.5074openalex-snapshot
Preheat Treatment for Mycobacterium tuberculosis Hsp16.3: Correlation between a Structural Phase Change at 60°C and a Dramatic Increase in Chaperone-like Activity
inferred← citeshttps://doi.org/10.1006/dbio.1998.9138openalex-snapshot
The Synthesis of a Small Heat Shock/α-Crystallin Protein inArtemiaand Its Relationship to Stress Tolerance during Development
inferred← citeshttps://doi.org/10.1006/excr.2001.5220openalex-snapshot
Regulation of the Levels of Small Heat-Shock Proteins during Differentiation of C2C12 Cells
inferred← citeshttps://doi.org/10.1006/jmbi.1997.1611openalex-snapshot
The small heat-shock protein, αb-crystallin, has a variable quaternary structure
inferred← citeshttps://doi.org/10.1006/jmbi.1999.2759openalex-snapshot
Site-directed mutations within the core “α-crystallin” domain of the small heat-shock protein, human αB-crystallin, decrease molecular chaperone functions
inferred← citeshttps://doi.org/10.1006/jmbi.1999.3242openalex-snapshot
Folding pattern of the α-crystallin domain in αA-crystallin determined by site-directed spin labeling
inferred← citeshttps://doi.org/10.1006/jsbi.1998.3969openalex-snapshot
Purification, Crystallization, and Preliminary X-Ray Crystallographic Data Analysis of Small Heat Shock Protein Homolog fromMethanococcus jannaschii,a Hyperthermophile
inferred← citeshttps://doi.org/10.1006/mpev.1996.0384openalex-snapshot
α-Crystallin Sequences Support a Galliform/Anseriform Clade
inferred← citeshttps://doi.org/10.1007/3-540-27998-9_14openalex-snapshot
Molecular chaperones—holding and folding
inferred← citeshttps://doi.org/10.1007/978-3-030-28151-9_14openalex-snapshot
Crystallins and Their Complexes
inferred← citeshttps://doi.org/10.1007/978-3-319-16077-1_1openalex-snapshot
The Multicolored World of the Human HSPB Family
inferred← citeshttps://doi.org/10.1007/978-3-319-16077-1_6openalex-snapshot
Regulation of the Chaperone Function of Small Hsps
inferred← citeshttps://doi.org/10.1007/978-3-319-46340-7_13openalex-snapshot
Molecular Chaperones and HSPs in Sugarcane and Eucalyptus
inferred← citeshttps://doi.org/10.1007/978-3-319-90725-3_14openalex-snapshot
Small Heat Shock Proteins in Stress Response of Higher Eukaryotes
inferred← citeshttps://doi.org/10.1007/978-3-642-56348-5_1openalex-snapshot
Evolution and Diversity of Prokaryotic Small Heat Shock Proteins
inferred← citeshttps://doi.org/10.1007/978-3-642-56348-5_4openalex-snapshot
The Small Heat Shock Proteins of the Nematode Caenorhabditis elegans: Structure, Regulation and Biology
inferred← citeshttps://doi.org/10.1007/978-3-642-56348-5_7openalex-snapshot
Expression and Phosphorylation of Mammalian Small Heat Shock Proteins
inferred← citeshttps://doi.org/10.1007/978-94-007-5899-5_14openalex-snapshot
Molecular Chaperones in Thermophilic Eubacteria and Archaea
inferred← citeshttps://doi.org/10.1007/978-94-017-0255-3_1openalex-snapshot
Plant Tolerance to Heat Stress: Current Strategies and New Emergent Insights
inferred← citeshttps://doi.org/10.1007/bf00986495openalex-snapshot
α-Crystallins, versatile stress-proteins
inferred← citeshttps://doi.org/10.1007/bf02352288openalex-snapshot
Protein sequences indicate that turtles branched off from the amniote tree after mammals
inferred← citeshttps://doi.org/10.1007/bf02936122openalex-snapshot
Heat induced stress proteins and the concept of molecular chaperones
inferred← citeshttps://doi.org/10.1007/bf03030450openalex-snapshot
Genes and expression pattern of tobacco mitochondrial small heat shock protein under high-temperature stress
inferred← citeshttps://doi.org/10.1007/bf03030571openalex-snapshot
Functional mode of NtHSP17.6, a cytosolic small heat-shock protein fromNicotiana tabacum
inferred← citeshttps://doi.org/10.1007/pl00000583openalex-snapshot
Heat stress proteins and transcription factors
inferred← citeshttps://doi.org/10.1007/pl00000733openalex-snapshot
Structure and function of small heat shock/α-crystallin proteins: established concepts and emerging ideas
inferred← citeshttps://doi.org/10.1007/s00018-003-3024-9openalex-snapshot
Hsp27 suppresses the formation of inclusion bodies induced by expression of R120GαB-crystallin, a cause of desmin-related myopathy
inferred← citeshttps://doi.org/10.1007/s00018-008-8327-4openalex-snapshot
Crystallin proteins and amyloid fibrils
inferred← citeshttps://doi.org/10.1007/s00239-006-0223-7openalex-snapshot
Evolutionary Analysis of the Small Heat Shock Proteins in Five Complete Algal Genomes
inferred← citeshttps://doi.org/10.1007/s00253-007-1228-xopenalex-snapshot
Improved adaptation to heat, cold, and solvent tolerance in Lactobacillus plantarum
inferred← citeshttps://doi.org/10.1007/s00284-020-02168-zopenalex-snapshot
Identification and Characterization of the Small Heat Shock Protein Hsp20 from Oenococcus oeni SD-2a
inferred← citeshttps://doi.org/10.1007/s00343-014-3111-9openalex-snapshot
Expression profiles of two small heat shock proteins and antioxidant enzyme activity in Mytilus galloprovincialis exposed to cadmium at environmentally relevant concentrations
inferred← citeshttps://doi.org/10.1007/s00401-005-0030-zopenalex-snapshot
Small heat shock protein HspB8: its distribution in Alzheimer’s disease brains and its inhibition of amyloid-β protein aggregation and cerebrovascular amyloid-β toxicity
inferred← citeshttps://doi.org/10.1007/s004360050422openalex-snapshot
Sequence and preliminary characterisation of a Taenia saginata oncosphere gene homologue of the small heat-shock protein family
inferred← citeshttps://doi.org/10.1007/s004970050117openalex-snapshot
A cDNA clone from hazelnut ( Corylus avellana L.) encoding a low molecular weight heat shock protein expressed in the reproductive structures
inferred← citeshttps://doi.org/10.1007/s00726-005-0377-4openalex-snapshot
The necessity of functional proteomics: protein species and molecular function elucidation exemplified by in vivo alpha A crystallin N-terminal truncation
inferred← citeshttps://doi.org/10.1007/s00792-002-0298-zopenalex-snapshot
Multi-subunit assembly of the Pyrococcus furiosus small heat shock protein is essential for cellular protection at high temperature
inferred← citeshttps://doi.org/10.1007/s00792-003-0362-3openalex-snapshot
Small heat shock proteins from extremophiles: a review
inferred← citeshttps://doi.org/10.1007/s10142-026-01920-1openalex-snapshot
Transcriptional insights into molecular events occurring during tuber maturation of tigernut (Cyperus esculentus L.)
inferred← citeshttps://doi.org/10.1007/s10545-015-9813-0openalex-snapshot
Bi‐allelic CLPB mutations cause cataract, renal cysts, nephrocalcinosis and 3‐methylglutaconic aciduria, a novel disorder of mitochondrial protein disaggregation
inferred← citeshttps://doi.org/10.1007/s10709-007-9215-9openalex-snapshot
A comparative genomic analysis of the small heat shock proteins in Caenorhabditis elegans and briggsae
inferred← citeshttps://doi.org/10.1007/s10811-022-02686-2openalex-snapshot
Identification and expression profiling of HSP20 genes in Neoporphyra haitanensis
inferred← citeshttps://doi.org/10.1007/s11010-011-1131-8openalex-snapshot
Quaternary structural parameters of the congenital cataract causing mutants of αA-crystallin
inferred← citeshttps://doi.org/10.1007/s11103-009-9477-yopenalex-snapshot
Comprehensive sequence and expression profile analysis of Hsp20 gene family in rice
inferred← citeshttps://doi.org/10.1007/s11627-997-0040-8openalex-snapshot
induction of heat shock response and acquisition of thermotolerance in callus cultures of Gerbera jamesonii
inferred← citeshttps://doi.org/10.1007/s11738-997-0051-4openalex-snapshot
The small heat shock proteins in plants are members of an ancient family of heat induced proteins
inferred← citeshttps://doi.org/10.1007/s12010-009-8809-3openalex-snapshot
Isolation, Purification, and Properties of a Novel Small Heat Shock Protein from the Hyperthermophile Sulfolobus solfataricus
inferred← citeshttps://doi.org/10.1007/s12010-015-1598-yopenalex-snapshot
Molecular Cloning and Differential Expression of Cytosolic Class I Small Hsp Gene Family in Pennisetum glaucum (L.)
inferred← citeshttps://doi.org/10.1007/s12192-008-0023-7openalex-snapshot
Comparative analysis of the small heat shock proteins in three angiosperm genomes identifies new subfamilies and reveals diverse evolutionary patterns
inferred← citeshttps://doi.org/10.1007/s12192-011-0299-xopenalex-snapshot
Characterisation of the Plasmodium falciparum Hsp70–Hsp90 organising protein (PfHop)
inferred← citeshttps://doi.org/10.1007/s12192-016-0748-7openalex-snapshot
Oligomerization and chaperone-like activity of Drosophila melanogaster small heat shock protein DmHsp27 and three arginine mutants in the alpha-crystallin domain
inferred← citeshttps://doi.org/10.1007/s12192-017-0787-8openalex-snapshot
The growing world of small heat shock proteins: from structure to functions
inferred← citeshttps://doi.org/10.1007/s12192-018-0947-5openalex-snapshot
Induced expression of small heat shock proteins is associated with thermotolerance in female Laodelphax striatellus planthoppers
inferred← citeshttps://doi.org/10.1007/s12192-019-00979-zopenalex-snapshot
Small heat shock proteins: multifaceted proteins with important implications for life
inferred← citeshttps://doi.org/10.1007/s12192-020-01096-yopenalex-snapshot
Studying heat shock proteins through single-molecule mechanical manipulation
inferred← citeshttps://doi.org/10.1007/s12192-020-01156-3openalex-snapshot
Analysis of insect nuclear small heat shock proteins and interacting proteins
inferred← citeshttps://doi.org/10.1007/s12192-022-01308-7openalex-snapshot
Is the lipochaperone activity of sHSP a key to the stress response encoded in its primary sequence?
inferred← citeshttps://doi.org/10.1007/s12892-010-0119-3openalex-snapshot
Importance of heat shock proteins in maize
inferred← citeshttps://doi.org/10.1016/0378-1119(96)00356-3openalex-snapshot
cDNA cloning of a 20-kDa protein (p20) highly homologous to small heat shock proteins: developmental and physiological changes in rat hindlimb muscles
inferred← citeshttps://doi.org/10.1016/b978-0-12-401717-7.00050-2openalex-snapshot
Acetyl-L-Carnitine as a Nutraceutical Agent in Preventing Selenite-Induced Cataract
inferred← citeshttps://doi.org/10.1016/b978-0-12-819311-2.00008-5openalex-snapshot
Molecular chaperones in protein folding and stress management in cyanobacteria
inferred← citeshttps://doi.org/10.1016/j.bbagen.2015.06.008openalex-snapshot
Structure and function of α-crystallins: Traversing from in vitro to in vivo
inferred← citeshttps://doi.org/10.1016/j.bbrc.2004.01.031openalex-snapshot
Role of the N-terminal region of the crenarchaeal sHsp, StHsp14.0, in thermal-induced disassembly of the complex and molecular chaperone activity
inferred← citeshttps://doi.org/10.1016/j.biocel.2007.01.014openalex-snapshot
Biochemical and biophysical characterization of small heat shock proteins from sugarcane
inferred← citeshttps://doi.org/10.1016/j.biocel.2012.03.011openalex-snapshot
The family of mammalian small heat shock proteins (HSPBs): Implications in protein deposit diseases and motor neuropathies
inferred← citeshttps://doi.org/10.1016/j.biocel.2012.06.006openalex-snapshot
Small heat shock proteins in redox metabolism: Implications for cardiovascular diseases
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2008.08.004openalex-snapshot
Microbial small heat shock proteins and their use in biotechnology
inferred← citeshttps://doi.org/10.1016/j.brainres.2006.03.058openalex-snapshot
Small heat shock proteins inhibit amyloid-β protein aggregation and cerebrovascular amyloid-β protein toxicity
inferred← citeshttps://doi.org/10.1016/j.cbd.2008.02.002openalex-snapshot
Molecular diversity and genomic organisation of the α, β and γ eye lens crystallins from the Antarctic toothfish Dissostichus mawsoni
inferred← citeshttps://doi.org/10.1016/j.exppara.2004.11.014openalex-snapshot
Taenia solium: characterization of a small heat shock protein (Tsol-sHSP35.6) and its possible relevance to the diagnosis and pathogenesis of neurocysticercosis
inferred← citeshttps://doi.org/10.1016/j.exppara.2007.01.004openalex-snapshot
Preliminary analysis of cold stress responsive proteins in Mesocestoides corti larvae
inferred← citeshttps://doi.org/10.1016/j.exppara.2008.01.020openalex-snapshot
Babesia divergens: Identification and characterization of BdHSP-20, a small heat shock protein
inferred← citeshttps://doi.org/10.1016/j.exppara.2011.05.010openalex-snapshot
Taenia solium: A two-dimensional Western blotting method combined with the use of an EST-library for the identification of immunogenic proteins recognized by sera from neurocysticercosis patients
inferred← citeshttps://doi.org/10.1016/j.gene.2008.01.006openalex-snapshot
Comprehensive sequence and expression profile analysis of PEX11 gene family in rice
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2018.06.004openalex-snapshot
3D structure of the native α-crystallin from bovine eye lens
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2019.08.178openalex-snapshot
The mechanism of the interaction of α-crystallin and UV-damaged βL-crystallin
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2021.07.186openalex-snapshot
Characterization and functional analysis of Cshsp19.0 encoding a small heat shock protein in Chilo suppressalis (Walker)
inferred← citeshttps://doi.org/10.1016/j.isci.2025.112640openalex-snapshot
Functional proteomic insights into the lateral oviduct-associated secretions of a bean bug
inferred← citeshttps://doi.org/10.1016/j.jmb.2004.10.056openalex-snapshot
Self-association of a Small Heat Shock Protein
inferred← citeshttps://doi.org/10.1016/j.jmb.2006.09.003openalex-snapshot
The β4-β8 Groove Is an ATP-interactive Site in the α Crystallin Core Domain of the Small Heat Shock Protein, Human αB Crystallin
inferred← citeshttps://doi.org/10.1016/j.jmb.2015.02.002openalex-snapshot
A First Line of Stress Defense: Small Heat Shock Proteins and Their Function in Protein Homeostasis
inferred← citeshttps://doi.org/10.1016/j.jspr.2024.102368openalex-snapshot
Molecular characterization and expression analysis of six small heat shock protein genes in Trogoderma granarium during cold and starvation-induced larval diapause
inferred← citeshttps://doi.org/10.1016/j.molbiopara.2008.02.010openalex-snapshot
A novel small heat shock protein 12.6 (HSP12.6) from Brugia malayi functions as a human IL-10 receptor binding protein
inferred← citeshttps://doi.org/10.1016/j.neurobiolaging.2007.06.001openalex-snapshot
Small heat shock proteins associated with cerebral amyloid angiopathy of hereditary cerebral hemorrhage with amyloidosis (Dutch type) induce interleukin-6 secretion
inferred← citeshttps://doi.org/10.1016/j.pep.2006.02.006openalex-snapshot
Purification and characterization of the chaperone-like Hsp26 from Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1016/j.plantsci.2011.03.004openalex-snapshot
Identification and expression analysis of two small heat shock protein cDNAs from developing seeds of biodiesel feedstock plant Jatropha curcas
inferred← citeshttps://doi.org/10.1016/j.preteyeres.2016.03.001openalex-snapshot
Heat shock proteins in the retina: Focus on HSP70 and alpha crystallins in ganglion cell survival
inferred← citeshttps://doi.org/10.1016/j.rvsc.2010.06.028openalex-snapshot
Variation in the expression of Hsp27, αB-crystallin mRNA and protein in heart and liver of pigs exposed to different transport times
inferred← citeshttps://doi.org/10.1016/j.semcdb.2007.10.003openalex-snapshot
Congenital cataracts and their molecular genetics
inferred← citeshttps://doi.org/10.1016/j.vetpar.2014.04.021openalex-snapshot
Molecular cloning and characterization of a novel heat shock protein 20 of Babesia orientalis
inferred← citeshttps://doi.org/10.1016/j.ygeno.2006.02.008openalex-snapshot
Diversity, structure, and expression of the gene for p26, a small heat shock protein from Artemia
inferred← citeshttps://doi.org/10.1016/j.ygeno.2026.111319openalex-snapshot
A chromosome-level genome assembly and developmental transcriptome profiling reveal stage-specific remodeling of the molecular chaperone system in Helicoverpa armigera
inferred← citeshttps://doi.org/10.1016/s0006-291x(02)02185-xopenalex-snapshot
C-terminal lysine truncation increases thermostability and enhances chaperone-like function of porcine αB-crystallin
inferred← citeshttps://doi.org/10.1016/s0006-291x(03)00257-2openalex-snapshot
Enhanced stability of αB-crystallin in the presence of small heat shock protein Hsp27
inferred← citeshttps://doi.org/10.1016/s0014-5793(00)02136-0openalex-snapshot
Interaction between β‐amyloid and lens αB‐crystallin
inferred← citeshttps://doi.org/10.1016/s0014-5793(02)02688-1openalex-snapshot
The determinants of the oligomeric structure in Hsp16.5 are encoded in the α‐crystallin domain
inferred← citeshttps://doi.org/10.1016/s0014-5793(97)00498-5openalex-snapshot
The hydrophobic probe 4,4′‐bis(1‐anilino‐8‐naphthalene sulfonic acid) is specifically photoincorporated into the N‐terminal domain of αB‐crystallin
inferred← citeshttps://doi.org/10.1016/s0022-2836(03)00356-5openalex-snapshot
Structural and Functional Defects Caused by Point Mutations in the α-Crystallin Domain of a Bacterial α-Heat Shock Protein
inferred← citeshttps://doi.org/10.1016/s0065-2164(01)50007-6openalex-snapshot
Protein folding and molecular chaperones in Archaea
inferred← citeshttps://doi.org/10.1016/s0065-3233(01)59004-xopenalex-snapshot
Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones
inferred← citeshttps://doi.org/10.1016/s0141-8130(98)00013-0openalex-snapshot
Genealogy of the α-crystallin—small heat-shock protein superfamily
inferred← citeshttps://doi.org/10.1016/s0141-8130(98)00014-2openalex-snapshot
The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25
inferred← citeshttps://doi.org/10.1016/s0141-8130(98)00019-1openalex-snapshot
α- C-terminal domain: on the track of an Ig fold
inferred← citeshttps://doi.org/10.1016/s0167-4838(00)00109-6openalex-snapshot
The small heat-shock chaperone protein, α-crystallin, does not recognise stable molten globule states of cytosolic proteins
inferred← citeshttps://doi.org/10.1016/s0167-4838(98)00172-1openalex-snapshot
Thiol/disulfide exchange between small heat shock protein 25 and glutathione
inferred← citeshttps://doi.org/10.1016/s0167-4838(99)00178-8openalex-snapshot
Eye lens αA- and αB-crystallin: complex stability versus chaperone-like activity
inferred← citeshttps://doi.org/10.1016/s0167-4889(98)00172-4openalex-snapshot
Glucose metabolism in Neurospora is altered by heat shock and by disruption of HSP30
inferred← citeshttps://doi.org/10.1016/s0168-9452(02)00027-4openalex-snapshot
Molecular characterization and evolution of the cytosolic class II 17.0 kDa small heat-shock protein gene family from Picea abies (L.) Karst
inferred← citeshttps://doi.org/10.1016/s0168-9452(98)00219-2openalex-snapshot
Triticum aestivum cDNAs homologous to nuclear-encoded mitochondrion-localized small heat shock proteins
inferred← citeshttps://doi.org/10.1016/s0306-9877(98)90004-4openalex-snapshot
Chromosomal fragility may be indicative of altered higher-order DNA organization as the underlying genetic diathesis in complex neurobehavioural disorders
inferred← citeshttps://doi.org/10.1016/s0378-1097(00)00038-0openalex-snapshot
Small heat shock proteins, IbpA and IbpB, are involved in resistances to heat and superoxide stresses in Escherichia coli
inferred← citeshttps://doi.org/10.1016/s1016-8478(23)13470-4openalex-snapshot
Comparison of the Structure and Expression Pattern for a Low Molecular Weight Heat-Shock Protein cDNA Clone from Nicotiana tabacum
inferred← citeshttps://doi.org/10.1016/s1350-9462(96)00018-3openalex-snapshot
X-ray diffraction and structure of crystallins
inferred← citeshttps://doi.org/10.1016/s1350-9462(98)00030-5openalex-snapshot
α-Crystallin as a molecular chaperone
inferred← citeshttps://doi.org/10.1016/s1389-1723(01)80218-8openalex-snapshot
Small Heat Shock Protein of a Hyperthermophilic Archaeum, Thermococcus sp. Strain KS-1, Exists as a Spherical 24 mer and Its Expression Is Highly Induced under Heat-Stress Conditions
inferred← citeshttps://doi.org/10.1021/acs.analchem.1c02282openalex-snapshot
Structural Probing of Hsp26 Activation and Client Binding by Quantitative Cross-Linking Mass Spectrometry
inferred← citeshttps://doi.org/10.1021/bi001882hopenalex-snapshot
Monomer−Dimer Equilibrium of Normal and Modified βA3-Crystallins: Experimental Determination and Molecular Modeling
inferred← citeshttps://doi.org/10.1021/bi030129wopenalex-snapshot
Influence of the C-Terminal Residues on Oligomerization of αA-Crystallin
inferred← citeshttps://doi.org/10.1021/bi034617fopenalex-snapshot
Energetics of Domain−Domain Interactions and Entropy Driven Association of β-Crystallins
inferred← citeshttps://doi.org/10.1021/bi060705zopenalex-snapshot
Role of Arginine-163 and the 163REEK166 Motif in the Oligomerization of Truncated αA-Crystallins
inferred← citeshttps://doi.org/10.1021/bi0618722openalex-snapshot
Cleavage of the C-Terminal Serine of Human αA-Crystallin Produces αA1-172with Increased Chaperone Activity and Oligomeric Size
inferred← citeshttps://doi.org/10.1021/bi200091qopenalex-snapshot
Binding of γ-Crystallin Substrate Prevents the Binding of Copper and Zinc Ions to the Molecular Chaperone α-Crystallin
inferred← citeshttps://doi.org/10.1021/bi2017624openalex-snapshot
Sequence, Structure, and Dynamic Determinants of Hsp27 (HspB1) Equilibrium Dissociation Are Encoded by the N-Terminal Domain
inferred← citeshttps://doi.org/10.1021/bi900212jopenalex-snapshot
Structure and Mechanism of Protein Stability Sensors: Chaperone Activity of Small Heat Shock Proteins
inferred← citeshttps://doi.org/10.1021/bi9712347openalex-snapshot
Structure and Function of the Conserved Domain in αA-Crystallin. Site-Directed Spin Labeling Identifies a β-Strand Located near a Subunit Interface
inferred← citeshttps://doi.org/10.1021/bi971700sopenalex-snapshot
Site-Directed Spin-Labeling Study of the Structure and Subunit Interactions along a Conserved Sequence in the α-Crystallin Domain of Heat-Shock Protein 27. Evidence of a Conserved Subunit Interface
inferred← citeshttps://doi.org/10.1021/bi9814078openalex-snapshot
Identification of Protein Folding Patterns Using Site-Directed Spin Labeling. Structural Characterization of a β-Sheet and Putative Substrate Binding Regions in the Conserved Domain of αA-Crystallin
inferred← citeshttps://doi.org/10.1021/cr100186dopenalex-snapshot
Flexible Nets of Malleable Guardians: Intrinsically Disordered Chaperones in Neurodegenerative Diseases
inferred← citeshttps://doi.org/10.1021/jacs.3c02022openalex-snapshot
Human Small Heat Shock Protein B8 Inhibits Protein Aggregation without Affecting the Native Folding Process
inferred← citeshttps://doi.org/10.1021/la5007007openalex-snapshot
Structure and Functional Properties of a Multimeric Protein αA-Crystallin Adsorbed on Silver Nanoparticle Surface
inferred← citeshttps://doi.org/10.1023/a:1006897910253openalex-snapshot
The rodent αA-crystallin gene: mutagenesis of a non-consensus 5′-splice site to study alternative splicing in vivo
inferred← citeshttps://doi.org/10.1023/a:1007051514282openalex-snapshot
Dissociation of Human αB-Crystallin Aggregates by Thiocyanate Is Structurally and Functionally Reversible
inferred← citeshttps://doi.org/10.1034/j.1399-3054.2001.1110302.xopenalex-snapshot
Does the chloroplast small heat shock protein protect photosystem II during heat stress in vitro?
inferred← citeshttps://doi.org/10.1038/29106openalex-snapshot
Crystal structure of a small heat-shock protein
inferred← citeshttps://doi.org/10.1038/nrmicro866openalex-snapshot
Minimal protein-folding systems in hyperthermophilic archaea
inferred← citeshttps://doi.org/10.1038/s41419-023-05972-0openalex-snapshot
HSPB1 facilitates chemoresistance through inhibiting ferroptotic cancer cell death and regulating NF-κB signaling pathway in breast cancer
inferred← citeshttps://doi.org/10.1038/s41467-021-23338-yopenalex-snapshot
Structural basis of substrate recognition and thermal protection by a small heat shock protein
inferred← citeshttps://doi.org/10.1038/s41467-021-27036-7openalex-snapshot
Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble
inferred← citeshttps://doi.org/10.1038/s41467-025-58964-3openalex-snapshot
Mechanism of small heat shock protein client sequestration and induced polydispersity
inferred← citeshttps://doi.org/10.1038/s41594-019-0332-9openalex-snapshot
The structure and oxidation of the eye lens chaperone αA-crystallin
inferred← citeshttps://doi.org/10.1038/srep32517openalex-snapshot
Identification and characterization of the GhHsp20 gene family in Gossypium hirsutum
inferred← citeshttps://doi.org/10.1039/d0cs01349hopenalex-snapshot
Redesign of protein nanocages: the way from 0D, 1D, 2D to 3D assembly
inferred← citeshttps://doi.org/10.1042/bj20071472openalex-snapshot
ArHsp21, a developmentally regulated small heat-shock protein synthesized in diapausing embryos of Artemia franciscana
inferred← citeshttps://doi.org/10.1042/bj20090907openalex-snapshot
Identification of the key structural motifs involved in HspB8/HspB6–Bag3 interaction
inferred← citeshttps://doi.org/10.1046/j.1365-313x.2000.00887.xopenalex-snapshot
Transient expression and heat‐stress‐inducedco‐aggregation of endogenous and heterologous small heat‐stress proteins in tobacco protoplasts
inferred← citeshttps://doi.org/10.1046/j.1365-313x.2002.029005545.xopenalex-snapshot
A peptide methionine sulfoxide reductase highly expressed in photosynthetic tissue in Arabidopsis thaliana can protect the chaperone‐like activity of a chloroplast‐localized small heat shock protein
inferred← citeshttps://doi.org/10.1046/j.1432-0436.1996.6120077.xopenalex-snapshot
Cellular and molecular features of lens differentiation: a review of recent advances
inferred← citeshttps://doi.org/10.1046/j.1432-1033.2002.02812.xopenalex-snapshot
Functional similarities between the small heat shock proteins Mycobacterium tuberculosis HSP 16.3 and human αB‐crystallin
inferred← citeshttps://doi.org/10.1046/j.1432-1033.2002.02958.xopenalex-snapshot
Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants
inferred← citeshttps://doi.org/10.1046/j.1432-1033.2002.03049.xopenalex-snapshot
A critical motif for oligomerization and chaperone activity of bacterial α‐heat shock proteins
inferred← citeshttps://doi.org/10.1046/j.1432-1327.2000.01188.xopenalex-snapshot
Mouse Hsp25, a small heat shock protein
inferred← citeshttps://doi.org/10.1046/j.1432-1327.2000.01423.xopenalex-snapshot
A small‐angle X‐ray solution scattering study of bovine α‐crystallin
inferred← citeshttps://doi.org/10.1046/j.1432-1327.2001.01929.xopenalex-snapshot
Chaperone function of mutant versions of αA‐ and αB‐crystallin prepared to pinpoint chaperone binding sites
inferred← citeshttps://doi.org/10.1046/j.1440-169x.1996.t01-1-00004.xopenalex-snapshot
Ontogeny of low molecular weight stress protein p26 during early development of the brine shrimp, Artemia franciscana
inferred← citeshttps://doi.org/10.1046/j.1440-1789.2003.00475.xopenalex-snapshot
Neuropathological study of C57BL/6Akita mouse, type 2 diabetic model: Enhanced expression of αB‐crystallin in oligodendrocytes
inferred← citeshttps://doi.org/10.1046/j.1471-4159.2001.00038.xopenalex-snapshot
Ser‐59 is the major phosphorylation site in αB‐crystallin accumulated in the brains of patients with Alexander's disease
inferred← citeshttps://doi.org/10.1073/pnas.180310197openalex-snapshot
Postsymbiotic plasmid acquisition and evolution of the repA1 -replicon in Buchnera aphidicola
inferred← citeshttps://doi.org/10.1073/pnas.2500029122openalex-snapshot
TaHSP18.6 and TaSRT1 interact to confer resistance to Fusarium crown rot by regulating the auxin content in common wheat
inferred← citeshttps://doi.org/10.1073/pnas.94.22.11767openalex-snapshot
Phosphotyrosine signaling and the single cell:metazoan boundary
inferred← citeshttps://doi.org/10.1073/pnas.94.22.12007openalex-snapshot
Origin and evolution of the slime molds (Mycetozoa)
inferred← citeshttps://doi.org/10.1073/pnas.95.16.9129openalex-snapshot
Small heat shock protein of Methanococcus jannaschii , a hyperthermophile
inferred← citeshttps://doi.org/10.1073/pnas.96.25.14394openalex-snapshot
Chloroplast small heat shock proteins: Evidence for atypical evolution of an organelle-localized protein
inferred← citeshttps://doi.org/10.1074/jbc.271.46.29060openalex-snapshot
Immobilization of the C-terminal Extension of Bovine αA-Crystallin Reduces Chaperone-like Activity
inferred← citeshttps://doi.org/10.1074/jbc.272.19.12847openalex-snapshot
Unique Structural Features of a Novel Class of Small Heat Shock Proteins
inferred← citeshttps://doi.org/10.1074/jbc.272.30.19051openalex-snapshot
Molecular Characterization of a Small Heat Shock/α-Crystallin Protein in Encysted Artemia Embryos
inferred← citeshttps://doi.org/10.1074/jbc.272.39.24646openalex-snapshot
Structure-Function Studies on Small Heat Shock Protein Oligomeric Assembly and Interaction with Unfolded Polypeptides
inferred← citeshttps://doi.org/10.1074/jbc.272.43.27470openalex-snapshot
A Plant Small Heat Shock Protein Gene Expressed during Zygotic Embryogenesis but Noninducible by Heat Stress
inferred← citeshttps://doi.org/10.1074/jbc.273.21.12999openalex-snapshot
Aggrecan Synthesis and Secretion
inferred← citeshttps://doi.org/10.1074/jbc.273.43.28346openalex-snapshot
Phosphorylation of αB-crystallin in Mitotic Cells and Identification of Enzymatic Activities Responsible for Phosphorylation
inferred← citeshttps://doi.org/10.1074/jbc.274.10.6305openalex-snapshot
Site-directed Spin Labeling Study of Subunit Interactions in the α-Crystallin Domain of Small Heat-shock Proteins
inferred← citeshttps://doi.org/10.1074/jbc.274.34.24137openalex-snapshot
Structural and Functional Consequences of the Mutation of a Conserved Arginine Residue in αA and αB Crystallins
inferred← citeshttps://doi.org/10.1074/jbc.274.42.30190openalex-snapshot
ATP and the Core “α-Crystallin” Domain of the Small Heat-shock Protein αB-crystallin
inferred← citeshttps://doi.org/10.1074/jbc.274.48.34067openalex-snapshot
Thermodynamic Stability of Human Lens Recombinant αA- and αB-crystallins
inferred← citeshttps://doi.org/10.1074/jbc.275.2.1095openalex-snapshot
Muscle Develops a Specific Form of Small Heat Shock Protein Complex Composed of MKBP/HSPB2 and HSPB3 during Myogenic Differentiation
inferred← citeshttps://doi.org/10.1074/jbc.m103373200openalex-snapshot
In Vivo Modifications of the Maize Mitochondrial Small Heat Stress Protein, HSP22
inferred← citeshttps://doi.org/10.1074/jbc.m107737200openalex-snapshot
Phe71 Is Essential for Chaperone-like Function in αA-crystallin
inferred← citeshttps://doi.org/10.1074/jbc.m110027200openalex-snapshot
Detection of Protein-Protein Interactions among Lens Crystallins in a Mammalian Two-hybrid System Assay
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