ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin.
about
Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG In vivoShotgun identification of protein modifications from protein complexes and lens tissueThe Box H/ACA snoRNP Assembly Factor Shq1p is a Chaperone Protein Homologous to Hsp90 Cochaperones that Binds to the Cbf5p EnzymeMyofibrillar myopathiesFunctional similarities between the small heat shock proteins Mycobacterium tuberculosis HSP 16.3 and human alphaB-crystallinInteraction of ATP with a small heat shock protein from Mycobacterium leprae: effect on its structure and functionRole of the C-terminal extensions of alpha-crystallins. Swapping the C-terminal extension of alpha-crystallin to alphaB-crystallin results in enhanced chaperone activityThe cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro.The endoplasmic reticulum chaperone Cosmc directly promotes in vitro folding of T-synthase.Multiple small heat shock proteins in rhizobia.Biochemical characterization of the small heat shock protein IbpB from Escherichia coli.Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.Regulation and mechanism of action of the small heat shock protein from the hyperthermophilic archaeon Pyrococcus furiosus.Functional characterization of Xenopus small heat shock protein, Hsp30C: the carboxyl end is required for stability and chaperone activityMinimal protein-folding systems in hyperthermophilic archaea.Novel roles for α-crystallins in retinal function and disease.Alpha-crystallin-derived peptides as therapeutic chaperones.Expression and biochemical characterization of two small heat shock proteins from the thermoacidophilic crenarchaeon Sulfolobus tokodaii strain 7.Chemical modulation of the chaperone function of human alphaA-crystallin.Alpha-crystallin and ATP facilitate the in vitro renaturation of xylanase: enhancement of refolding by metal ions.In vivo substrate diversity and preference of small heat shock protein IbpB as revealed by using a genetically incorporated photo-cross-linker.Lens aging: effects of crystallins.Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures.Microarray expression profiling identifies genes regulating sustained cell specific productivity (S-Qp) in CHO K1 production cell lines.Alphab-crystallin-assisted reactivation of glucose-6-phosphate dehydrogenase upon refolding.High-molecular-mass complexes formed in vivo contain smHSPs and HSP70 and display chaperone-like activity.Effect of mutations of murine lens alphaB crystallin on transfected neural cell viability and cellular translocation in response to stress.Effect of site-directed mutagenesis of methylglyoxal-modifiable arginine residues on the structure and chaperone function of human alphaA-crystallin.Drosophila UNC-45 prevents heat-induced aggregation of skeletal muscle myosin and facilitates refolding of citrate synthase.Effect of dicarbonyl-induced browning on alpha-crystallin chaperone-like activity: physiological significance and caveats of in vitro aggregation assaysalpha-crystallin assists the renaturation of glyceraldehyde-3-phosphate dehydrogenase.Differences in properties between human alphaA- and alphaB-crystallin proteins expressed in Escherichia coli cells in response to cold and extreme pH.A S52P mutation in the 'α-crystallin domain' of Mycobacterium leprae HSP18 reduces its oligomeric size and chaperone function.Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants.Suppression of DTT-induced aggregation of abrin by alphaA- and alphaB-crystallins: a model aggregation assay for alpha-crystallin chaperone activity in vitro.Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins.Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function.Interaction of a small heat shock protein of the fission yeast, Schizosaccharomyces pombe, with a denatured protein at elevated temperature.Heterologous expression of a plant small heat-shock protein enhances Escherichia coli viability under heat and cold stress.Oligomeric structure and chaperone-like activity of Drosophila melanogaster mitochondrial small heat shock protein Hsp22 and arginine mutants in the alpha-crystallin domain.
P2860
Q24521559-442F970D-5EEB-4DB1-804B-DD7A60222208Q24534333-CAE2BA8C-16DE-48C0-A05F-1B19F3768739Q27655418-8A43D0CE-0721-44E8-A162-013DD0E822D8Q28303812-D273E66E-158F-4313-B0B7-583092043ED9Q28486864-FDCF1866-0723-47A4-B6CA-B518D00DCCADQ28545057-C25645B2-8C5C-4F85-8EDC-413375B18601Q28910389-F2D88628-D53E-489A-8FE7-AF8AFC5B8D78Q30323290-27B0CD5F-6C0F-499D-A4F5-E80D7224B957Q33593911-92C4EB33-8AA6-4CD9-B40C-85D8C070CF5BQ33634296-D481FFB2-F5DE-48C8-BDDE-0FDBA3751B9DQ33857365-5022CB05-4749-4AAA-B0E6-036E5C9E4757Q33969470-CA502A17-A4A5-4221-A5E0-4AD1F8E9AC7DQ33996779-CB72984F-1261-4E70-BD9E-EC480DDA620DQ35084694-DEC3DB65-7C4E-465B-8982-19DBDF0D0B69Q35697547-99BEAD16-DB98-45D0-8374-DB6DE7DAEE0FQ36319594-928A6045-D652-43CF-B828-057C57B41D97Q36355484-915899C1-BC53-40DB-8E2A-EF304288ADD2Q36526201-1DF5B3E9-C15F-49C8-8FD2-7466F0AAF500Q36587179-3E58BEEA-7873-4078-B754-E996EB3EE5D1Q36639622-1772B349-28C5-4DE6-89B0-F0C9811DC7E9Q37272122-30B06219-8A66-421A-9C28-EC9D11ED23A1Q37346358-31DF11FE-DACA-48DD-950A-666A1D623B47Q38362898-301B809E-DA49-4C15-A38A-8D293063035EQ39432041-7E73D0ED-C59B-4276-97DD-53E93A1D3790Q39498284-591DD649-3567-48EA-A29D-F54F209FE944Q40887941-1B61E41A-078C-4E61-A96D-7A3D14BE64BEQ40994033-E2C24FC9-AF82-41C4-BFAC-B89EA740D801Q41127730-84DE5436-20FA-4F71-8E0C-73516D2E47FBQ41200755-41360450-F5F4-47BC-A50A-0DD8FF85DAB9Q41764565-ABC50409-5856-48F4-89DF-F4EAB755F767Q41828623-BC9DB0A4-7CBC-4A10-A850-E2946C447999Q41830926-2BD911E0-3E7F-455C-84F8-7C9AAFE543D3Q43746026-5B9D6AF9-A421-4D37-9D37-9A92B93CEF4EQ44033098-9C097B75-5F2F-4889-BA8B-5795CE28BC1FQ44048927-2EFC63D3-C905-40D9-B05B-3696C31F984FQ44299975-08B07D52-E873-4E86-90F1-949D06E87826Q45005891-B93CCF9E-7314-4330-B2AB-DE1AFFE01D30Q46627905-F3B7B8ED-C63C-49F4-8278-F46422006757Q47957084-514527C0-6DE4-47D2-AEBA-0F09BFA1904DQ51066662-8488161A-9B46-4EFA-B7E4-7303EACED248
P2860
ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
ATP-enhanced molecular chapero ...... otein human alphaB crystallin.
@ast
ATP-enhanced molecular chapero ...... otein human alphaB crystallin.
@en
type
label
ATP-enhanced molecular chapero ...... otein human alphaB crystallin.
@ast
ATP-enhanced molecular chapero ...... otein human alphaB crystallin.
@en
prefLabel
ATP-enhanced molecular chapero ...... otein human alphaB crystallin.
@ast
ATP-enhanced molecular chapero ...... otein human alphaB crystallin.
@en
P2860
P356
P1476
ATP-enhanced molecular chapero ...... otein human alphaB crystallin.
@en
P2093
P J Muchowski
P2860
P304
P356
10.1073/PNAS.95.3.1004
P407
P577
1998-02-01T00:00:00Z