Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.
about
Heat shock proteins and hormesis in the diagnosis and treatment of neurodegenerative diseasesStructural basis for the antifolding activity of a molecular chaperoneThe human HSP70 family of chaperones: where do we stand?A Non-enveloped Virus Hijacks Host Disaggregation Machinery to Translocate across the Endoplasmic Reticulum MembraneRuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils.Synergism between a foldase and an unfoldase: reciprocal dependence between the thioredoxin-like activity of DnaJ and the polypeptide-unfolding activity of DnaK.Challenging muscle homeostasis uncovers novel chaperone interactions in Caenorhabditis elegansMulti-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperonesQuantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPsA Differentiation Transcription Factor Establishes Muscle-Specific Proteostasis in Caenorhabditis elegans.Quantitative proteomics of rat livers shows that unrestricted feeding is stressful for proteostasis with implications on life span.How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions.Induction of heat shock proteins in differentiated human neuronal cells following co-application of celastrol and arimoclomol.Overexpression of the transcription factor Yap1 modifies intracellular redox conditions and enhances recombinant protein secretion.Expanding role of molecular chaperones in regulating α-synuclein misfolding; implications in Parkinson's disease.Chaperone-client interactions: Non-specificity engenders multifunctionality.Differential Targeting of Hsp70 Heat Shock Proteins HSPA6 and HSPA1A with Components of a Protein Disaggregation/Refolding Machine in Differentiated Human Neuronal Cells following Thermal Stress.Components of a mammalian protein disaggregation/refolding machine are targeted to nuclear speckles following thermal stress in differentiated human neuronal cells.On the role, ecology, phylogeny, and structure of dual-family immunophilins.HSP60 possesses a GTPase activity and mediates protein folding with HSP10.Folding of maltose binding protein outside of and in GroEL.Misfolding and aggregation of nascent proteins: a novel mode of toxic cadmium action in vivo.Dynamic and Active Proteins: Biomolecular Motors in Engineered Nanostructures.The role of heat shock proteins and co-chaperones in heart failure.Oligomerization of a molecular chaperone modulates its activity.Immune Responses Induced by HSP60 DNA Vaccine against Toxoplasma gondii Infection in Kunming MiceImmunization with plasmid DNA expressing Heat Shock Protein 40 confers prophylactic protection against chronic Toxoplasma gondii infection in Kunming mice
P2860
Q26778791-7ECFEDBE-D327-47F7-96E8-6A2C786F1469Q27726706-ED33BA5C-B0E4-4A52-B1E8-2DB265DA7D58Q28071416-E345A708-25F4-4EFF-9BCD-6574D899C1B0Q28547004-B835B484-39F9-4481-BD79-7A0DE8AE20C4Q30356564-161AD99D-8BB9-40CB-91FB-65F0E150CEE6Q30650128-FAE6729A-E215-4B30-89AF-57EFFE7F42D8Q35596765-E62B1026-5F11-40C6-A380-4A17F4C63FA9Q35686747-550ED77D-6669-4ED6-BB37-3A95A5D99684Q35725189-53619C8C-32D8-4491-B3FA-5A029E49E2D5Q36236487-70591CF1-AF76-4CBD-832D-66153915833DQ37274989-F55C0E03-D590-4398-9EEB-BA98447D7A6DQ38356312-54FC6013-B979-4257-A732-A5E5FC552289Q38765994-74857E37-6E2F-43BA-A86B-BEB0FC6543E4Q38868027-873B8E79-2961-4C7F-AE01-FA000DA9A7DFQ38927256-BE8BB496-173D-40EE-B6BC-AC21EC3A09A8Q39376939-A5F7FBEF-447E-4EA7-AA51-A493FE9E6498Q42290756-6E1B11AE-A54E-44C5-99A3-A797A00933A6Q42316145-B110C248-AEF5-465A-9E83-DD28D24F5E04Q43030855-5C82F066-1785-49DA-A01F-6F3356695F9DQ47144907-09A0AB96-7FE7-4D75-B3D8-E9FAF2F61125Q47236838-4B2C476B-A8B3-49A3-91C2-0042A242CC72Q47763358-20CBEAF2-3ED5-4D7C-80CD-5F3201BBF489Q51152158-674961A4-20BD-425A-8D6A-0E11A9F91BB5Q51424623-E79F1981-1DFD-44E4-8758-BF882E943C17Q54203917-B8A14868-38C6-40DB-8744-B02F7A1A646FQ56573168-657822EB-B872-4AFD-B828-ABBE681F5C74Q57179393-9526CF25-E4DC-4468-B7E1-1DE962B6A78C
P2860
Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.
description
2014 nî lūn-bûn
@nan
2014 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Molecular chaperones are nanom ...... alternatively folded proteins.
@ast
Molecular chaperones are nanom ...... alternatively folded proteins.
@en
Molecular chaperones are nanom ...... alternatively folded proteins.
@nl
type
label
Molecular chaperones are nanom ...... alternatively folded proteins.
@ast
Molecular chaperones are nanom ...... alternatively folded proteins.
@en
Molecular chaperones are nanom ...... alternatively folded proteins.
@nl
prefLabel
Molecular chaperones are nanom ...... alternatively folded proteins.
@ast
Molecular chaperones are nanom ...... alternatively folded proteins.
@en
Molecular chaperones are nanom ...... alternatively folded proteins.
@nl
P2860
P1476
Molecular chaperones are nanom ...... alternatively folded proteins.
@en
P2093
Pierre Goloubinoff
Rayees U H Mattoo
P2860
P2888
P304
P356
10.1007/S00018-014-1627-Y
P577
2014-04-24T00:00:00Z
2014-09-01T00:00:00Z