The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
about
CLUH regulates mitochondrial biogenesis by binding mRNAs of nuclear-encoded mitochondrial proteinsThe chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregationCytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulumDepletion of the C. elegans NAC engages the unfolded protein response, resulting in increased chaperone expression and apoptosis.Control of apoptosis by asymmetric cell divisionStructural characterization of a eukaryotic chaperone--the ribosome-associated complexDual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunitsSpecific effects of ribosome-tethered molecular chaperones on programmed -1 ribosomal frameshifting.Iron-dependent regulation of MDM2 influences p53 activity and hepatic carcinogenesisThe HSP70 chaperone machinery: J proteins as drivers of functional specificityHSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.Asymmetric divisions, aggresomes and apoptosisMolecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.Protein folding in the cytoplasm and the heat shock response.The nascent polypeptide-associated complex is a key regulator of proteostasis.A conserved motif is prerequisite for the interaction of NAC with ribosomal protein L23 and nascent chains.Induction of HSPA4 and HSPA14 by NBS1 overexpression contributes to NBS1-induced in vitro metastatic and transformation activity.Identification of HYPK-interacting proteins reveals involvement of HYPK in regulating cell growth, cell cycle, unfolded protein response and cell death.Birth, life and death of nascent polypeptide chains.Identification of AMP-activated protein kinase targets by a consensus sequence search of the proteome.Heat-induced ribosome pausing triggers mRNA co-translational decay in Arabidopsis thaliana.Role for the molecular chaperones Zuo1 and Ssz1 in quorum sensing via activation of the transcription factor Pdr1Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperonesDistinct yet linked: chaperone networks in the eukaryotic cytosol.Evidence from case-control and longitudinal studies supports associations of genetic variation in APOE, CETP, and IL6 with human longevity.Ribosome association and stability of the nascent polypeptide-associated complex is dependent upon its own ubiquitination.Multiple hsp70 isoforms in the eukaryotic cytosol: mere redundancy or functional specificity?FACS purification and transcriptome analysis of drosophila neural stem cells reveals a role for Klumpfuss in self-renewal.Transcription regulation of HYPK by Heat Shock Factor 1Inefficient SRP interaction with a nascent chain triggers a mRNA quality control pathway.Faithful chaperones.Functional conservation and divergence of J-domain-containing ZUO1/ZRF orthologs throughout evolution.Conserved C-terminal nascent peptide binding domain of HYPK facilitates its chaperone-like activity.On-site remodeling at chromatin: How multiprotein complexes are rebuilt during DNA repair and transcriptional activation.Shaping proteostasis at the cellular, tissue, and organismal level.The Role of Co-chaperones in Synaptic Proteostasis and Neurodegenerative Disease.Hsp70/J-protein machinery from Glossina morsitans morsitans, vector of African trypanosomiasisMethylation of histone H3 lysine 9 occurs during translation.Multivalent contacts of the Hsp70 Ssb contribute to its architecture on ribosomes and nascent chain interactionBiP modulates the affinity of its co-chaperone ERj1 for ribosomes.
P2860
Q24306257-90958BE7-1BCD-4BA3-A5C9-4E51AF885A76Q24605078-1765F9CD-0AEA-4FBD-A882-62BD5DAA058DQ24643310-9482006D-561D-4190-A534-0EA6336CAD9DQ27321332-11B27286-851C-4F34-8E85-97F02C28868DQ27333582-6FCC8C0B-8CC8-4821-8017-5E11457E2C40Q27683526-5825A562-4B8B-4FB7-9644-46992B656F79Q27728116-0B9B34C2-E1AC-4D05-871A-D1CEE5DDD11BQ27940051-077D6767-9CE8-4577-9793-1D2237DA27D7Q28576835-44683DA0-B55F-43A9-9CF1-CF669C5238EEQ29616140-2E09A6B2-B2D7-4FF2-8564-338341436AB8Q30354473-601F14DF-3BAE-4135-9EA4-A29F1469DCADQ33621958-8F12F461-C0A8-4BD8-A4C9-0B4AC5AD2B59Q34038270-92F7886E-76A0-4920-8891-E09D4CDEA2B9Q34152827-5A7EE526-C656-4A20-9CD9-60840A804219Q34340544-857F6580-101E-4111-A72F-4D9A42BBB933Q34471343-B3B487EB-FED9-4606-A764-A9F8038725C1Q34499737-E4DFC5CE-C368-460D-A758-55CCF543F13DQ34525270-8A148D0C-C0B1-41E7-89D9-B199DB1A501AQ35089834-91D34ED3-5BC0-4898-A54A-C5B077F981B9Q35169812-D2D55C2D-6943-4026-9081-984C77D85F5DQ35562070-627A422C-1073-496F-ABAF-2D622504F7D5Q35673652-08CF7F7E-4642-4409-A543-3373D803AFEAQ35686747-AF6B5C00-6885-4882-97DA-3BAE702A3C2FQ36439262-51B30176-FE87-45C3-A4AA-D7C110385171Q36670196-1CA1D8C3-EF1A-481C-9A09-E07791A2D2A5Q37102597-25DE5C33-64ED-4025-8AFE-F5AD32E20D2AQ37200825-40B62D0A-404B-4B8F-99FB-AA9AACC5EBCAQ37308487-42A75E99-E1C8-49A9-88A6-A4B76FE8215FQ37499606-BA84CD2E-67AB-41AF-B6FC-1446B8A5AF3FQ37597107-6DC8204A-E56B-4651-A731-540F98728BB5Q37886778-83774810-4B0D-4FE1-81EF-7D86CBF6A713Q38198555-539AD908-D37E-4CE0-B313-BA58FA597249Q38305067-640458D8-C678-4174-86B8-A37E654A86ADQ38947385-F7857798-3FC0-4AFE-BD18-4225D1BF0ABFQ39235911-E5F18E97-06B2-4DAB-AA85-0556A581209CQ39349922-98ACA28E-2BAD-40C5-8726-FC64D81D20C8Q41142344-984F8192-B95F-476D-AB6F-37D7760064FCQ41838640-E0E93785-17A2-4AA4-A411-0F90B54D8B40Q41933973-221A46BF-B2EC-4FC4-9526-FCFAD77D2CEAQ42081379-C4AC3F7F-96D2-44CC-BC45-15F96766D628
P2860
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
description
2005 nî lūn-bûn
@nan
2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
name
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
@ast
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
@en
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
@en-gb
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
@nl
type
label
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
@ast
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
@en
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
@en-gb
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
@nl
prefLabel
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
@ast
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
@en
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
@en-gb
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
@nl
P2093
P2860
P921
P356
P1476
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
@en
P2093
Carolyn K Suzuki
Charlotte Conz
Hendrik Otto
Joachim Stahl
Peter Rücknagel
Philipp Maier
Tina Wölfle
P2860
P304
P356
10.1073/PNAS.0504400102
P407
P577
2005-07-19T00:00:00Z