In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum.
about
Coupling endoplasmic reticulum stress to the cell death program: role of the ER chaperone GRP78A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functionsATPase activity of a yeast secretory glycoprotein allows ER exit during inactivation of COPII components Sec24p and Sec13p.Co- and Post-Translational Protein Folding in the ERUPR-induced resistance to etoposide is downstream of PERK and independent of changes in topoisomerase IIα levelsCloning and characterization of a novel GRP78-binding protein in the rat brainERdj4 protein is a soluble endoplasmic reticulum (ER) DnaJ family protein that interacts with ER-associated degradation machineryTranscriptional and post-transcriptional regulation of proangiogenic factors by the unfolded protein response.Probing for membrane domains in the endoplasmic reticulum: retention and degradation of unassembled MHC class I molecules.Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress.Sil1, a nucleotide exchange factor for BiP, is not required for antibody assembly or secretionGRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development.Antigen retrieval to improve the immunocytochemistry detection of sigma-1 receptors and ER chaperones.Misfolded proteins, endoplasmic reticulum stress and neurodegeneration.Hsp70 promotes epithelial sodium channel functional expression by increasing its association with coat complex II and its exit from endoplasmic reticulum.Proteomic assessment shows that many endoplasmic reticulum (ER)-resident proteins are targeted by N(epsilon)-lysine acetylation in the lumen of the organelle and predicts broad biological impact.Physiological modulation of BiP activity by trans-protomer engagement of the interdomain linkerDimerization-dependent folding underlies assembly control of the clonotypic αβT cell receptor chainsThe in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP.Dominant-interfering Hsc70 mutants disrupt multiple stages of the clathrin-coated vesicle cycle in vivo.BiP mutants that are unable to interact with endoplasmic reticulum DnaJ proteins provide insights into interdomain interactions in BiP.Bacteria- and host-derived mechanisms to control intestinal epithelial cell homeostasis: implications for chronic inflammation.Tissue-specific expression of dominant negative mutant Drosophila HSC70 causes developmental defects and lethality.In vitro reconstitution of microtubule plus end-directed, GTPgammaS-sensitive motility of Golgi membranesHsc70 negatively regulates epithelial sodium channel trafficking at multiple sites in epithelial cells.Central ceramide-induced hypothalamic lipotoxicity and ER stress regulate energy balanceThe large Hsp70 Grp170 binds to unfolded protein substrates in vivo with a regulation distinct from conventional Hsp70s.Endoplasmic reticulum (ER) stress and hypoxia response pathways interact to potentiate hypoxia-inducible factor 1 (HIF-1) transcriptional activity on targets like vascular endothelial growth factor (VEGF)Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants.Endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins and mutant P23H rhodopsin in photoreceptor cells.Glucose-regulated proteins in cancer: molecular mechanisms and therapeutic potentialA soluble secretory reporter system in Trypanosoma brucei. Studies on endoplasmic reticulum targeting.Herp coordinates compartmentalization and recruitment of HRD1 and misfolded proteins for ERAD.BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly.Transcriptional and post-transcriptional regulation of transmembrane protein 132A.The unfolded protein response regulator GRP78/BiP is required for endoplasmic reticulum integrity and stress-induced autophagy in mammalian cells.The Role of BiP Retrieval by the KDEL Receptor in the Early Secretory Pathway and its Effect on Protein Quality Control and Neurodegeneration.Protein processing: a role in the pathophysiology of genetic disease.ERdj3, a luminal ER DnaJ homologue, binds directly to unfolded proteins in the mammalian ER: identification of critical residues.
P2860
Q24293643-1DF703E2-C4B3-4755-A994-92C8C78ACD37Q24541564-F4957A3B-E23C-4E77-85F4-E2B43F931A91Q26825679-50F285C0-C22A-4945-923D-4B0CF529E767Q27939316-DC21F4AC-5970-4BC5-8919-99F5E4913DCCQ28078736-36EA679C-3910-4C28-A62A-E201DE04D6FEQ28484607-EACCBFD1-744D-46C9-9AD3-7530E5A1CA3CQ28582544-1DA45CAE-F9F3-416A-8427-C2FDEFF457F8Q28587463-2AB4356F-7361-4736-A30E-7025FD73C36BQ33686864-2196CD60-711B-457A-A22C-794324F53589Q33787846-B84A0E21-7DCE-4474-8D5B-1DCCE7CB5ABEQ34113413-F3A815C1-79D3-4C74-9928-FB60ED5A85BAQ35027549-AF872B34-0E31-4327-A59B-DC690479B3E1Q35070987-08834745-FF12-4A5C-B0D2-DE83EB8C97BDQ35163203-0E89357F-40C0-47BD-A16F-A89317BB36D3Q35941821-DEF6CC0C-0D6A-4BA7-B1F2-DD77A2F1AB65Q36003749-DD1B1F2E-A022-4961-906C-38409469C78DQ36080582-C66E508B-D6F6-4039-ADCD-8B9608839194Q36169640-7329F231-2B12-40F7-988B-0B37666B45ACQ36283774-B7F90511-526C-4B43-BF0A-1D5A7F34C048Q36288125-DC0191B2-58F8-4362-B477-B7EEC5F77515Q36376458-26CC5357-02DF-4778-B3B3-190A830AEF2BQ36446097-D2636212-C972-422E-9B14-486771C08E0FQ36809889-2FD4EC36-1BFC-4455-84D0-ACBCDE4BDDEFQ36889334-92759BB6-14E4-4C37-BEE0-9812F0594F35Q36911226-D9EEFDB5-29D6-4B26-8908-36026864BCA6Q37234555-0B709627-6B90-46CD-A8E0-A451C0A307ADQ37505073-FC4BA5D3-1E0D-4BC0-B6D6-A8013AE5F956Q37536567-A8F02F78-6BC8-4283-842E-29B29149F53CQ37563444-DAE47237-C56C-4C36-BBB2-440737F469A5Q37581998-C4DE76A2-1F8B-4D5E-9751-26BE6A505D60Q37969971-4C2F82BE-D6BB-44F1-96D3-B0026F89A14BQ38198491-571E693D-1796-4948-976D-6C444282BF2EQ38354409-4E1786BC-7DE4-4F66-BD09-9F9B974DF316Q38542175-A96AD7B9-A00F-417D-8333-7813EE14115DQ38612305-8D19887D-EF45-45F6-BC4B-3BF403880AB5Q38880726-916BE9B9-9209-4FA2-B390-6AA720E35ACDQ39972647-F04F1384-3466-438D-90E5-A6E628F54EE3Q41023936-849C8E81-EF38-4508-B75D-0106635D2B5EQ41513851-2B1EB7C4-DD1C-4E1D-B320-B659AAB2FEA8Q41969715-8EC647A4-2208-4A37-A43B-B384258E7539
P2860
In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum.
description
1995 nî lūn-bûn
@nan
1995 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մարտին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
In vivo expression of mammalia ...... of the endoplasmic reticulum.
@ast
In vivo expression of mammalia ...... of the endoplasmic reticulum.
@en
In vivo expression of mammalia ...... of the endoplasmic reticulum.
@nl
type
label
In vivo expression of mammalia ...... of the endoplasmic reticulum.
@ast
In vivo expression of mammalia ...... of the endoplasmic reticulum.
@en
In vivo expression of mammalia ...... of the endoplasmic reticulum.
@nl
prefLabel
In vivo expression of mammalia ...... of the endoplasmic reticulum.
@ast
In vivo expression of mammalia ...... of the endoplasmic reticulum.
@en
In vivo expression of mammalia ...... of the endoplasmic reticulum.
@nl
P2093
P2860
P356
P1476
In vivo expression of mammalia ...... of the endoplasmic reticulum.
@en
P2093
P2860
P304
P356
10.1091/MBC.6.3.283
P577
1995-03-01T00:00:00Z