A new role for BiP: closing the aqueous translocon pore during protein integration into the ER membrane
about
Mechanisms of CFTR Folding at the Endoplasmic ReticulumBiP-mediated closing of the Sec61 channel limits Ca2+ leakage from the ERThe SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activityControl of translocation through the Sec61 translocon by nascent polypeptide structure within the ribosome.Cellular mechanisms of membrane protein folding.The plug domain of yeast Sec61p is important for efficient protein translocation, but is not essential for cell viability.Polytopic membrane protein folding at L17 in the ribosome tunnel initiates cyclical changes at the transloconTransmembrane segments of nascent polytopic membrane proteins control cytosol/ER targeting during membrane integrationCotranslational stabilization of Sec62/63 within the ER Sec61 translocon is controlled by distinct substrate-driven translocation events.Intraribosomal regulation of expression and fate of proteins.Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP.Cotranslational membrane protein biogenesis at the endoplasmic reticulum.The Candida albicans Kar2 protein is essential and functions during the translocation of proteins into the endoplasmic reticulum.The co-translational folding and interactions of nascent protein chains: a new approach using fluorescence resonance energy transfer.Versatility of the endoplasmic reticulum protein folding factory.The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulumThe Ribosome-Sec61 Translocon Complex Forms a Cytosolically Restricted Environment for Early Polytopic Membrane Protein Folding.Protein translocation across the rough endoplasmic reticulum.Understanding integration of α-helical membrane proteins: the next stepsPushing, pulling and trapping--modes of motor protein supported protein translocation.Sequence-specific retention and regulated integration of a nascent membrane protein by the endoplasmic reticulum Sec61 translocon.Organellar calcium buffers.Protein transport into the human ER and related diseases, Sec61-channelopathies.The Brl domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons.A phaseolin domain involved directly in trimer assembly is a determinant for binding by the chaperone BiP.GRP78 at the Centre of the Stage in Cancer and Neuroprotection.The molecular chaperone binding protein BiP prevents leaf dehydration-induced cellular homeostasis disruption.Different transmembrane domains associate with distinct endoplasmic reticulum components during membrane integration of a polytopic protein.Mammalian BiP controls posttranslational ER translocation of the hepatitis B virus large envelope protein.Co-chaperone Specificity in Gating of the Polypeptide Conducting Channel in the Membrane of the Human Endoplasmic Reticulum.Stop-transfer efficiency of marginally hydrophobic segments depends on the length of the carboxy-terminal tail.Polypeptide-binding proteins mediate completion of co-translational protein translocation into the mammalian endoplasmic reticulum.Membrane protein TM segments are retained at the translocon during integration until the nascent chain cues FRET-detected release into bulk lipid.Activation of the unfolded protein response in sarcoma cells treated with rapamycin or temsirolimus.Real-time fluorescence detection of ERAD substrate retrotranslocation in a mammalian in vitro system.The structural and functional coupling of two molecular machines, the ribosome and the transloconSpatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.Translocon closure to Ca2+ leak in proliferating vascular smooth muscle cells.Translocon pores in the endoplasmic reticulum are permeable to small anions.A trans-membrane segment inside the ribosome exit tunnel triggers RAMP4 recruitment to the Sec61p translocase.
P2860
Q21129277-3A3B031D-6408-4CA9-AA7D-D6B514F0D7CEQ24293288-854D0F7C-CAEF-48B0-BCC2-4B4998D1B791Q24301641-38D13352-CEAE-422C-B03E-C8EC252100CAQ33334739-BD83D421-C750-49FB-96EA-3A3B360BE25FQ33624056-96A1048E-B46D-441F-9A41-401CA5B1769BQ35010304-46CE370B-7765-4266-A0C2-C539CADF4D9EQ35276847-2644C892-9E54-488B-9E13-1695BCDF0D34Q35276891-3F340595-FC37-4B87-B626-B96CB3080207Q35470364-F8D0F9EF-F4D6-4CA4-AFFD-971D83C68AE5Q35616327-CC1B5FC2-3E7C-498F-B818-12621C7E3642Q35670486-40C91119-5AF0-4B3C-885E-9E1064A5C757Q35695015-E152ACC8-0E7A-4F14-95B1-B9C2112A5435Q35891168-C5AF7B95-25CC-4B38-8C93-3E1074FA71C1Q36024278-8D6FF14B-BCED-4BBC-8896-448F3D17C9B9Q36242585-E5016F7A-8EB5-46DE-AAEF-FDDE05AAF6BCQ36321326-D0633BB7-4A6E-4F38-9047-8470A8684A87Q36323490-BBB18CE3-6797-4A5C-902F-828FB5018528Q36555178-04B51F32-F654-4EBE-8BFB-27D84D584198Q36570393-1DBCCF56-D8F5-4EC0-BA40-F4DE853D37F8Q36804933-B57D5A19-A33D-4311-AF95-0AE8986E05CAQ37061529-0C564891-F4D6-4725-9418-BB912E9C9956Q37855346-9BBEE26C-A64F-4010-B6A2-9994779174BBQ38220635-F939B3B3-F0DA-4274-9333-6A18F42BB21FQ38317482-D23310C6-33BE-483B-AAC1-A3CC883C306DQ38350038-62A0E902-277F-46FC-B6C8-C71EAB46919DQ38692967-D3374839-D33B-45B6-BBB5-21836FA60B0DQ38933542-AC13B45F-539E-48B8-9632-A7B78F56BB73Q39691810-39B98A93-1D36-40FD-B210-9E18717DD943Q39950009-71DE8578-E20A-41BE-BFF8-ACAAC9BF420DQ40289318-9E5A8910-CF07-48B8-B9CF-4F314EF3CC69Q40663807-F5967E44-8896-448A-8DEF-55519F59D999Q40772361-E0E897A1-C175-4A37-B6C4-B57BFC3C7945Q41217184-773E9990-7779-405A-9939-1B87BE6C8A14Q41677150-AED320A6-0D1C-418F-8CD5-68AC4CC8DD5FQ41785201-8D2CA416-3CCA-441B-8CAA-ECE9D3AF3B29Q41911587-1D0002AC-AB75-4494-933F-DD9245B6B3ECQ42096150-8E8868F6-A29B-4CA3-90A4-FFD36FED2409Q42151020-69643B27-5DAE-4842-AC4D-3B89FF0079BAQ42493299-C1F61093-1A50-4FC4-9C3C-2DBDBB793082Q43092073-EBCF2F25-8ACA-4BEA-8E0E-5D0BA56F40D1
P2860
A new role for BiP: closing the aqueous translocon pore during protein integration into the ER membrane
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
A new role for BiP: closing th ...... tegration into the ER membrane
@ast
A new role for BiP: closing th ...... tegration into the ER membrane
@en
type
label
A new role for BiP: closing th ...... tegration into the ER membrane
@ast
A new role for BiP: closing th ...... tegration into the ER membrane
@en
prefLabel
A new role for BiP: closing th ...... tegration into the ER membrane
@ast
A new role for BiP: closing th ...... tegration into the ER membrane
@en
P2860
P356
P1476
A new role for BiP: closing th ...... tegration into the ER membrane
@en
P2093
Arthur E Johnson
Nora G Haigh
P2860
P304
P356
10.1083/JCB.200110074
P407
P577
2002-01-21T00:00:00Z