about
Mammalian homologues of yeast sec31p. An ubiquitously expressed form is localized to endoplasmic reticulum (ER) exit sites and is essential for ER-Golgi transportSec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cellsCellular COPII proteins are involved in production of the vesicles that form the poliovirus replication complex.Selective protein exit from yeast endoplasmic reticulum in absence of functional COPII coat component Sec13p.Smy2p participates in COPII vesicle formation through the interaction with Sec23p/Sec24p subcomplex.Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members.Sfb2p, a yeast protein related to Sec24p, can function as a constituent of COPII coats required for vesicle budding from the endoplasmic reticulum.Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae.Sec24p and Iss1p function interchangeably in transport vesicle formation from the endoplasmic reticulum in Saccharomyces cerevisiae.Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesiclesA membrane protein enriched in endoplasmic reticulum exit sites interacts with COPIIGlobal Gene Expression Profiling through the Complete Life Cycle of Trypanosoma vivaxMammalian COPII coat component SEC24C is required for embryonic development in miceGenome-wide mapping of in vivo targets of the Drosophila transcription factor Kruppel.Trafficking through COPII stabilises cell polarity and drives secretion during Drosophila epidermal differentiation.Transcriptome and gene expression profile of ovarian follicle tissue of the triatomine bug Rhodnius prolixus.Regulation of G-protein coupled receptor traffic by an evolutionary conserved hydrophobic signal.Sterols block binding of COPII proteins to SCAP, thereby controlling SCAP sorting in ERTranscription profiling of Candida albicans cells undergoing the yeast-to-hyphal transition.Regulation of a COPII component by cytosolic O-glycosylation during mitosis.Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulumStructural disorder provides increased adaptability for vesicle trafficking pathways.Study of the plant COPII vesicle coat subunits by functional complementation of yeast Saccharomyces cerevisiae mutants.The genetic basis of a craniofacial disease provides insight into COPII coat assembly.Ebola virus matrix protein VP40 uses the COPII transport system for its intracellular transport.The lysophospholipid acyltransferase antagonist CI-976 inhibits a late step in COPII vesicle budding.Mechanisms of COPII vesicle formation and protein sorting.Sec24C/D-isoform-specific sorting of the preassembled ER-Golgi Q-SNARE complex.Prediction of biological functions of Shewanella-like protein phosphatases (Shelphs) across different domains of life.Sequence determinants of the Caenhorhabditis elegans dopamine transporter dictating in vivo axonal export and synaptic localization.Differential selection of Golgi proteins by COPII Sec24 isoforms in procyclic Trypanosoma brucei.Unexpected ancient paralogs and an evolutionary model for the COPII coat complex.Molecular genetic contributions to self-rated health.Sorting competition with membrane-permeable peptides in intact epithelial cells revealed discrimination of transmembrane proteins not only at the trans-Golgi network but also at pre-Golgi stages.ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat.Evidence for prebudding arrest of ER export in animal cell mitosis and its role in generating Golgi partitioning intermediates.Redundant function of two Arabidopsis COPII components, AtSec24B and AtSec24C, is essential for male and female gametogenesis.Two Sec13p homologs, AtSec13A and AtSec13B, redundantly contribute to the formation of COPII transport vesicles in Arabidopsis thaliana.Ceramide biosynthesis is required for the formation of the oligomeric H+-ATPase Pma1p in the yeast endoplasmic reticulum.Active and specific recruitment of a soluble cargo protein for endoplasmic reticulum exit in the absence of functional COPII component Sec24p.
P2860
Q22254007-72C05077-7CAB-4EDE-A94F-F84A716AB5CCQ24670130-08D6C55C-460A-4D86-9635-519CF32F14CCQ27469873-32BEFC50-4BF6-4E82-A89C-9B9D94B64EA5Q27932128-66644015-4913-43BC-BE96-FDE8FADBA2C9Q27933025-2E29BE48-5EF6-4FD2-83DC-C2CA7096BB86Q27936142-603F9155-6E4C-423A-B572-3D0A2FC4DE71Q27938615-2399E886-BF9F-4ECE-BBEB-7705E4D977D3Q27939936-EE1FAAF6-10D9-4DCB-973B-411601C1B26CQ27940030-FA8593AF-C3CE-4971-BD87-DC263ACB4BCDQ27940100-B1FDBB9F-93F6-41C0-B5EF-D99BAEFF866EQ28510912-60362716-3B9B-42AA-8C19-19F8BF315E87Q28547186-B5A23619-061E-44AB-8CCB-9718926F7F84Q28593531-3EF20F03-E81A-45B6-A19F-39287CD76455Q31058906-A351F0CD-D588-40E2-A436-EEED65C74113Q33593110-89EB1254-2FA7-4921-B585-94F1A23E9523Q33954026-51E2AF0B-6FBE-4DA5-AE8C-F2D9AD31B671Q34056261-E55C02B4-3075-45F1-9C80-E4F67B35B01FQ34154078-D013A603-89C6-4EB6-A280-2AF81DDDC529Q34167828-36161929-3A10-49A2-89AC-30D7300657D1Q34304768-A36CD75D-4767-4227-94B9-1535C00889E4Q34606627-B203995C-CE0D-4EAB-BC43-7CBAD079E11BQ34845322-D5742C6A-F785-4FDB-9F59-2560D40094A4Q35108633-530E449A-1E1A-49C8-8DDE-F2C5438F75BEQ36487336-71D6B54F-9669-41C7-8440-053832D59C5DQ36580850-BD1CAF1C-B307-4FC9-826E-51401EA3AD8FQ36729092-92093F49-D3DD-4625-AA00-3FDA5EDCEA9DQ36742809-38F4BCEB-49F8-432B-BEC2-899E9C8B8959Q37222548-477FF4E5-53FA-4708-9749-82F1DCC14569Q37940905-1FDF22CB-7335-4C78-A68A-73431EF3C59AQ38434567-9E630945-310B-4C99-A650-B8118BF3BFF6Q39498522-A8FF3FFF-EAB2-44AE-8A41-93B04ABAE1C1Q40269973-88E778E2-078D-40A5-AD07-D87EE892D38FQ40467398-EF007264-0E02-4467-8A0F-24E59323882FQ40592227-30BFA54B-57B5-4CBD-A79F-E8828A8C75CAQ42917503-53999B04-9016-494D-A190-FB175AB41610Q43605988-6C32EA46-8A89-4C43-9235-F75EEFA2459BQ44024130-6D24425E-F8E0-4BE7-AEFD-DB5850AC16F5Q45928022-601A76DA-12AD-4813-800A-9AD87BFA0263Q46058043-5A54402B-29C1-4B00-B73A-E6FD5B863810Q47789652-6ACB1EC1-42F3-435F-94B0-A17C114DA742
P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի մարտին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Sec24 proteins and sorting at the endoplasmic reticulum
@ast
Sec24 proteins and sorting at the endoplasmic reticulum
@en
Sec24 proteins and sorting at the endoplasmic reticulum
@en-gb
Sec24 proteins and sorting at the endoplasmic reticulum
@nl
type
label
Sec24 proteins and sorting at the endoplasmic reticulum
@ast
Sec24 proteins and sorting at the endoplasmic reticulum
@en
Sec24 proteins and sorting at the endoplasmic reticulum
@en-gb
Sec24 proteins and sorting at the endoplasmic reticulum
@nl
prefLabel
Sec24 proteins and sorting at the endoplasmic reticulum
@ast
Sec24 proteins and sorting at the endoplasmic reticulum
@en
Sec24 proteins and sorting at the endoplasmic reticulum
@en-gb
Sec24 proteins and sorting at the endoplasmic reticulum
@nl
P2093
P2860
P921
P3181
P356
P1476
Sec24 proteins and sorting at the endoplasmic reticulum
@en
P2093
D Garcia-Estefania
J L Carpentier
J P Paccaud
P2860
P304
P3181
P356
10.1074/JBC.274.12.7833
P407
P50
P577
1999-03-01T00:00:00Z