Structural mechanism for sterol sensing and transport by OSBP-related proteins.
about
The role of hydrophobic interactions in positioning of peripheral proteins in membranesThe mammalian oxysterol-binding protein-related proteins (ORPs) bind 25-hydroxycholesterol in an evolutionarily conserved pocketInteractome map uncovers phosphatidylserine transport by oxysterol-binding proteinsGOLPH3 bridges phosphatidylinositol-4- phosphate and actomyosin to stretch and shape the Golgi to promote buddingINTRACELLULAR TRANSPORT. PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER-plasma membrane contactsOxysterol-binding protein and vesicle-associated membrane protein-associated protein are required for sterol-dependent activation of the ceramide transport proteinOsh4p exchanges sterols for phosphatidylinositol 4-phosphate between lipid bilayersOxysterol binding protein-related Protein 9 (ORP9) is a cholesterol transfer protein that regulates Golgi structure and functionSterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: oxysterols block transport by binding to InsigInter-organelle ER-endolysosomal contact sites in metabolism and disease across evolutionOSBP-related proteins: liganding by glycerophospholipids opens new insight into their functionGolgi membrane dynamics and lipid metabolismCrystal structure of cholesteryl ester transfer protein reveals a long tunnel and four bound lipid moleculesStructural Basis of Sterol Binding by NPC2, a Lysosomal Protein Deficient in Niemann-Pick Type C2 DiseaseSchistosoma mansonivenom allergen-like protein 4 (SmVAL4) is a novel lipid-binding SCP/TAPS protein that lacks the prototypical CAP motifsINTRACELLULAR TRANSPORT. Phosphatidylserine transport by ORP/Osh proteins is driven by phosphatidylinositol 4-phosphateLipid binding requirements for oxysterol-binding protein Kes1 inhibition of autophagy and endosome-trans-Golgi trafficking pathways.Structural and functional characterization of the CAP domain of pathogen-related yeast 1 (Pry1) proteinTrans-Golgi network and endosome dynamics connect ceramide homeostasis with regulation of the unfolded protein response and TOR signaling in yeast.Tritium suicide selection identifies proteins involved in the uptake and intracellular transport of sterols in Saccharomyces cerevisiae.A new family of StART domain proteins at membrane contact sites has a role in ER-PM sterol transport.The yeast oxysterol binding protein Kes1 maintains sphingolipid levelsLipid-regulated sterol transfer between closely apposed membranes by oxysterol-binding protein homologues.Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited: lipidome meets proteome.A genomewide screen reveals a role of mitochondria in anaerobic uptake of sterols in yeast.Pathogen-Related Yeast (PRY) proteins and members of the CAP superfamily are secreted sterol-binding proteins.Homologues of oxysterol-binding proteins affect Cdc42p- and Rho1p-mediated cell polarization in Saccharomyces cerevisiae.Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositidesOSBP-Related Protein Family in Lipid Transport Over Membrane Contact SitesMolecular characterization of oxysterol binding to the Epstein-Barr virus-induced gene 2 (GPR183)OSBP-related protein 8 (ORP8) suppresses ABCA1 expression and cholesterol efflux from macrophagesGenetic basis of haloperidol resistance in Saccharomyces cerevisiae is complex and dose dependentOligo-astheno-teratozoospermia in mice lacking ORP4, a sterol-binding protein in the OSBP-related protein familyLipopolysaccharide transport to the cell surface: periplasmic transport and assembly into the outer membrane.The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrelBinding and release of cholesterol in the Osh4 protein of yeastYou are lost without a map: Navigating the sea of protein structuresHigh-throughput computational structure-based characterization of protein families: START domains and implications for structural genomicsA detour for yeast oxysterol binding proteinsOsh4p is needed to reduce the level of phosphatidylinositol-4-phosphate on secretory vesicles as they mature.
P2860
Q21093294-8526ECA2-8007-45C4-8ACF-77C4C63B40DCQ24302379-AAA1A8E6-D099-440A-85B1-1EA6F04CD17FQ24316991-2B123E7A-66C3-4DCC-92C0-FCD826B6DE59Q24336708-AD67DF6B-7144-43B5-82A0-B6C7CF566EE4Q24338551-AEF1B4EF-DDF7-45B9-B1FC-47A660A92C01Q24547407-21D7189A-4837-4FB9-B401-EBF4C745E397Q24627193-3A7927FA-F926-4B40-ACC5-FE1F3CD50CE6Q24647008-CD427900-2E93-40DD-B077-A5F671E7836AQ24683936-A88493CD-6677-44E1-BDBB-9232A92EDFB9Q26739484-2CC2E99B-251A-4229-B2A6-E04EC66B86E7Q27011239-87B57DAD-2183-4A6B-9DB3-A80D9A09A736Q27016562-315FCCB8-989E-4E4C-9D25-08102C1E95E7Q27643587-11933F25-4749-4FFE-A276-9117042BF6E3Q27645956-2A05FFEE-C51B-4D42-ABB0-3BEB58A01C53Q27684904-547A708E-FE48-4863-A8D6-E17EE2A9EFD1Q27701626-600E2EB6-547A-411F-ACA7-70AE960C57A0Q27930042-ED945031-AC2F-457B-9F73-4F9A585E1FF1Q27932138-A313CCF1-9D70-4A73-A76B-F787351F62DDQ27932969-110A73D9-270E-4472-B113-E5804303EE20Q27934405-8AC36BF2-5CF3-4CCD-AD0A-E0EC56C6C4FCQ27934991-CBBD6138-974B-4819-88FD-EF95EE25C9F1Q27935692-7B7B66BA-4B81-4F36-9107-8235BDBAADE6Q27935807-438CBBF5-83D2-4F7C-BC5E-B6A2092257D7Q27936020-2C91F692-3BA3-47FF-BFAE-C3D8CDD086E7Q27936829-F7C27FAB-B1DE-47BE-9C99-900BE6DC9502Q27937495-127112D2-52AC-49DA-AB7C-30B6D617F008Q27938690-9D6ED3DE-60CF-463E-85F9-E12D8198E889Q27939970-3C1A8BF6-3ED7-47F0-9E58-4EEA9ACEF540Q28074147-A91D8032-4129-4BFB-BB09-1023542BC9BEQ28115398-5A0B6828-F8A7-40A9-BBB7-9592F18ED824Q28256750-B9209529-303D-40B4-B72A-531AC0A800EBQ28542762-A132B55C-D626-4F34-B62E-09B6E0868469Q28589077-1993A6DB-9EDB-4873-A381-FCA3A18F1E98Q30152829-28B5A398-567B-4159-B266-0CCDE745F21EQ30155882-F7235294-12A5-4D9F-9EE4-0D172E191FE3Q30157496-BD1AEF3C-55A3-45EB-9B1A-AF21692BD02BQ30370362-11A884E9-3659-440B-B24B-AF0A4DD76770Q30387975-C20D91BC-5E78-4253-B411-0132A0B786AAQ30421723-6264992B-813D-4273-B457-32DE61AB55F5Q30596615-5F1053C4-CC12-44BD-8E0B-520F9A5CCD84
P2860
Structural mechanism for sterol sensing and transport by OSBP-related proteins.
description
2005 nî lūn-bûn
@nan
2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Structural mechanism for sterol sensing and transport by OSBP-related proteins
@nl
Structural mechanism for sterol sensing and transport by OSBP-related proteins.
@ast
Structural mechanism for sterol sensing and transport by OSBP-related proteins.
@en
type
label
Structural mechanism for sterol sensing and transport by OSBP-related proteins
@nl
Structural mechanism for sterol sensing and transport by OSBP-related proteins.
@ast
Structural mechanism for sterol sensing and transport by OSBP-related proteins.
@en
prefLabel
Structural mechanism for sterol sensing and transport by OSBP-related proteins
@nl
Structural mechanism for sterol sensing and transport by OSBP-related proteins.
@ast
Structural mechanism for sterol sensing and transport by OSBP-related proteins.
@en
P2093
P2860
P3181
P356
P1433
P1476
Structural mechanism for sterol sensing and transport by OSBP-related proteins.
@en
P2093
James H Hurley
Sumana Raychaudhuri
William A Prinz
Young Jun Im
P2860
P2888
P304
P3181
P356
10.1038/NATURE03923
P407
P577
2005-09-01T00:00:00Z
P5875
P6179
1002347490