Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor
about
Combinatorial SNARE complexes with VAMP7 or VAMP8 define different late endocytic fusion events.Molecular basis for the sorting of the SNARE VAMP7 into endocytic clathrin-coated vesicles by the ArfGAP HrbThe similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevanceX-ray structure of the T. Aquaticus Ftsy:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPasesThe structure of BtuB with bound colicin E3 R-domain implies a transloconA structural explanation for the binding of endocytic dileucine motifs by the AP2 complexLipids Trigger a Conformational Switch That Regulates Signal Recognition Particle (SRP)-mediated Protein TargetingAn interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation.The beta-subunit of the protein-conducting channel of the endoplasmic reticulum functions as the guanine nucleotide exchange factor for the beta-subunit of the signal recognition particle receptor.Metal ion-mediated reduction in surface entropy improves diffraction quality of crystals of the IRAK-4 death domainHomodimerization of the G protein SRbeta in the nucleotide-free state involves proline cis/trans isomerization in the switch II region.Differential regulation of the TRAIL death receptors DR4 and DR5 by the signal recognition particleComparative analysis of plant genomes allows the definition of the "Phytolongins": a novel non-SNARE longin domain protein familyHighly efficient gene silencing using perfect complementary artificial miRNA targeting AP1 or heteromeric artificial miRNA targeting AP1 and CAL genesLipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting.The structure of the MAPK scaffold, MP1, bound to its partner, p14. A complex with a critical role in endosomal map kinase signaling.Molecular mechanism of co-translational protein targeting by the signal recognition particleStructure, function and evolution of the signal recognition particle.Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sitesRegulation of Srpr Expression by miR-330-5p Controls Proliferation of Mouse Epidermal KeratinocyteSignal recognition particles in chloroplasts, bacteria, yeast and mammals (review).Dual recognition of the ribosome and the signal recognition particle by the SRP receptor during protein targeting to the endoplasmic reticulum.Dynamics of co-translational protein targeting.Circular permutation as a tool to reduce surface entropy triggers crystallization of the signal recognition particle receptor beta subunit.Protein translocation across the rough endoplasmic reticulum.A novel oncoprotein Pirh2: rising from the shadow of MDM2.Signal recognition particle: an essential protein-targeting machine.The Sec translocon mediated protein transport in prokaryotes and eukaryotes.Dynamin GTPase domain mutants that differentially affect GTP binding, GTP hydrolysis, and clathrin-mediated endocytosis.Pathogenic role of anti-signal recognition protein and anti-3-Hydroxy-3-methylglutaryl-CoA reductase antibodies in necrotizing myopathies: Myofiber atrophy and impairment of muscle regeneration in necrotizing autoimmune myopathies.ATPase and GTPase Tangos Drive Intracellular Protein Transport.Biological Insights into Therapeutic Protein Modifications throughout Trafficking and Their Biopharmaceutical Applications.Extreme genome diversity in the hyper-prevalent parasitic eukaryote Blastocystis.FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG translocon.Longin-like folds identified in CHiPS and DUF254 proteins: vesicle trafficking complexes conserved in eukaryotic evolution.Design of improved membrane protein production experiments: quantitation of the host response.The beta-subunit of the signal recognition particle receptor is a novel GTP-binding protein without intrinsic GTPase activity.Longin and GAF domains: structural evolution and adaptation to the subcellular trafficking machinery.The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domains.Small GTPases and the evolution of the eukaryotic cell.
P2860
Q24292734-096EFBE1-EDE8-4BD3-86FE-A6F3FF18B5A2Q24310785-E3E6335E-2C07-479B-8CBD-9A623F2AD56FQ26781543-A85F5394-1B4F-48DC-BE28-E5AD9EF69C5CQ27640901-4A29DC0D-BA8E-4048-8C03-D859DB022B65Q27642291-678DA6A2-FB1E-46DF-A9DA-1AD35152A219Q27653407-B23903EC-97B0-441E-A22C-E83A6F2277CFQ27667685-DBACFC7A-8916-4982-8359-F1625068E86AQ27932958-C57F973A-4F08-42AA-8C2D-625F7DCFC329Q27940066-4317E9CC-A100-4E6F-BE28-6CD8B99F90E6Q30354708-8E3C9780-77BF-4640-96B4-8B83C33A8F23Q30477283-0977228C-E876-409B-8D3C-F3506B875620Q33206588-F03A2B20-C8E8-440E-BB5C-3C125803AD8CQ33514955-CE8961E9-D99A-4A54-AB52-ED5758DDEA3AQ33573031-E40A7909-C26C-4F0B-8650-525655920CE9Q34083157-D445545C-A551-448D-A087-25B2CF8ECECAQ34305323-C3A4AF4C-CB03-4ECA-AB21-10CBF1E23E5BQ34797147-5E5D9656-55CA-48D2-A0FF-186776BBA093Q35174625-539FD213-F676-46FC-9B3B-F4FC40234431Q36118522-11A8EA6F-803A-4C7B-B4CB-C378267DFCAAQ36170771-41C228FD-58CE-4F43-AB8F-5FB02A49CDB4Q36224486-D9D3B222-3EE9-4052-89A0-2F7F24C0DF2FQ36325055-6208B1D3-1CEA-49D4-B6B8-1913A87E89ACQ36385101-A245C086-52B9-4595-B4BD-31646E52DB46Q36526239-DE64586F-BD0A-48F4-8E02-73626FDA0280Q36555178-8966970E-124B-4982-91F7-613CB7D19B6CQ37834073-013CBCEA-B5E7-4DFA-A235-3609C896AE1CQ38081948-63C6363C-8C81-4C06-848F-1B7E62840F6FQ38206834-A3BBE427-6FB6-43DD-BC6F-AE697809E6B8Q38338732-7C360FB3-D4EC-4B3A-A679-417300650393Q38948633-089FE906-3B77-400E-8022-B4D8F8E37B7DQ38961828-86CE58DB-3912-4144-B7D0-E3244F8E38FDQ39149359-5E5B1D3F-0754-4B06-9182-62A8C44413A5Q40053656-162D0063-8850-4211-8AF3-5FD79DD9DE53Q40110503-F98D3AEF-2359-4369-AF65-9BDBEC68C710Q41789015-4ABCD78B-150C-4406-9BA3-93D02515EFFDQ43057961-66FB3FFA-EC2E-4A18-B640-EA5FB90F9C5CQ44448851-96B5A48F-BEA8-4F61-85A2-FFAC654FAE74Q44943882-EDC6FD28-6936-41F3-B67B-3AA5792F6C1AQ46913511-78244E89-D342-4920-B69D-0BCFACA633F9Q47071309-589B5011-8EC8-4C92-9FC5-E2A667C3E723
P2860
Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor
description
2003 nî lūn-bûn
@nan
2003 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մարտին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Structural basis for the funct ...... recognition particle receptor
@ast
Structural basis for the funct ...... recognition particle receptor
@en
Structural basis for the funct ...... recognition particle receptor
@nl
type
label
Structural basis for the funct ...... recognition particle receptor
@ast
Structural basis for the funct ...... recognition particle receptor
@en
Structural basis for the funct ...... recognition particle receptor
@nl
prefLabel
Structural basis for the funct ...... recognition particle receptor
@ast
Structural basis for the funct ...... recognition particle receptor
@en
Structural basis for the funct ...... recognition particle receptor
@nl
P3181
P1433
P1476
Structural basis for the funct ...... recognition particle receptor
@en
P2093
Thomas Schwartz
P304
P3181
P356
10.1016/S0092-8674(03)00161-2
P407
P577
2003-03-21T00:00:00Z