A fusion protein required for vesicle-mediated transport in both mammalian cells and yeast
about
Ykt6p, a prenylated SNARE essential for endoplasmic reticulum-Golgi transportPhotolysis of a caged peptide reveals rapid action of N-ethylmaleimide sensitive factor before neurotransmitter releaseStimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosisCrystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion proteinCrystal structure of the Sec18p N-terminal domainStructure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATPStructural and enzymatic properties of the AAA protein Drg1p from Saccharomyces cerevisiae. Decoupling of intracellular function from ATPase activity and hexamerization.Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF)The vesicle transport protein Vps33p is an ATP-binding protein that localizes to the cytosol in an energy-dependent manner.A heterodimer of thioredoxin and I(B)2 cooperates with Sec18p (NSF) to promote yeast vacuole inheritanceA role for Yip1p in COPII vesicle biogenesis.Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositidesSPAF, a new AAA-protein specific to early spermatogenesis and malignant conversionIdentification of a novel mammalian member of the NSF/CDC48p/Pas1p/TBP-1 family through heterologous expression in yeastPeroxisome assembly factor-2, a putative ATPase cloned by functional complementation on a peroxisome-deficient mammalian cell mutantThe N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxinCharacterization of alpha-soluble N-ethylmaleimide-sensitive fusion attachment protein in alveolar type II cells: implications in lung surfactant secretion.Nucleotide sequence of grapevine (Vitis vinifera) cDNA similar to SNAP proteins.SNARE-complex disassembly by NSF follows synaptic-vesicle fusionLocalization of human and mouse N-ethylmaleimide-sensitive factor (NSF) gene: a two-domain member of the AAA family that is involved in membrane fusion.Mechanistic insights into the recycling machine of the SNARE complex.Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnoverSec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking.Live Salmonella recruits N-ethylmaleimide-sensitive fusion protein on phagosomal membrane and promotes fusion with early endosome.SNAREpins are functionally resistant to disruption by NSF and alphaSNAP.Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin.A protein associated with the manchette during rat spermiogenesis is encoded by a gene of the TBP-1-like subfamily with highly conserved ATPase and protease domains.Cholesterol, regulated exocytosis and the physiological fusion machine.The molecular machinery of neurotransmitter release (Nobel lecture).Review: Progresses in understanding N-ethylmaleimide sensitive factor (NSF) mediated disassembly of SNARE complexes.SNAREs and targeted membrane fusion.Inhibition of the membrane fusion machinery prevents exit from the TGN and proteolytic processing by furin.Structure of neurosecretory granules and the chemistry of exocytosis.Analysis of regulated exocytosis in adrenal chromaffin cells: insights into NSF/SNAP/SNARE function.A possible predocking attachment site for N-ethylmaleimide-sensitive fusion protein. Insights from in vitro endosome fusion.An architecture for the fusion site of influenza hemagglutinin.Inhibition of endocytic vesicle fusion by Plk1-mediated phosphorylation of vimentin during mitosis.Developmental changes of the 26 S proteasome in abdominal intersegmental muscles of Manduca sexta during programmed cell death.Nobel Prize for Cellular Logistics!YLL031c belongs to a novel family of membrane proteins involved in the transfer of ethanolaminephosphate onto the core structure of glycosylphosphatidylinositol anchors in yeast.
P2860
Q24315775-71A4B675-06B7-46B8-ADD2-0C23AF904CFFQ24657428-E0AACDEC-537D-41BE-BD18-DA2DD33FEBCDQ24678373-96034305-B80C-4951-A7C6-C93451BA25C1Q27620369-5D88F0AE-7000-44EE-A696-8A898D264DB9Q27620819-A2FFAB8A-DC47-4963-896D-B561647FF948Q27765278-F2E03DFC-7C7E-40FC-A1B4-CC3DC00B393AQ27932034-9C49E4DB-5835-4073-AAB5-A3E691300078Q27934304-9B4FA7F9-3351-438D-8449-E992680C8A94Q27936863-CF86F6F1-466C-44E2-8288-5C9F7F69C5E0Q27937950-C30037F3-5D8F-4D1B-87AF-98C7EBABA8F5Q27939417-CDC850FA-FA93-4EB8-AC5F-6465A5EC85F1Q27939970-BB035759-123E-428F-B7F5-641C2E045640Q28139844-4329CC2A-D5F2-4B55-9FC3-FA964236124DQ28247881-2B293F4E-0610-4C55-B473-0B13A9107159Q28284605-ED55446D-A329-4006-B5DD-977C50194F1DQ28294139-18F50788-CC1D-426C-B958-F2C1AFC4CF9EQ30770193-414FE90F-B8C7-4FC4-849A-BFF7733B4D6EQ32079799-B3C87DDB-3CC6-4FF7-A9E6-FB3D979B62E3Q33947145-F0592671-1240-4C7F-ADF3-616059D5CE14Q34403192-755B68BD-CD30-46FB-9225-3ADE9AD0EDD8Q35058666-8F696C8F-7649-4C9A-B100-C54D4D3C856BQ35636093-47744B76-433F-42D3-952A-DEE8DF0FA320Q36264678-67F4E303-550F-42CB-B38A-6301EBBCCC78Q36316409-B90124B2-6648-4500-995B-50C4A6C1FF05Q36327510-5309BCFB-D96F-4EBF-9B49-C5F789FAFC36Q36693214-0D697AEA-47DF-4CE2-B550-C4B8223B238FQ36878141-3E289402-BCEA-4EF1-BB39-4196CDFA8128Q37594134-F6F1DB3F-A7FF-40B9-8AB9-1307A63F93D3Q38262070-CDCC9F15-6968-44EA-9BDA-DB520301294BQ38803266-D70005E6-2D09-4CD4-82B5-8244F161A586Q40463768-6644B8F3-CA36-4FF9-9C54-FBC433FCCDFFQ40780580-68116740-559F-402C-8795-E9BD51797B20Q40846803-D969F4D4-4484-4210-9899-9E05942DD0C6Q40855920-6C3C5C8A-E9F0-46AF-B2F2-0CF8CC0BCD97Q41176448-9621ECA7-B360-4306-B22A-9F12FEAF1906Q41710887-53EBDD26-37F0-4AE0-87BC-AD2F2798F04DQ41958198-FAE14D68-DB22-4DDD-B40F-23C9ADCC4DF5Q42067000-61018279-9B5D-4CCE-B86C-96F936B47CADQ42250291-FA52179E-4B7C-4591-9D17-35C7B1A08511Q42626792-5EA2BA7B-F5F4-4346-A9F8-C37AE4F63FCB
P2860
A fusion protein required for vesicle-mediated transport in both mammalian cells and yeast
description
article publié dans la revue scientifique Nature
@fr
scientific article published in Nature
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в Nature в червні 1989
@uk
name
A fusion protein required for ...... both mammalian cells and yeast
@en
A fusion protein required for ...... both mammalian cells and yeast
@nl
type
label
A fusion protein required for ...... both mammalian cells and yeast
@en
A fusion protein required for ...... both mammalian cells and yeast
@nl
prefLabel
A fusion protein required for ...... both mammalian cells and yeast
@en
A fusion protein required for ...... both mammalian cells and yeast
@nl
P2093
P356
P1433
P1476
A fusion protein required for ...... both mammalian cells and yeast
@en
P2093
Rothman JE
P2888
P304
P356
10.1038/339355A0
P407
P577
1989-06-01T00:00:00Z
P6179
1052281913