Membrane fusion induced by neuronal SNAREs transits through hemifusion. - Wikidata - awgldk - TriplyDB

Membrane fusion induced by neuronal SNAREs transits through hemifusion.

Membrane fusion induced by neuronal SNAREs transits through hemifusion.

http://www.wikidata.org/entity/Q54483375

about

Membrane tension and membrane fusion Open syntaxin docks synaptic vesicles A Chemical Controller of SNARE-Driven Membrane Fusion That Primes Vesicles for Ca(2+)-Triggered Millisecond Exocytosis The polybasic juxtamembrane region of Sso1p is required for SNARE function in vivo Inner/Outer nuclear membrane fusion in nuclear pore assembly: biochemical demonstration and molecular analysis Bem1p is a positive regulator of the homotypic fusion of yeast vacuoles.Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion.Multiple intermediates in SNARE-induced membrane fusion.Productive hemifusion intermediates in fast vesicle fusion driven by neuronal SNAREs.SNAREpin/Munc18 promotes adhesion and fusion of large vesicles to giant membranes Paleontological evidence for membrane fusion between a unit membrane and a half-unit membrane.Atomic force microscope spectroscopy reveals a hemifusion intermediate during soluble N-ethylmaleimide-sensitive factor-attachment protein receptors-mediated membrane fusion Single Molecule Measurements of Interaction Free Energies Between the Proteins Within Binary and Ternary SNARE Complexes Investigation of SNARE-Mediated Membrane Fusion Mechanism Using Atomic Force Microscopy.Docking, not fusion, as the rate-limiting step in a SNARE-driven vesicle fusion assay Protein determinants of SNARE-mediated lipid mixing.Network motif comparison rationalizes Sec1/Munc18-SNARE regulation mechanism in exocytosis.A computational analysis framework for molecular cell dynamics: case-study of exocytosis.Field theoretic study of bilayer membrane fusion: II. Mechanism of a stalk-hole complex SNARE-mediated lipid mixing depends on the physical state of the vesicles.Dissection of SNARE-driven membrane fusion and neuroexocytosis by wedging small hydrophobic molecules into the SNARE zipper Are there too many or too few SNAREs in proteoliposomes?A continuum model of docking of synaptic vesicle to plasma membrane.Asymmetric phospholipid distribution drives in vitro reconstituted SNARE-dependent membrane fusion.Fusing a lasting relationship between ER tubules.C2B polylysine motif of synaptotagmin facilitates a Ca2+-independent stage of synaptic vesicle priming in vivo.A novel phase of compressed bilayers that models the prestalk transition state of membrane fusion.Membranes of the world unite!Transition from hemifusion to pore opening is rate limiting for vacuole membrane fusion Towards reconstitution of membrane fusion mediated by SNAREs and other synaptic proteins The conserved plant sterility gene HAP2 functions after attachment of fusogenic membranes in Chlamydomonas and Plasmodium gametes A scissors mechanism for stimulation of SNARE-mediated lipid mixing by cholesterol Fusion step-specific influence of cholesterol on SNARE-mediated membrane fusion.CAPS drives trans-SNARE complex formation and membrane fusion through syntaxin interactions Cholesterol, regulated exocytosis and the physiological fusion machine.Hemifusion in Synaptic Vesicle Cycle.Visualization of SNARE-Mediated Hemifusion between Giant Unilamellar Vesicles Arrested by Myricetin.Vesicle trafficking and membrane remodelling in cytokinesis.The Multifaceted Role of SNARE Proteins in Membrane Fusion.Ca(2+)-synaptotagmin directly regulates t-SNARE function during reconstituted membrane fusion.

P2860

Q26797464-A3A58B4B-BE6F-4865-92CB-7AF576FFE67F Q27334556-49924B0E-ECA3-485B-AA45-7AA868D8DD74 Q27336160-E88B4238-418C-4A5C-B968-C195D552BBA7 Q27931683-FBF3F762-D764-4F38-8383-6A9E10960332 Q28294996-DEABD597-CBAD-4303-BE04-918C6DA166CB Q30159716-694071F1-E30F-424A-B6BE-C2C95E1855B0 Q30369961-D865A884-A652-4D2E-A7AE-A8AFD289B520 Q30478481-7AF361B8-935E-4633-991E-8D53316AEF4A Q30481113-30B6AFA1-D0F4-4655-A811-DDC02E32A22B Q30481470-628230A2-57E9-41F4-9E09-56E25868AD0D Q33294741-AA527D05-27C8-4F10-B370-586B48BE6F25 Q33299157-755B6DD4-D72D-47F6-A7F5-C94BAA25FF39 Q33526994-D1161E3B-4BE7-4C00-9875-38626A9C04EB Q33540688-B5F0CB78-169A-4C30-BF1B-651C7B50A115 Q33888728-051D2618-11B1-484D-BA56-9F6A63ED8A79 Q33999406-E9BCC6B9-0A7C-4852-8A80-96082763439E Q34198065-AE20FB05-7359-4F67-8DD8-C7093EF7E258 Q34341484-1CDB8899-F875-4FBA-86B2-66FDAED188C9 Q34353236-10CBA258-EE6D-46B0-9564-4B4BEBB19BD9 Q34418818-F2F4266E-826E-467D-8A75-B77F06C4D1A9 Q34438246-86D6D707-80B0-4358-83D1-A95D3FE414F0 Q34481444-F0AA2892-BD6D-458C-9A2C-17FF57476F66 Q34775346-5E0EF3A6-9143-42BF-9915-28DD1079B094 Q35075467-0A5D2A10-1894-4B1B-BD19-DADF002AF533 Q35083786-2A4CF0E2-356F-40C1-A0EE-7A1EFC7CD836 Q35190997-C09E6621-9C88-4926-AA9E-19B22ACB4DE2 Q35649577-D1DF6DB1-39DC-4C03-AF03-FCDDD8E2AB94 Q36119093-9974DCB1-0CED-4810-A90A-C83B4445C447 Q36320585-74C76272-49B0-49FE-936B-E870B44E37A3 Q36357369-E1D632BD-E2D2-43BB-B9AF-8AF728E6E960 Q36585513-12CD175B-F6F3-405A-8A21-648B07C6E75E Q37146782-B709F756-AFEE-4F9B-9F6D-0EDD9EBCC016 Q37279368-A830D18A-5A2B-4AB7-B9E0-FA517BCBEBAF Q37394786-CBAE4F1F-9509-4833-A4CA-077A13AC901F Q37594134-B01A9A59-6588-4ECF-A556-38D066BDD72E Q37703099-8AEF7407-54B4-4D61-9316-FE4402747711 Q37731034-F9BE5D0F-CDDE-4D60-B0B0-FD4141692FF7 Q37888728-58DF3F77-8FA3-4A72-98F4-A96016609C1B Q39121037-B104B622-080A-46D3-B2F5-61C1757D33E1 Q41791620-46E5ED22-2329-439C-9B09-AD95F5DF4E2B

P2860

Membrane fusion induced by neuronal SNAREs transits through hemifusion.

http://www.wikidata.org/entity/Q54483375

description

2005 nî lūn-bûn

@nan

2005年の論文

@ja

2005年学术文章

@wuu

2005年学术文章

@zh-cn

2005年学术文章

@zh-hans

2005年学术文章

@zh-my

2005年学术文章

@zh-sg

2005年學術文章

@yue

2005年學術文章

@zh

2005年學術文章

@zh-hant

name

Membrane fusion induced by neuronal SNAREs transits through hemifusion.

@en

Membrane fusion induced by neuronal SNAREs transits through hemifusion.

@nl

type

label

Membrane fusion induced by neuronal SNAREs transits through hemifusion.

@en

Membrane fusion induced by neuronal SNAREs transits through hemifusion.

@nl

prefLabel

Membrane fusion induced by neuronal SNAREs transits through hemifusion.

@en

Membrane fusion induced by neuronal SNAREs transits through hemifusion.

@nl

P1433

Q54483375-660148C7-8735-47A1-BC86-8A2B41A001F0

P1476

Q54483375-86C63BB6-58BE-4F56-B8AD-0E24F8831ABB

P2093

Q54483375-1D54AEF4-EF9E-4C8E-9DFA-8F78FDDE9C11

Q54483375-2A241A08-CC8B-46E6-AE71-692C74917BDE

Q54483375-653387A8-6741-4E26-931D-FC10E39B73B8

Q54483375-82FEB901-E60F-4DA0-BC14-BFECD7B11D7E

P2860

Q54483375-02480541-70FE-4774-A3BE-74AE18D42E0B

Q54483375-07B9C99C-3152-4BE5-AB67-7266A6F05C18

Q54483375-12182364-C6AA-4393-B39F-6EDF1F47EA97

Q54483375-2B01CD5C-7752-4B73-BB03-AE6B1FE8B7CB

Q54483375-3BE82B8D-54B0-4DEA-BEA5-E047C715E5FA

Q54483375-5040DFE8-0316-4591-82C6-C7FCAB4CAAFB

Q54483375-56377385-AD1E-4FFF-9CE0-161561E12843

Q54483375-641BF940-C59B-4DBB-9565-9089AF9DA958

Q54483375-6A4F87CF-34F1-45AD-AE7E-C09B31DFA9FE

Q54483375-6C948DF3-394A-44CA-B842-DB411C316E82

P304

Q54483375-B12F4427-7F76-41E4-93A6-F03AE617F410

P31

Q54483375-D8B5B88A-0266-4537-8938-AFF30F97A810

P356

Q54483375-51D41611-B48D-4EF6-9CDA-CA41117AC3B0

P407

Q54483375-EAA88C2A-3A45-4A41-A4FE-DE510279E6E0

P433

Q54483375-D19DAFCF-094D-48E0-A812-A60F4BA103A5

P478

Q54483375-87E9F914-20B5-40F4-89E0-3C370E0C94D1

P577

Q54483375-A781C9F9-5524-4040-B1BF-E4E53007A89C

P5875

Q54483375-7E86E45B-C060-420D-8D77-1CB8607FB4C7

P698

Q54483375-2BC869E0-B7DF-48BE-A207-8AAB7281399F

P356

P1433

Journal of Biological Chemistry

P1476

Membrane fusion induced by neuronal SNAREs transits through hemifusion.

@en

P2093

Fan Zhang

http://www.w3.org/2001/XMLSchema#string

James A McNew

http://www.w3.org/2001/XMLSchema#string

Xiaobing Lu

http://www.w3.org/2001/XMLSchema#string

Yeon-Kyun Shin

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution

Compartmental specificity of cellular membrane fusion encoded in SNARE proteins.

Hemifusion in SNARE-mediated membrane fusion.

Mechanisms of intracellular protein transport

SNAREpins: minimal machinery for membrane fusion

A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion

Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase

Membrane fusion

The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition

The pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation.

P304

30538-30541

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M506862200

http://www.w3.org/2001/XMLSchema#string

P407

P433

34

http://www.w3.org/2001/XMLSchema#string

P478

280

http://www.w3.org/2001/XMLSchema#string

P577

2005-06-24T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

7763867

http://www.w3.org/2001/XMLSchema#string

P698

15980065

http://www.w3.org/2001/XMLSchema#string