Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus.
about
Herpes simplex virus glycoprotein B associates with target membranes via its fusion loopsStructure of dengue virus: implications for flavivirus organization, maturation, and fusionFormation and characterization of the trimeric form of the fusion protein of Semliki Forest VirusAn epitope of the Semliki Forest virus fusion protein exposed during virus-membrane fusion.Mutational Evidence for an Internal Fusion Peptide in Flavivirus Envelope Protein EReversible Acid-Induced Inactivation of the Membrane Fusion Protein of Semliki Forest VirusMolecular dissection of the Semliki Forest virus homotrimer reveals two functionally distinct regions of the fusion protein.The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains.Membrane interactions of the tick-borne encephalitis virus fusion protein E at low pH.Novel mutations that control the sphingolipid and cholesterol dependence of the Semliki Forest virus fusion proteinPlacement of the structural proteins in Sindbis virusSecond-Site Revertants of a Semliki Forest Virus Fusion-Block Mutation Reveal the Dynamics of a Class II Membrane Fusion ProteinFunctions of the Stem Region of the Semliki Forest Virus Fusion Protein during Virus Fusion and AssemblyCharacterization of a Structural Intermediate of Flavivirus Membrane FusionDomain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusionOligomerization-dependent folding of the membrane fusion protein of Semliki Forest virusDifferential Cholesterol Binding by Class II Fusion Proteins Determines Membrane Fusion PropertiesRole of Conserved Histidine Residues in the Low-pH Dependence of the Semliki Forest Virus Fusion ProteinA structural and functional perspective of alphavirus replication and assemblyE1 Mutants Identify a Critical Region in the Trimer Interface of the Semliki Forest Virus Fusion ProteinA Stable Prefusion Intermediate of the Alphavirus Fusion Protein Reveals Critical Features of Class II Membrane FusionMolecular mechanism of the synaptotagmin–SNARE interaction in Ca2+-triggered vesicle fusionCharacterization of an early-stage fusion intermediate of Sindbis virus using cryoelectron microscopyVirus membrane-fusion proteins: more than one way to make a hairpinActivation of a retroviral membrane fusion protein: soluble receptor-induced liposome binding of the ALSV envelope glycoprotein.The surface conformation of Sindbis virus glycoproteins E1 and E2 at neutral and low pH, as determined by mass spectrometry-based mappingSindbis virus glycoprotein E1 is divided into two discrete domains at amino acid 129 by disulfide bridge connections.The cholesterol requirement for sindbis virus entry and exit and characterization of a spike protein region involved in cholesterol dependenceBiochemical consequences of a mutation that controls the cholesterol dependence of Semliki Forest virus fusionMutations in the E1 hydrophobic domain of rubella virus impair virus infectivity but not virus assembly.Low-pH-dependent fusion of Sindbis virus with receptor-free cholesterol- and sphingolipid-containing liposomes.Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment.Oligomerization of fusogenic peptides promotes membrane fusion by enhancing membrane destabilizationPseudorevertants of a Semliki forest virus fusion-blocking mutation reveal a critical interchain interaction in the core trimerAlphavirus Entry and Membrane Fusion.Residue-level resolution of alphavirus envelope protein interactions in pH-dependent fusion.The interaction of alphavirus E1 protein with exogenous domain III defines stages in virus-membrane fusionMutational evidence of internal fusion loops in herpes simplex virus glycoprotein BIntercellular Extensions Are Induced by the Alphavirus Structural Proteins and Mediate Virus TransmissionA single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exit
P2860
Q24644405-012514AF-08ED-4E32-93F4-01F911FA32BFQ24736810-99C42CD0-891A-48BD-9973-4D33F257926DQ27469686-F03B2DB4-6CDF-45CF-9E86-6581ED6002FEQ27469752-C0666080-D056-4115-8880-9FA2D44501E1Q27469788-CCB3E913-41A6-416E-886E-79351A085632Q27469816-8D24C1BA-58EC-42BF-ADA5-9250DD41ED76Q27472838-BEE0651D-EFEC-491F-96FA-4C68CA1E2ECAQ27472848-6582807B-CF89-4EB0-B947-805435FF7443Q27472865-967AEC95-29BC-411A-93C5-A2AA5F4DA91AQ27472923-73F59988-67FC-49D8-B8F4-0D3FFD58304AQ27472934-A1F1466E-861D-4E8C-B1B8-3EB4A424A7C1Q27473232-798ACFAF-C11B-4755-B0BE-F62A1B9364EEQ27477615-E88948E1-5B16-4A60-BA28-A456D4FF1F25Q27478061-99EA55D2-FDAB-4AA6-885D-83CC0BE077DBQ27485039-EA782D25-5504-4C43-BB11-E920D2AC7C45Q27485868-E6368707-86F9-4153-A104-6AED39102DE3Q27486916-5E1FBA98-45DA-4DB8-8B7F-90995CD257FFQ27488309-5338B63B-D263-4F33-9862-7935FF7F093AQ27490173-A9CC5B45-EBEC-4026-8C25-5DE80BC82B6BQ27490331-C39903FC-7E2A-49A4-AD54-B91136CBE9E3Q27490513-8F184E4E-2CC9-4AF4-B81E-AAE43751F31BQ27659974-DE7335B0-D00A-4D1F-A3AF-46CC20DD6027Q28295578-8CB2F065-1EA8-40E4-A3A2-EF54024D3E6DQ29620769-6497BA35-D76A-4769-A057-CB64292AC23DQ30442135-8825A6F4-355D-49EA-A759-E7B70E02AA1FQ30872909-8021EAD3-0633-4E61-9932-C6CE3E5C99AEQ33605141-3ABE058E-06F5-47F9-A98D-7EC62125201EQ33647933-E3886856-A64B-4923-8E8E-1BB60217096AQ33797087-6DD527E9-0A30-4870-BB83-1B8CB36BE880Q33808160-C0BF4E1F-B0DC-44A4-9E0A-C5FAEAF48670Q33820410-63EA0D4B-3BCC-4EDE-A1BA-B71934A9F490Q34179684-BB160EF7-CB52-4DD5-86E5-E3219304FD15Q34184290-A7EFAB72-D6C6-4C77-9EBD-DFA1C8939725Q34295892-8856D7F1-44F9-4EAC-BDB6-E1EAABC97DFBQ34905189-A3AAF51F-1043-45B9-8F6E-C0DC8D4CC8F7Q35128812-96AA98C2-2F79-4AA5-9F6C-FDA12924A853Q35531595-74BEE7EC-789E-44E3-9F61-029DBCCAC609Q35857450-66AAB9F3-F39D-4DA3-8D8D-DA28BA779CBEQ36225228-E1AD7207-587A-48A7-9231-5CCED4FD2AC4Q36254866-5C5CB1A3-B66F-4235-93BF-CA93EACE8B98
P2860
Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus.
@ast
Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus.
@en
type
label
Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus.
@ast
Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus.
@en
prefLabel
Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus.
@ast
Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus.
@en
P2093
P2860
P356
P1476
Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus
@en
P2093
P2860
P304
P356
10.1083/JCB.134.4.863
P407
P577
1996-08-01T00:00:00Z