about
Genetic variability of the envelope gene of Type D simian retrovirus-2 (SRV-2) subtypes associated with SAIDS-related retroperitoneal fibromatosis in different macaque speciesThe Moraxella adhesin UspA1 binds to its human CEACAM1 receptor by a deformable trimeric coiled-coil.Poliovirus cell entry: common structural themes in viral cell entry pathwaysSelection of functional human antibodies from retroviral display librariesFusoselect: cell-cell fusion activity engineered by directed evolution of a retroviral glycoprotein.Human Non-neutralizing HIV-1 Envelope Monoclonal Antibodies Limit the Number of Founder Viruses during SHIV Mucosal Infection in Rhesus MacaquesMapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein EThe Coronavirus Spike Protein Is a Class I Virus Fusion Protein: Structural and Functional Characterization of the Fusion Core ComplexOligomerization-dependent folding of the membrane fusion protein of Semliki Forest virusCore structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-A resolutionCrystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteinsCrystal structure of a designed, thermostable, heterotrimeric coiled coilN- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coilInhibition of human immunodeficiency virus type 1 infectivity by the gp41 core: role of a conserved hydrophobic cavity in membrane fusionInteractions between HIV-1 gp41 core and detergents and their implications for membrane fusionStructural characterization of the human respiratory syncytial virus fusion protein coreThe trimer-of-hairpins motif in membrane fusion: Visna virusStructure of the Ebola virus glycoprotein bound to an antibody from a human survivorStructural plasticity of the phage P22 tail needle gp26 probed with xenon gasCharge-Surrounded Pockets and Electrostatic Interactions with Small Ions Modulate the Activity of Retroviral Fusion ProteinsCrystal Structure of the Marburg Virus GP2 Core Domain in Its Postfusion ConformationCrystal Structures of Beta- and Gammaretrovirus Fusion Proteins Reveal a Role for Electrostatic Stapling in Viral EntryStructural Characterization of the Glycoprotein GP2 Core Domain from the CAS Virus, a Novel Arenavirus-Like SpeciesAtomic structure of a thermostable subdomain of HIV-1 gp41Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: conserved helical interactions underlie the broad inhibitory activity of gp41 peptidesCrystal structure of botulinum neurotoxin type A and implications for toxicityStudies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics.Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug targetA synthetic all D-amino acid peptide corresponding to the N-terminal sequence of HIV-1 gp41 recognizes the wild-type fusion peptide in the membrane and inhibits HIV-1 envelope glycoprotein-mediated cell fusionBetaretroviral envelope subunits are noncovalently associated and restricted to the mammalian classMultiCoil: a program for predicting two- and three-stranded coiled coilsVaccinia viral protein A27 is anchored to the viral membrane via a cooperative interaction with viral membrane protein A17Studies of the "chain reversal regions" of the avian sarcoma/leukosis virus (ASLV) and ebolavirus fusion proteins: analogous residues are important, and a His residue unique to EnvA affects the pH dependence of ASLV entry.Specific single or double proline substitutions in the "spring-loaded" coiled-coil region of the influenza hemagglutinin impair or abolish membrane fusion activity.Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers.Isomerization of the intersubunit disulphide-bond in Env controls retrovirus fusion.Receptor-induced conformational changes in the SU subunit of the avian sarcoma/leukosis virus A envelope protein: implications for fusion activation.Turning of the receptor-binding domains opens up the murine leukaemia virus Env for membrane fusion.Noninfectious retrovirus particles drive the APOBEC3/Rfv3 dependent neutralizing antibody response
P2860
Q21093217-8CAFDF46-8D3A-482C-BCE9-A855B20E5C1FQ24315795-35672AA8-0467-47C4-BF05-E2DBC96E1803Q24550839-1C9E9DB7-5F9A-4EFB-B205-B46768D5037EQ24794038-F23B783E-E3AD-4B79-923E-585F2EABD86DQ25256213-CFEBDFF1-EEBC-48E1-8E8C-34F78D3A10C0Q27318508-CBF04556-51DF-4CD5-A9AD-DDB5F8099A85Q27469713-60C59C1E-E10E-48FA-B66C-58CC87C2A505Q27477706-326AE77B-1ABA-4AAC-AC6E-FE5750BCC070Q27485868-26E7746F-296A-442A-8B70-2305F22DD4FCQ27617533-B4134D3F-E0AA-47EA-8B58-52D0BCC22482Q27617901-80E81133-A182-41A9-812E-83FA48509AC2Q27617972-B6EDE2E8-2A6E-403A-A55E-863DBC147991Q27619272-119326F9-5A4B-4F00-BFCB-D01592BF54B2Q27619600-5A907283-75E6-4A3B-BDA7-DD723D23605BQ27620993-75559524-2EA6-455B-B601-D140DEB44FEAQ27628799-1503728E-72FC-4302-9684-2537DC95C77EQ27633137-2652A06C-EF96-4D3D-AA59-462F8EF3EDBAQ27651112-AFF06D4B-7FB9-4DE3-A49F-67F4F06FF56DQ27653932-12E749F6-869D-4C57-8891-CB6827308343Q27666913-5225C630-D280-47B2-833E-BCFE812827BEQ27671801-7E9C1EF2-8B39-4018-BE26-5C77F87015D2Q27680387-6F9AC18E-3701-4DA3-82F9-0180F4779B4BQ27680867-DB3854E9-8994-40DE-A15B-739D1BF14861Q27746904-70742AAD-6D4F-4F00-89D9-8F36770A9466Q27764897-4FFE7E7D-7A2B-48C0-AE90-94A772B84019Q27765727-B508A7D5-A520-4CB4-BDDF-DE127B4276D6Q28345849-FE1A24A6-48D6-437C-A253-AA6919C21174Q28369397-ED963D60-F8F2-430B-AA8F-474E06910738Q28379574-AC2D3E9F-ACA7-4D3E-B0E9-39E7734B1DA9Q28708989-A2C7205D-1FD0-4A90-BAE1-34FF5BF756E1Q29619769-2CA7C4C0-12B0-4F49-8680-75FA06F09713Q30358168-27D935C9-D3F9-4A3A-BA71-5333F89E6872Q30434014-CF087B49-E485-4AFC-AF78-6A5B01C7AC3FQ30442103-48224FE0-78EF-4E7F-BD01-50DC9B6DB2C7Q30442126-26A56BCF-76D4-4391-B57C-188147AF0A56Q30444021-A924F5A2-B0C6-47B7-88FA-1AB9F5A36C1DQ30448089-81D657DE-8BE3-4654-81A0-3EC838EB24A8Q30448472-EB3D0605-95E7-4BC9-B155-59D181A03129Q30483804-290ECF5A-20A8-40D0-890B-B12CB64D137FQ31036522-0334434D-3952-45DA-9D8E-0F43CCF9B654
P2860
description
1996 nî lūn-bûn
@nan
1996 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Retrovirus envelope domain at 1.7 angstrom resolution
@ast
Retrovirus envelope domain at 1.7 angstrom resolution
@en
Retrovirus envelope domain at 1.7 angstrom resolution
@nl
type
label
Retrovirus envelope domain at 1.7 angstrom resolution
@ast
Retrovirus envelope domain at 1.7 angstrom resolution
@en
Retrovirus envelope domain at 1.7 angstrom resolution
@nl
prefLabel
Retrovirus envelope domain at 1.7 angstrom resolution
@ast
Retrovirus envelope domain at 1.7 angstrom resolution
@en
Retrovirus envelope domain at 1.7 angstrom resolution
@nl
P2093
P2860
P3181
P356
P1476
Retrovirus envelope domain at 1.7 angstrom resolution
@en
P2093
P2860
P2888
P3181
P356
10.1038/NSB0596-465
P577
1996-05-01T00:00:00Z
P5875
P6179
1021968388