Characterisation and physical mapping of an HSV-1 glycoprotein of approximately 115 X 10(3) molecular weight.
about
Role of the small GTPase Rab27a during herpes simplex virus infection of oligodendrocytic cellsBimolecular complementation defines functional regions of Herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusionConstruction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deletedCrystal structure of the conserved herpesvirus fusion regulator complex gH–gLNuclear egress and envelopment of herpes simplex virus capsids analyzed with dual-color fluorescence HSV1(17+)The gH-gL complex of herpes simplex virus (HSV) stimulates neutralizing antibody and protects mice against HSV type 1 challengeMonoclonal antibodies to distinct sites on herpes simplex virus (HSV) glycoprotein D block HSV binding to HVEMHerpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry.Structural and antigenic analysis of a truncated form of the herpes simplex virus glycoprotein gH-gL complex.Binding of complement component C3b to glycoprotein gC of herpes simplex virus type 1: mapping of gC-binding sites and demonstration of conserved C3b binding in low-passage clinical isolatesA novel herpes simplex virus glycoprotein, gL, forms a complex with glycoprotein H (gH) and affects normal folding and surface expression of gH.Glycoprotein gI of pseudorabies virus promotes cell fusion and virus spread via direct cell-to-cell transmission.Herpes virus fusion and entry: a story with many characters.Epitope mapping of herpes simplex virus type 2 gH/gL defines distinct antigenic sites, including some associated with biological function.Dissection of the antibody response against herpes simplex virus glycoproteins in naturally infected humansStructure-function analysis of herpes simplex virus type 1 gD and gH-gL: clues from gDgH chimerasHSV-1 Glycoproteins Are Delivered to Virus Assembly Sites Through Dynamin-Dependent Endocytosis.Sequential isolation of proteoglycan synthesis mutants by using herpes simplex virus as a selective agent: evidence for a proteoglycan-independent virus entry pathway.Bovine herpesvirus 1 UL49.5 homolog gene encodes a novel viral envelope protein that forms a disulfide-linked complex with a second virion structural protein.An endoplasmic reticulum-retained herpes simplex virus glycoprotein H is absent from secreted virions: evidence for reenvelopment during egress.DNA sequence of the herpes simplex virus type 1 gene encoding glycoprotein gH, and identification of homologues in the genomes of varicella-zoster virus and Epstein-Barr virus.Use of lambda gt11 to isolate genes for two pseudorabies virus glycoproteins with homology to herpes simplex virus and varicella-zoster virus glycoproteinsUse of lambda gt11 and monoclonal antibodies to map the genes for the six major glycoproteins of equine herpesvirus 1Live visualization of herpes simplex virus type 1 compartment dynamicsCharacterization of baculovirus-expressed herpes simplex virus type 1 glycoprotein K.Localization and putative function of the UL20 membrane protein in cells infected with herpes simplex virus 1.The UL10 gene of herpes simplex virus 1 encodes a novel viral glycoprotein, gM, which is present in the virion and in the plasma membrane of infected cells.A mutant herpes simplex virus type 1 unable to express glycoprotein L cannot enter cells, and its particles lack glycoprotein HDifferential rates of processing and transport of herpes simplex virus type 1 glycoproteins gB and gC.Characterization and sequence analyses of antibody-selected antigenic variants of herpes simplex virus show a conformationally complex epitope on glycoprotein H.Herpes simplex virus particles are unable to traverse the secretory pathway in the mouse L-cell mutant gro29.Oligomer formation of the gB glycoprotein of herpes simplex virus type 1.Protection from herpes simplex virus type 1 lethal and latent infections by secreted recombinant glycoprotein B constitutively expressed in human cells with a BK virus episomal vector.Characterization of the antigenic structure of herpes simplex virus type 1 glycoprotein C through DNA sequence analysis of monoclonal antibody-resistant mutants.Identification of C3b-binding regions on herpes simplex virus type 2 glycoprotein CEntry of herpes simplex virus 1 in BJ cells that constitutively express viral glycoprotein D is by endocytosis and results in degradation of the virusNeutralizing antibodies specific for glycoprotein H of herpes simplex virus permit viral attachment to cells but prevent penetrationPathogenicity in mice of herpes simplex virus type 2 mutants unable to express glycoprotein CAntigenic variation (mar mutations) in herpes simplex virus glycoprotein B can induce temperature-dependent alterations in gB processing and virus production.Identification of the Epstein-Barr virus gp85 gene.
P2860
Q21263104-C5FA2BA6-7FFE-46FD-91BA-EA8DA4F7195BQ24604871-0520DABF-7CAA-4872-BA68-0B3CFC339C6EQ24655638-042BE502-F5F5-4E2F-8AC9-1B19C32537CEQ27663096-8AEACF59-CD4A-4688-B160-22B95902F03BQ30441453-48249B1C-0D58-448A-92F5-AC95C132058BQ33781867-BF01A78D-A0D0-4BAE-BC71-3DA3427ED363Q33782593-FC686BA2-E963-45FD-908B-28E4742F2F45Q33783740-B8E8BFB2-243B-4D1E-B68F-87066D319BC3Q33785730-B2FA2E06-980A-427B-AA5F-BB77186A85EFQ33927513-56A7D79A-2516-4F96-9AE6-298B02596068Q33931805-4D52E9EC-A5B3-4145-8A71-559C4318967AQ33932322-436F5292-5A8A-4D70-942E-E1947CE033AEQ34285628-D8E35B52-7295-4AF1-A129-427ED7C12268Q34435088-1D7FD56B-60FE-4898-9728-EB021641C5CCQ34593833-5778CF12-F04C-4417-98AD-411F3FEE51B0Q35020198-78F2DD4B-CBEF-437C-8461-8D279F58C3D6Q35804208-7E43E149-87BD-4C3E-997B-011B9B4287DDQ35839400-34C65E07-4BB5-47B3-BDAB-E65EF87439F4Q35856101-5D713147-949E-4505-8057-42247194FE3FQ35863489-FFD6E169-6BAE-4B6E-A4EE-DC7A5B88B0B7Q36099945-030E7741-45FB-4C8F-9A23-9AE77204B22DQ36425586-A669BBEB-2C66-4D67-9AA2-62EDD1CFB91CQ36427073-FEC6FD1B-CB99-4D34-BF5B-E5315184A20DQ36594186-95D87BAE-316C-4F4C-B79A-2A522549AD84Q36631832-8BC644C7-2F08-48E1-AA97-ACF5C4E087E7Q36637226-13A5DD30-F42A-449C-B4A6-B8DCDF51C812Q36643531-92D70744-8B04-42F8-960A-532B11141519Q36686818-9EAB7C8A-862F-41FC-9A63-0127CA400870Q36688245-F5713170-04BC-4558-98A8-614E68C8DB32Q36688739-753BA8DD-14A1-4048-A1C4-B01F28453726Q36795629-8F21CBB4-2767-401A-B831-ADEA05DB40EDQ36797314-DDEE5951-3E59-4813-BA4C-2D0F0B5BBAB5Q36799854-FD45B4C9-2A83-431C-9EBC-7403B58E000EQ36801252-059A3EEB-0E60-4538-B5BD-80D267D646D1Q36804841-2C243454-3E77-4372-B94F-A09BBBB7B72EQ36825917-855DF790-2FBD-4A64-8CEB-54535C223A35Q36829924-ED5A0A13-AE03-4799-93D1-A0260D544B12Q36860736-46A20BC2-7FA5-4313-8BED-6A0A70EE02E2Q36864290-5EFA2780-EEB3-46C5-B559-D0FA9DE2A437Q36865571-6F40D91E-E39F-4402-8439-60478CB49DD2
P2860
Characterisation and physical mapping of an HSV-1 glycoprotein of approximately 115 X 10(3) molecular weight.
description
1984 nî lūn-bûn
@nan
1984年の論文
@ja
1984年学术文章
@wuu
1984年学术文章
@zh
1984年学术文章
@zh-cn
1984年学术文章
@zh-hans
1984年学术文章
@zh-my
1984年学术文章
@zh-sg
1984年學術文章
@yue
1984年學術文章
@zh-hant
name
Characterisation and physical mapping of an HSV-1 glycoprotein of approximately 115 X 10
@nl
Characterisation and physical ...... 115 X 10(3) molecular weight.
@en
type
label
Characterisation and physical mapping of an HSV-1 glycoprotein of approximately 115 X 10
@nl
Characterisation and physical ...... 115 X 10(3) molecular weight.
@en
prefLabel
Characterisation and physical mapping of an HSV-1 glycoprotein of approximately 115 X 10
@nl
Characterisation and physical ...... 115 X 10(3) molecular weight.
@en
P2093
P1433
P1476
Characterisation and physical ...... 115 X 10(3) molecular weight.
@en
P2093
Buckmaster EA
P304
P356
10.1016/0042-6822(84)90387-8
P407
P577
1984-12-01T00:00:00Z