Mutations within the proteolytic cleavage site of the Rous sarcoma virus glycoprotein define a requirement for dibasic residues for intracellular cleavage.
about
RNA dimerization defect in a Rous sarcoma virus matrix mutant.Mutational analysis of the subgroup A avian sarcoma and leukosis virus putative fusion peptide domain.Mapping of receptor binding domains in the envelope protein of spleen necrosis virusViral DNA synthesis defects in assembly-competent Rous sarcoma virus CA mutants.Novel monoclonal antibody directed at the receptor binding site on the avian sarcoma and leukosis virus Env complexEndoproteolytic processing of the ebola virus envelope glycoprotein: cleavage is not required for function.Characterization of the proline-rich region of murine leukemia virus envelope protein.Failure To cleave murine leukemia virus envelope protein does not preclude its incorporation in virions and productive virus-receptor interactiontrans-acting inhibition of genomic RNA dimerization by Rous sarcoma virus matrix mutantsHIV-1 interacts with human endogenous retrovirus K (HML-2) envelopes derived from human primary lymphocytes.The Rous sarcoma virus Env glycoprotein contains a highly conserved motif homologous to tyrosine-based endocytosis signals and displays an unusual internalization phenotypeCytoplasmic tail of Moloney murine leukemia virus envelope protein influences the conformation of the extracellular domain: implications for mechanism of action of the R Peptide.Furin cleavage potentiates the membrane fusion-controlling intersubunit disulfide bond isomerization activity of leukemia virus Env.Cooperative cleavage of the R peptide in the Env trimer of Moloney murine leukemia virus facilitates its maturation for fusion competence.Mutations within a putative cysteine loop of the transmembrane protein of an attenuated immunodeficiency-inducing feline leukemia virus variant inhibit envelope protein processing.Genetic analysis of the major homology region of the Rous sarcoma virus Gag protein.Analysis of the cleavage site of the human immunodeficiency virus type 1 glycoprotein: requirement of precursor cleavage for glycoprotein incorporationDifferential proteolytic processing leads to multiple forms of the CA protein in avian sarcoma and leukemia viruses.A large region within the Rous sarcoma virus matrix protein is dispensable for budding and infectivityRetroviral env glycoprotein trafficking and incorporation into virions.Ancestral Mutations Acquired in Refrex-1, a Restriction Factor against Feline Retroviruses, during its Cooption and Domestication.Stabilization of TM trimer interactions during activation of moloney murine leukemia virus Env.Modifications in the binding domain of avian retrovirus envelope protein to redirect the host range of retroviral vectors.Microglial infection by a neurovirulent murine retrovirus results in defective processing of envelope protein and intracellular budding of virus particles.A chimeric avian retrovirus containing the influenza virus hemagglutinin gene has an expanded host rangeIdentification of residues outside of the receptor binding domain that influence the infectivity and tropism of porcine endogenous retrovirus.The major site of phosphorylation within the Rous sarcoma virus MA protein is not required for replication.Two distinct mechanisms regulate recruitment of murine leukemia virus envelope protein to retroviral assembly sites.Evidence for a second function of the MA sequence in the Rous sarcoma virus Gag proteinDelayed cytopathicity of a feline leukemia virus variant is due to four mutations in the transmembrane protein gene.Endosomal proteolysis by cathepsins is necessary for murine coronavirus mouse hepatitis virus type 2 spike-mediated entry.Effect of alpha-1 antitrypsin Portland variant (alpha 1-PDX) on HIV-1 replication.A study of human furin specificity using synthetic peptides derived from natural substrates, and effects of potassium ions.A substitution in rous sarcoma virus integrase that separates its two biologically relevant enzymatic activities.Proteolytic processing is required for viral superantigen activity.
P2860
Q24524289-C290C6E6-2274-44A8-B9B1-E908BB6360FFQ24524815-14C0CE48-8FA4-4B94-BF60-2CB7F4C945EBQ28302477-0368EB87-CEB7-4797-AD8B-4F8BF7335D75Q30327614-9080BD8F-FA74-4EDE-B33C-4432877BB5C6Q30453272-DC038CAF-35CC-4FDF-AAA8-3B3471D7DD13Q33641497-31D1CFDB-2710-47AE-83C3-A21E9ECBA826Q33784874-861C3C2D-6F98-4DE7-94BD-4DD7A2289409Q33815376-2A165465-5EF5-4C1F-BDA2-A03A1174DF37Q33834799-A89ABF03-E160-47E7-A738-876FC05B6E85Q33887743-F4998B35-E1B6-4522-A6DE-626821CE0B06Q33961280-6C72C38B-212D-4200-AE42-4A144B2808E0Q34464572-0E719392-392F-4F7F-A1AB-B1120FF36F76Q34648413-6D165E06-9B90-42CA-BA69-B460C19484DCQ34742571-0B6FA91A-16BF-471B-BEF1-08C519E169B3Q35837311-A6DD506C-E363-4D22-BD77-4A7F3D29B6FDQ35841323-5D9FE473-46CD-4ABC-B610-69A6098A8D9AQ35844026-8D39998B-8FAB-43E5-BEE2-60A19851818BQ35848720-E69C14A3-0195-4BE1-8DDF-4F09BC558BD1Q35858713-D0A96C8F-A9DF-412D-9025-31EF3F83C3D0Q36090433-B3867E30-C42C-4C57-A739-2A8402F7E088Q36481475-EC816391-267E-4214-A6F8-A378782FC1DEQ36483979-5E1EE4BD-B197-4D49-B46B-A35D3F3B1633Q36622965-26744E8E-15A2-41A9-B52F-C1623A51C8C8Q36633809-24B430DA-C3E5-4781-A9BC-E42F886DEFA1Q36687350-B1791905-B2C8-45B0-BB33-C963277D657DQ38879279-AD74875D-69F7-4859-B7DA-40CC5C437DE2Q39642211-95026C26-A93B-41A8-A943-19CAA680B7B5Q39676464-0B320B25-C4C7-4850-A039-B8EE38ACE739Q39873408-826825A5-7829-4F4D-94C5-4494D41CD5B4Q40047285-51F3B3E3-0928-486A-BB2C-F63F3686A613Q40274378-E30650EA-67B2-4E52-AEBF-91DAFFCC8FBEQ40844705-02E41277-DC89-453B-8D0A-77F07D9775B9Q41878430-2F30B6F3-6CE1-4A40-B4DD-D613054EA5ADQ42026855-FC9684CE-4134-4FAF-9A2D-38438DF30B50Q42066411-50E579D1-1AD4-4985-9808-735D52F3B9FD
P2860
Mutations within the proteolytic cleavage site of the Rous sarcoma virus glycoprotein define a requirement for dibasic residues for intracellular cleavage.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Mutations within the proteolyt ...... es for intracellular cleavage.
@ast
Mutations within the proteolyt ...... es for intracellular cleavage.
@en
type
label
Mutations within the proteolyt ...... es for intracellular cleavage.
@ast
Mutations within the proteolyt ...... es for intracellular cleavage.
@en
prefLabel
Mutations within the proteolyt ...... es for intracellular cleavage.
@ast
Mutations within the proteolyt ...... es for intracellular cleavage.
@en
P2093
P2860
P1433
P1476
Mutations within the proteolyt ...... es for intracellular cleavage.
@en
P2093
P2860
P304
P407
P577
1992-02-01T00:00:00Z