Mutations in the Ty3 major homology region affect multiple steps in Ty3 retrotransposition.
about
Determinants of Genomic RNA Encapsidation in the Saccharomyces cerevisiae Long Terminal Repeat Retrotransposons Ty1 and Ty3Domain-swapped dimerization of the HIV-1 capsid C-terminal domainA triclinic crystal structure of the carboxy-terminal domain of HIV-1 capsid protein with four molecules in the asymmetric unit reveals a novel packing interfaceTy3 capsid mutations reveal early and late functions of the amino-terminal domainInvestigation by atomic force microscopy of the structure of Ty3 retrotransposon particles.Viral DNA synthesis defects in assembly-competent Rous sarcoma virus CA mutants.How HIV-1 Gag assembles in cells: Putting together pieces of the puzzle.Suppression of a morphogenic mutant in Rous sarcoma virus capsid protein by a second-site mutation: a cryoelectron tomography study.Gag proteins of Drosophila telomeric retrotransposons: collaborative targeting to chromosome ends.Schizosaccharomyces pombe retrotransposon Tf2 mobilizes primarily through homologous cDNA recombination.Proline residues in human immunodeficiency virus type 1 p6(Gag) exert a cell type-dependent effect on viral replication and virion incorporation of Pol proteins.Two-hybrid analysis of Ty3 capsid subdomain interactionsElement-specific localization of Drosophila retrotransposon Gag proteins occurs in both nucleus and cytoplasm.Heterogeneous terminal structure of Ty1 and Ty3 reverse transcriptsEssential domains for ribonucleoprotein complex formation required for retrotransposition of telomere-specific non-long terminal repeat retrotransposon SART1A long terminal repeat-containing retrotransposon of Schizosaccharomyces pombe expresses a Gag-like protein that assembles into virus-like particles which mediate reverse transcription.Biophysical analysis of the MHR motif in folding and domain swapping of the HIV capsid protein C-terminal domain.Intracellular targeting of Gag proteins of the Drosophila telomeric retrotransposonsSequence requirements for localization and packaging of Ty3 retroelement RNA.Critical role of conserved hydrophobic residues within the major homology region in mature retroviral capsid assembly.Cooperative role of the MHR and the CA dimerization helix in the maturation of the functional retrovirus capsidMolecular Architecture of the Retroviral Capsid.Origin, antiviral function and evidence for positive selection of the gammaretrovirus restriction gene Fv1 in the genus Mus.Comprehensive analysis of human immunodeficiency virus type 1-specific CD4 responses reveals marked immunodominance of gag and nef and the presence of broadly recognized peptides.Mutations of Conserved Residues in the Major Homology Region Arrest Assembling HIV-1 Gag as a Membrane-Targeted Intermediate Containing Genomic RNA and Cellular Proteins.Pyret, a Ty3/Gypsy retrotransposon in Magnaporthe grisea contains an extra domain between the nucleocapsid and protease domains.Functional surfaces of the human immunodeficiency virus type 1 capsid protein.Formation of RNA Granule-Derived Capsid Assembly Intermediates Appears To Be Conserved between Human Immunodeficiency Virus Type 1 and the Nonprimate Lentivirus Feline Immunodeficiency Virus.
P2860
Q26739675-1D1F28B7-5A84-473C-9DBA-24A2E587712DQ27644067-8A43A990-A7C7-495B-B5DD-B2B5955A776BQ27678401-00D4EDA6-5001-41A6-8BEA-61129261D073Q27931343-B0E8F099-405C-4DD6-86AF-CF828FC44B21Q27931628-6AD9437D-A761-4698-A6F0-1C92306CFC16Q30327614-D1E64F03-6A6D-4C7D-833D-504590E64739Q33358839-DD55F7CC-A57B-4C95-8A89-5F32AE2EA252Q33567553-34BC0C7D-1020-43AA-8489-57761A7BA1EFQ33752592-CFC4FD78-275E-400E-8107-1284C627A392Q33781601-A3CB4A9D-E574-482F-AFD4-C20079FB59D9Q33813648-6D1EDD99-FAE3-4A85-BE27-4532042B35DFQ33884329-A94A94B5-8FD7-47A7-BDC7-5DC1667C4292Q34019412-C0D35A09-B571-482A-B585-1342F60638DFQ34630021-92A36C25-CAD0-4D87-9EDC-5D5FDA8EAE82Q34718262-1E02EBD1-C3DF-4E91-A014-0E95C6F7E939Q34975957-62EE49B0-9972-49A4-A0D8-A788B00182F1Q34996596-D79C1F16-9073-4BC9-8174-316F43EB75DEQ34996849-72665045-BF0A-488B-AB68-71698A290FA9Q36626099-45D903F9-05D0-4137-BFF1-8EA5BED76AAFQ36673166-837049C0-11D8-47B6-92F7-6BD59A30E29FQ36776033-ED673533-005B-467B-8A9C-B26AC710BE0CQ36934635-EC749367-5F37-4825-B2CE-9E418AAD7DFEQ37117741-EE7B7610-A619-4359-9B2D-EB6878DFF727Q37422520-E4917171-D74D-48C8-A573-6F2D0878E24EQ38812540-1899F706-F43F-478F-BF60-A9A05BB2CD6FQ39229337-0DFF60C0-A570-42B7-A1FD-714C7DAB0D3EQ39748566-1413BB3A-AC07-43EB-97BB-F681AA5D0B5AQ52375200-72BC4C77-A008-4F73-9F97-0B9FF69EBA9C
P2860
Mutations in the Ty3 major homology region affect multiple steps in Ty3 retrotransposition.
description
1996 nî lūn-bûn
@nan
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
1996年论文
@zh
1996年论文
@zh-cn
name
Mutations in the Ty3 major hom ...... eps in Ty3 retrotransposition.
@en
Mutations in the Ty3 major hom ...... eps in Ty3 retrotransposition.
@nl
type
label
Mutations in the Ty3 major hom ...... eps in Ty3 retrotransposition.
@en
Mutations in the Ty3 major hom ...... eps in Ty3 retrotransposition.
@nl
prefLabel
Mutations in the Ty3 major hom ...... eps in Ty3 retrotransposition.
@en
Mutations in the Ty3 major hom ...... eps in Ty3 retrotransposition.
@nl
P2093
P2860
P1433
P1476
Mutations in the Ty3 major hom ...... teps in Ty3 retrotransposition
@en
P2093
P2860
P304
P407
P577
1996-06-01T00:00:00Z