about
Identification and characterization of a novel retroviral-like aspartic protease specifically expressed in human epidermisCleavage of human and mouse cytoskeletal and sarcomeric proteins by human immunodeficiency virus type 1 protease. Actin, desmin, myosin, and tropomyosinStructure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypesStructural studies of the retroviral proteinase from avian myeloblastosis associated virusNon-viral cellular substrates for human immunodeficiency virus type 1 proteaseIn vitro antiviral activity of AG7088, a potent inhibitor of human rhinovirus 3C proteaseLiposome-mediated delivery of antiviral agents to human immunodeficiency virus-infected cells.Human immunodeficiency virus type 1 protease cleaves the intermediate filament proteins vimentin, desmin, and glial fibrillary acidic protein.Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyproteinVaccinia virus proteolysis--a review.Determinants of substrate recognition by poliovirus 2A proteinaseThe role of proteolytic processing in the morphogenesis of virus particles.Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymesFirst generation inhibitors of the adenovirus proteinaseA rapid method for determination of endoproteinase substrate specificity: specificity of the 3C proteinase from hepatitis A virus.Viruses and viral proteins.An antiviral peptide inhibitor that is active against picornavirus 2A proteinases but not cellular caspases.Protease inhibitors as antiviral agents.Characterization of the Epstein-Barr virus proteinase and comparison with the human cytomegalovirus proteinase.The spacer peptide between human immunodeficiency virus capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivitySpecific in vitro cleavage of a Leishmania virus capsid-RNA-dependent RNA polymerase polyprotein by a host cysteine-like proteaseSpecific inhibitor of human immunodeficiency virus proteinase prevents the cytotoxic effects of a single-chain proteinase dimer and restores particle formation.Mutagenesis of protease cleavage sites in the human immunodeficiency virus type 1 gag polyprotein.Expression of active human immunodeficiency virus type 1 protease by noninfectious chimeric virus particles.Recent development in the design of antiviral agents.Cystatins in health and disease.An engineered retroviral proteinase from myeloblastosis associated virus acquires pH dependence and substrate specificity of the HIV-1 proteinase.Configurations of diastereomeric hydroxyethylene isosteres strongly affect biological activities of a series of specific inhibitors of human-immunodeficiency-virus proteinase.Human immunodeficiency virus type-1 reverse transcriptase and ribonuclease H as substrates of the viral protease.High-level expression of enzymatically active bovine leukemia virus proteinase in E. coli.Mengo virus 3C proteinase: recombinant expression, intergenus substrate cleavage and localization in vivo.Sub-site preferences of the aspartic proteinase from the human immunodeficiency virus, HIV-1.Endopeptidase variations among different life-cycle stages of African trypanosomes.Proteases and protease inhibitors in infectious diseases.A transient precursor of the HIV-1 protease. Isolation, characterization, and kinetics of maturation.Intrinsic activity of precursor forms of HIV-1 proteinase.Mutating P2 and P1 residues at cleavage junctions in the HIV-1 pol polyprotein. Effects on hydrolysis by HIV-1 proteinase.
P2860
Q24314564-23F0C959-8670-4F01-BB93-3DAF3BEDBC4DQ24676673-8B53B454-B12C-4F66-A611-50F5316033E3Q27619756-E6112109-2739-4046-8FEC-FCE017CB1ACDQ27642090-AE3632A3-565B-44AD-B136-B31EEC819C8AQ28264830-FB1C5D09-A083-4750-A671-EAD7D0733C2FQ28343611-A232F9E6-74D1-41B9-B590-6C83F56953F6Q33637970-3644685F-9999-408D-BA48-0628A11FD501Q33750683-BE68543B-3D50-410A-9347-DD645FBD563EQ35675295-C49BD85F-B94E-4403-B06E-975FE1E8072BQ36482612-B57DA6FB-BE08-4DE7-A1D8-A78B3ED98C22Q36697851-D71EAD8C-7E2A-4E2E-96F0-977978F3ABA7Q36777585-0CC6B6E2-7CC5-4B03-97C3-1D1A2530ED57Q37059742-BAEA2181-D833-4114-A8BE-F4EC2D5D262BQ37262441-0D16DB86-E82E-4D48-BB3B-FB304E1FBE09Q37651614-CCF7E75C-7D8E-4655-817A-C4F35B7C3327Q38284963-19B87EBC-1A98-4C76-B9D5-B3B44FA42597Q38760904-D4A9FAA5-B20B-40A6-9B68-AE7221501B86Q39468942-178174F0-B3E5-43FF-BE9A-9DB560F25772Q39868895-1FDCA356-F308-449A-9899-E43E13A74D71Q39870242-B216EC76-9291-4807-80AF-5B0AD6C7F7A9Q40015256-58AA4E0D-9237-4D34-A6C2-E76CFB53E9A6Q40049266-CE1BB08B-5C42-438F-B941-4C3E3F9711F0Q40059062-CF201661-62CB-4169-BB6C-6662EA8B209DQ40064802-2A546048-413D-4206-9AF0-D9E5B0EDF3D7Q40943840-D1371D2E-A191-4FE0-A8A5-22BB599D2747Q41161690-DF2009F8-5D4C-49A0-A03F-CC7DE664B474Q41519480-9EAA06FC-3346-4C1B-9299-1169022BEBBDQ42545682-120EAE65-6809-4720-87E2-B8E0F9EE7FF2Q42842599-8B853E27-5EB2-448E-A44A-58F35EE339DDQ44135902-3681A50C-A58A-4053-8334-7980C4BA844DQ45765662-55AA6235-FD27-49F3-ADEC-63907C2086CAQ45850256-69787BA7-810F-4EFA-804D-58234B52D341Q46449921-9498CF89-DE6B-493B-9374-76E0EE6BC957Q47576680-5B16982B-257C-4482-9E3B-EBBCFBE69B2DQ52202674-FCC3F0F1-D4AF-4DB4-9FF1-5098F88DA544Q54667327-C709D170-BAC7-4837-95E2-91B6FE3CA5E8Q54695804-27CFBA3D-5CC7-4072-9A7D-43B5E6D8773F
P2860
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年学术文章
@wuu
1990年学术文章
@zh-cn
1990年学术文章
@zh-hans
1990年学术文章
@zh-my
1990年学术文章
@zh-sg
1990年學術文章
@yue
1990年學術文章
@zh
1990年學術文章
@zh-hant
name
Viral proteinases: weakness in strength.
@en
type
label
Viral proteinases: weakness in strength.
@en
prefLabel
Viral proteinases: weakness in strength.
@en
P1476
Viral proteinases: weakness in strength.
@en
P356
10.1016/0167-4781(90)90015-T
P407
P577
1990-01-01T00:00:00Z