Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein
about
Structural and kinetic analysis of drug resistant mutants of HIV-1 proteaseSolution structure of the mature HIV-1 protease monomer: insight into the tertiary fold and stability of a precursorPotent nonnucleoside reverse transcriptase inhibitors target HIV-1 Gag-PolGag-Pol processing during HIV-1 virion maturation: a systems biology approachA Functional Interplay between Human Immunodeficiency Virus Type 1 Protease Residues 77 and 93 Involved in Differential Regulation of Precursor Autoprocessing and Mature Protease ActivityKinetic characterization of the critical step in HIV-1 protease maturationUnderstanding HIV-1 protease autoprocessing for novel therapeutic development.Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease.Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes.Assembly and processing of human immunodeficiency virus Gag mutants containing a partial replacement of the matrix domain by the viral protease domainActivation of the Mason-Pfizer monkey virus protease within immature capsids in vitroVirion instability of human immunodeficiency virus type 1 reverse transcriptase (RT) mutated in the protease cleavage site between RT p51 and the RT RNase H domain.Maturation mechanism of severe acute respiratory syndrome (SARS) coronavirus 3C-like proteinase.Placement of leucine zipper motifs at the carboxyl terminus of HIV-1 protease significantly reduces virion production.Molecular basis for substrate recognition and drug resistance from 1.1 to 1.6 angstroms resolution crystal structures of HIV-1 protease mutants with substrate analogs.Proline residues within spacer peptide p1 are important for human immunodeficiency virus type 1 infectivity, protein processing, and genomic RNA dimer stability.The nature of the N-terminal amino acid residue of HIV-1 RNase H is critical for the stability of reverse transcriptase in viral particles.Human immunodeficiency virus (HIV) type 1 transframe protein can restore activity to a dimerization-deficient HIV protease variant.Gag-Pol Transframe Domain p6* Is Essential for HIV-1 Protease-Mediated Virus Maturation.A critical proteolytic cleavage site near the C terminus of the yeast retrotransposon Ty1 Gag protein.The Race against Protease Activation Defines the Role of ESCRTs in HIV BuddingMechanism of dissociative inhibition of HIV protease and its autoprocessing from a precursor.Analysis of resistance to human immunodeficiency virus type 1 protease inhibitors by using matched bacterial expression and proviral infection vectorsThe HIV-1 late domain-2 S40A polymorphism in antiretroviral (or ART)-exposed individuals influences protease inhibitor susceptibilityBinding of Clinical Inhibitors to a Model Precursor of a Rationally Selected Multidrug Resistant HIV-1 Protease Is Significantly Weaker Than That to the Released Mature EnzymeUncoupling human immunodeficiency virus type 1 Gag and Pol reading frames: role of the transframe protein p6* in viral replication.Interactions of different inhibitors with active-site aspartyl residues of HIV-1 protease and possible relevance to pepsin.A real-time killing assay to follow viral epitope presentation to CD8 T cellsC-Terminal HIV-1 Transframe p6* Tetrapeptide Blocks Enhanced Gag Cleavage Incurred by Leucine Zipper Replacement of a Deleted p6* Domain.Cleavage of human immunodeficiency virus type 1 proteinase from the N-terminally adjacent p6* protein is essential for efficient Gag polyprotein processing and viral infectivity.Ty1 proteolytic cleavage sites are required for transposition: all sites are not created equal.Importance of the N terminus of rous sarcoma virus protease for structure and enzymatic function.The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage.Cysteine 95 and other residues influence the regulatory effects of Histidine 69 mutations on Human Immunodeficiency Virus Type 1 protease autoprocessing.Formation of transient dimers by a retroviral protease.Characterization of the protease of a fish retrovirus, walleye dermal sarcoma virus.Analysis of cleavage site mutations between the NC and PR Gag domains of Rous sarcoma virusImportance of protease cleavage sites within and flanking human immunodeficiency virus type 1 transframe protein p6* for spatiotemporal regulation of protease activation.Reaction-diffusion basis of retroviral infectivity.The maturation of HIV-1 protease precursor studied by discrete molecular dynamics.
P2860
Q27619254-3E6A6632-1EEF-42B9-AA9D-1B7EAA615882Q27641889-74C729D4-7D76-41B5-9BB1-D741173882D9Q28469069-BFC6B617-5318-4567-B185-C85187DB64A0Q28533696-CCB8781A-DF67-4C8D-A5A2-375076A34AFFQ28546560-D899E9FF-0C70-4D61-BD62-BF2D5A488977Q30530468-29C1CA95-ADC5-405B-8721-F4494B6E72C2Q33356201-D5449C03-B9C1-4BBC-823E-909EB99D98ADQ33559311-8504AD05-B9DC-49B3-AE28-AB3571E75AE0Q33671554-42E4BE8B-0BD5-45A0-9877-54E5FEDD0E4CQ33801779-420C0CCE-8204-4162-8C74-A05750462ED3Q33952099-F93AA118-2F9E-4F8B-A94F-C3AC74F7D5ABQ33987368-EA048E1D-BA8A-4334-B90B-6687B721475DQ34107407-FFFF81B6-88CF-4313-B65B-0BCF71A2C7F9Q34187294-4320E488-BEAD-4CA3-B73A-3A9CF26E4E11Q34334101-C5C2AB19-07A6-40CB-A9BB-2EA689A4EC26Q34354549-D569D80A-B039-4A94-9654-1C54D2104389Q34991047-D1DBCF7A-CB37-4A9F-A378-C95E966BE5CBQ35155106-2003975F-68F9-4F4F-8890-0CF4EB7B1A46Q35672342-87403BDE-D7F2-4B4E-A6A9-009EB5C266F3Q35866466-9C783DC1-4BC5-45CF-905E-2F6CD53168E1Q36046317-5692F4EB-28DD-4389-A467-95F65F71AB7EQ36162047-EC347410-00C2-47CA-82B1-09C21E64ADDEQ36689848-C899EE44-D8CB-4EE5-8586-C86FF70AAF88Q37233259-E53E19F3-F673-40A5-AE71-2F7DA6DB83F9Q37237447-B1F31AEA-72D5-437F-8444-7679B592326EQ37248021-4EAE4583-846A-476D-89E0-3C0CFAC7AEA5Q37286930-D6475101-097E-4C8D-904C-1D9818A99912Q37352748-7D4EDCDB-888D-4079-A3E4-259BACA2C65BQ38934936-8FA538BC-5E3D-4930-80A0-D09F846363D7Q39579642-A7E553D1-0EC8-450E-85FE-9566FD85E121Q39601419-43E844E8-8531-47BF-8498-5DDA7C85DD9FQ39602769-BFCBC466-3764-41EC-89E2-0F34796DC327Q39698249-DADA31CD-C7CC-4078-8D9A-E1BFF268E2E8Q39724170-0F92855E-6CA1-4D62-93A3-C72EF1C3D188Q39742958-8656E5C1-79D6-459D-9EAB-D1AE659BA64FQ39752728-063E170B-8780-4EE6-A928-006D6590AFBEQ39877732-7EED4B26-AF70-4021-850A-C9744092CDF9Q40005589-425296A0-EC5F-4A6D-94F8-082A309A9B05Q40518477-92221977-A0E2-44C3-ACF1-C096E0076F71Q41815499-CCF2F851-C01F-4B22-83ED-1C4712009888
P2860
Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Kinetics and mechanism of auto ...... log of the Gag-Pol polyprotein
@ast
Kinetics and mechanism of auto ...... log of the Gag-Pol polyprotein
@en
type
label
Kinetics and mechanism of auto ...... log of the Gag-Pol polyprotein
@ast
Kinetics and mechanism of auto ...... log of the Gag-Pol polyprotein
@en
prefLabel
Kinetics and mechanism of auto ...... log of the Gag-Pol polyprotein
@ast
Kinetics and mechanism of auto ...... log of the Gag-Pol polyprotein
@en
P2093
P2860
P356
P1476
Kinetics and mechanism of auto ...... log of the Gag-Pol polyprotein
@en
P2093
P2860
P304
P356
10.1073/PNAS.91.17.7970
P407
P577
1994-08-01T00:00:00Z