Proteolytic processing of HIV-1 protease precursor, kinetics and mechanism. - Wikidata - wikimedia - TriplyDB

Proteolytic processing of HIV-1 protease precursor, kinetics and mechanism.

Proteolytic processing of HIV-1 protease precursor, kinetics and mechanism.

http://www.wikidata.org/entity/Q47940296

about

Solution structure of the mature HIV-1 protease monomer: insight into the tertiary fold and stability of a precursor The L76V Drug Resistance Mutation Decreases the Dimer Stability and Rate of Autoprocessing of HIV-1 Protease by Reducing Internal Hydrophobic Contacts Gag-Pol processing during HIV-1 virion maturation: a systems biology approach Kinetic characterization of the critical step in HIV-1 protease maturation 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.Activation of the Mason-Pfizer monkey virus protease within immature capsids in vitro Novel macromolecular inhibitors of human immunodeficiency virus-1 protease.RC1339/APRc from Rickettsia conorii is a novel aspartic protease with properties of retropepsin-like enzymes Placement of leucine zipper motifs at the carboxyl terminus of HIV-1 protease significantly reduces virion production.Analysis of natural variants of the human immunodeficiency virus type 1 gag-pol frameshift stem-loop structure Proline residues within spacer peptide p1 are important for human immunodeficiency virus type 1 infectivity, protein processing, and genomic RNA dimer stability.Inhibition of autoprocessing of natural variants and multidrug resistant mutant precursors of HIV-1 protease by clinical inhibitors.Human immunodeficiency virus (HIV) type 1 transframe protein can restore activity to a dimerization-deficient HIV protease variant.Rational design of p53, an intrinsically unstructured protein, for the fabrication of novel molecular sensors Efavirenz enhances HIV-1 gag processing at the plasma membrane through Gag-Pol dimerization Binding 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 Enzyme C-terminal residues of mature human T-lymphotropic virus type 1 protease are critical for dimerization and catalytic activity.Human immunodeficiency virus type 1 protease cleavage site mutations associated with protease inhibitor cross-resistance selected by indinavir, ritonavir, and/or saquinavir.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.Importance of protease cleavage sites within and flanking human immunodeficiency virus type 1 transframe protein p6* for spatiotemporal regulation of protease activation.Developing HIV-1 Protease Inhibitors through Stereospecific Reactions in Protein Crystals.Effect of internal cleavage site mutations in human immunodeficiency virus type 1 capsid protein on its structure and function.Non-infectious in-cell HIV-1 protease assay utilizing translocalization of a fluorescent reporter protein and apoptosis induction.Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism.Mutations Proximal to Sites of Autoproteolysis and the α-Helix That Co-evolve under Drug Pressure Modulate the Autoprocessing and Vitality of HIV-1 Protease.A Direct Interaction with RNA Dramatically Enhances the Catalytic Activity of the HIV-1 Protease In Vitro The maturation of HIV-1 protease precursor studied by discrete molecular dynamics.Folded monomer of HIV-1 protease.Probing Structural Changes among Analogous Inhibitor-Bound Forms of HIV-1 Protease and a Drug-Resistant Mutant in Solution by Nuclear Magnetic Resonance.

P2860

Q27641889-28F13812-0318-4436-B54C-9B5B639C347E Q27667353-4ABBD449-75C5-4C86-911A-00103EC46FFB Q28533696-1076F9D5-2309-4ADF-B807-C6408EA98E09 Q30530468-2C91DA46-9FAF-419B-84CF-D48A34161A85 Q33559311-2396AF87-AD34-454E-8B8D-ABAC00082B11 Q33671554-A4856DAB-D9E2-401D-AB76-54A1457A0431 Q33952099-4AD2FD8C-869A-47EE-A453-AACF39C30F62 Q33988828-D91E6319-19EF-479D-BC15-4B20093924DE Q34075786-53913C14-5BA8-4E24-BDBF-857450D16383 Q34187294-7B201754-8453-46BD-B530-F31B3C9EBA17 Q34343740-531DC206-26E3-42F3-A343-05B01B303000 Q34354549-49436D16-EFF2-4460-89C4-9FFA628148E9 Q35022049-444E01CC-4EA5-4CCA-9EDC-04192FCA6B07 Q35155106-82F63B65-1210-40DF-9AC8-710C36A659C4 Q36099479-26C0BB2C-53C5-4DD7-9583-061F38E706E9 Q36667876-96BAD5DD-AA93-484A-A552-D2095D8C8019 Q37237447-586CD055-F95E-4C7F-B56C-3D60658741B3 Q37424824-F8974464-F3F4-4D68-82CF-EA16C824F929 Q39601382-62CAFC51-8F5E-4055-BC92-074589CBC5D4 Q39724170-C8E2D549-DC60-4A64-9C3B-0A24992A473C Q39742958-C1860C42-18B5-458D-82F1-A953FF65EDDC Q39752728-E21BFA48-1060-45CF-9B24-F3AEDDDC9CF5 Q40005589-C081D997-D14B-42E3-9651-A9279D22244A Q40467926-FE25F6FF-822F-4D72-AFDD-E8E276DC947B Q40578149-24DBDF41-7AC6-4C3E-9093-3473211F42EA Q41050684-9864A666-D205-4873-BC6A-2167D77ACA11 Q41275889-E828A9DB-945A-4D24-8A75-3014F23F10A0 Q41490002-2D856E29-B0E0-4BB6-B192-9482E74D458A Q41730903-36129AB2-B262-44E6-8414-8FD785B763F7 Q41815499-883B93D4-A654-45EB-9406-954BE092BC6B Q43764692-225183AD-57F9-4364-A69B-6B02099C4EDC Q49851708-E42ACA80-16BD-4ADD-8F7C-CCE8A402139B

P2860

Proteolytic processing of HIV-1 protease precursor, kinetics and mechanism.

http://www.wikidata.org/entity/Q47940296

description

1999 nî lūn-bûn

@nan

1999年の論文

@ja

1999年学术文章

@wuu

1999年学术文章

@zh

1999年学术文章

@zh-cn

1999年学术文章

@zh-hans

1999年学术文章

@zh-my

1999年学术文章

@zh-sg

1999年學術文章

@yue

1999年學術文章

@zh-hant

name

Proteolytic processing of HIV-1 protease precursor, kinetics and mechanism.

@en

Proteolytic processing of HIV-1 protease precursor, kinetics and mechanism.

@nl

type

label

Proteolytic processing of HIV-1 protease precursor, kinetics and mechanism.

@en

Proteolytic processing of HIV-1 protease precursor, kinetics and mechanism.

@nl

prefLabel

Proteolytic processing of HIV-1 protease precursor, kinetics and mechanism.

@en

Proteolytic processing of HIV-1 protease precursor, kinetics and mechanism.

@nl

P1433

Q47940296-A59464A7-3C19-4796-B620-0EC5B76F352E

P1476

Q47940296-FD2A06E1-BEC0-43EB-81D1-DF8324170B29

P2093

Q47940296-11D3F037-028F-4FED-839F-257F7682F87C

Q47940296-252ABADA-B559-42EC-B6A4-3950B6D279EF

Q47940296-909C0A4F-64D4-4127-8EFA-C01DC363EA5D

Q47940296-9A8E2AC3-1609-41AB-907E-75A65C401E2F

Q47940296-B767B16A-82BC-4EBA-AB3B-97E0D22C99C2

P2860

Q47940296-0FF81A40-761C-41E0-B346-F07C83B97CDC

Q47940296-128F6558-EED9-4352-8A8A-38DCEE74427B

Q47940296-1C1668ED-9CE7-43F4-8330-C1F20D95EB60

Q47940296-1C69D269-9477-41D9-A880-0DF02C406F24

Q47940296-2188D8B7-9367-4BFE-8CC3-60864D0D6E97

Q47940296-23DA25C8-1416-4971-8342-F61712C647FA

Q47940296-25461B7C-836D-4DDD-AA4D-FC1B30099C5D

Q47940296-2D808A5C-7BB7-4A33-AD32-6E015588517A

Q47940296-39A51C9D-3807-414B-A931-8BC9EB66C7B9

Q47940296-7F00CDDE-1812-44A6-AAF0-4A95CB11C638

P304

Q47940296-F19BB26D-FCD5-4E26-8CC7-074C125CF146

P31

Q47940296-1599F947-311E-46B7-82FD-6FEEEFAFF53A

P356

Q47940296-8A5C9A0D-3C0B-440F-B119-466D406C776F

P407

Q47940296-5CA2DFCB-3C54-4EEE-B32D-4AF5980156D8

P433

Q47940296-E8330BAF-B651-45E9-B0FD-53609C8F3597

P478

Q47940296-AF31CFC5-4A47-4055-A580-F4A029F13D04

P577

Q47940296-E1321A02-142D-4726-8023-411F20C22D76

P5875

Q47940296-CAC9B58C-7C7B-4446-B398-0FBCB7AC3E95

P698

Q47940296-1D0DD009-4339-43C4-A36B-6F7661D903C1

P921

Q47940296-49ACDCDB-444D-4D01-8295-1D8C512BCC81

P356

JBC.274.33.23437

P1433

Journal of Biological Chemistry

P1476

Proteolytic processing of HIV-1 protease precursor, kinetics and mechanism.

@en

P2093

Kimmel AR

http://www.w3.org/2001/XMLSchema#string

Louis JM

http://www.w3.org/2001/XMLSchema#string

Nashed NT

http://www.w3.org/2001/XMLSchema#string

Wingfield PT

http://www.w3.org/2001/XMLSchema#string

Wondrak EM

http://www.w3.org/2001/XMLSchema#string

P2860

A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions

Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes

Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease

Structural basis for specificity of retroviral proteases

Use of T7 RNA polymerase to direct expression of cloned genes

Comparison of the HIV-1 and HIV-2 proteinases using oligopeptide substrates representing cleavage sites in Gag and Gag-Pol polyproteins.

Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein

Human immunodeficiency virus proteinase dimer as component of the viral polyprotein prevents particle assembly and viral infectivity.

Deletion of sequences upstream of the proteinase improves the proteolytic processing of human immunodeficiency virus type 1.

Human immunodeficiency viral protease is catalytically active as a fusion protein: characterization of the fusion and native enzymes produced in Escherichia coli.

P304

23437-23442

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.274.33.23437

http://www.w3.org/2001/XMLSchema#string

P407

P433

33

http://www.w3.org/2001/XMLSchema#string

P478

274

http://www.w3.org/2001/XMLSchema#string

P577

1999-08-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

12860307

http://www.w3.org/2001/XMLSchema#string

P698

10438521

http://www.w3.org/2001/XMLSchema#string

P921