Molecular Basis for Drug Resistance in HIV-1 Protease - Wikidata - awgldk - TriplyDB

Molecular Basis for Drug Resistance in HIV-1 Protease

Molecular Basis for Drug Resistance in HIV-1 Protease

http://www.wikidata.org/entity/Q35260370

about

Current perspectives on HIV-1 antiretroviral drug resistance Malarial dihydrofolate reductase as a paradigm for drug development against a resistance-compromised target Small Molecule Regulation of Protein Conformation by Binding in the Flap of HIV Protease HIV-1 Protease-Substrate Coevolution in Nelfinavir Resistance Expanding the Binding Envelope of CYP51 Inhibitors TargetingTrypanosoma cruziwith 4-Aminopyridyl-Based Sulfonamide Derivatives Avibactam and Class C -Lactamases: Mechanism of Inhibition, Conservation of the Binding Pocket, and Implications for Resistance Thermodynamic and structural analysis of HIV protease resistance to darunavir - analysis of heavily mutated patient-derived HIV-1 proteases Diverse inhibitor chemotypes targeting Trypanosoma cruzi CYP51 Identification of novel HIV 1--protease inhibitors: application of ligand and structure based pharmacophore mapping and virtual screening GalaxyHomomer: a web server for protein homo-oligomer structure prediction from a monomer sequence or structure Dynamical basis for drug resistance of HIV-1 protease.A multifaceted analysis of HIV-1 protease multidrug resistance phenotypes HIV-1 antiretroviral resistance: scientific principles and clinical applications Structural basis and distal effects of Gag substrate coevolution in drug resistance to HIV-1 protease X-ray solution scattering studies of the structural diversity intrinsic to protein ensembles Natural polymorphisms and unusual mutations in HIV-1 protease with potential antiretroviral resistance: a bioinformatic analysis.Multi-step inhibition explains HIV-1 protease inhibitor pharmacodynamics and resistance.Genetic Changes in HIV-1 Gag-Protease Associated with Protease Inhibitor-Based Therapy Failure in Pediatric Patients.In Silico and In Vitro Comparison of HIV-1 Subtypes B and CRF02_AG Integrases Susceptibility to Integrase Strand Transfer Inhibitors.From antiretroviral therapy access to provision of third line regimens: evidence of HIV Drug resistance mutations to first and second line regimens among Ugandan adults.Differential Flap Dynamics in Wild-type and a Drug Resistant Variant of HIV-1 Protease Revealed by Molecular Dynamics and NMR Relaxation.Contribution of Gag and Protease to HIV-1 Phenotypic Drug Resistance in Pediatric Patients Failing Protease Inhibitor-Based Therapy.The Path of Least Resistance: Mechanisms to Reduce Influenza's Sensitivity to Oseltamivir Prototypical Recombinant Multi-Protease-Inhibitor-Resistant Infectious Molecular Clones of Human Immunodeficiency Virus Type 1 Epistasis and Pleiotropy Affect the Modularity of the Genotype-Phenotype Map of Cross-Resistance in HIV-1 Strategies for lead discovery: application of footprint similarity targeting HIVgp41.Computing Clinically Relevant Binding Free Energies of HIV-1 Protease Inhibitors.Enhancing protein backbone binding--a fruitful concept for combating drug-resistant HIV.From crystal to compound: structure-based antimalarial drug discovery.Resistance mechanism of human immunodeficiency virus type-1 protease to inhibitors: A molecular dynamic approach.Evolution of gag and gp41 in Patients Receiving Ritonavir-Boosted Protease Inhibitors.Room Temperature Neutron Crystallography of Drug Resistant HIV-1 Protease Uncovers Limitations of X-ray Structural Analysis at 100 K.Understanding the basis of I50V-induced affinity decrease in HIV-1 protease via molecular dynamics simulations using polarized force field.Protease-Mediated Maturation of HIV: Inhibitors of Protease and the Maturation Process Quantitative assessment of in vivo HIV protease activity using genetically engineered QD-based FRET probes.Gp41 and Gag amino acids linked to HIV-1 protease inhibitor-based second-line failure in HIV-1 subtype A from Western Kenya.Forbidden Coherence Transfer of 19F Nuclei to Quantitatively Measure the Dynamics of a CF₃-Containing Ligand in Receptor-Bound States.Interchain hydrophobic clustering promotes rigidity in HIV-1 protease flap dynamics: new insights from molecular dynamics.

P2860

Q26852626-0F576191-357D-4915-A4E6-788863436695 Q27674154-A7BF0004-E1BB-437C-967B-BAF68510CAB0 Q27677124-7DBE29B3-1809-475F-8DDA-CB28A71FDA9D Q27683192-94E8171F-4E4E-4DB4-B39B-BADE36C1A279 Q27683570-E3F5507E-B702-4A53-A1C7-948B13FBCA33 Q27684678-98802D40-9965-4477-AE27-57A40FA57A39 Q27690132-A8DC5E61-57B3-4B72-92EF-3F4CC09C10B5 Q28481694-A3944677-2954-40C7-8517-CA30A671263C Q28485115-575888F3-04FD-448E-A2DE-8826FBBE4621 Q30400859-4F66D687-B03A-44B1-9E65-2F5809CBD8E6 Q33955900-125CCA69-1595-440A-BE75-B6872F3952CD Q34102058-F5D953BB-EBEE-4B5D-B875-36886B3DC3C1 Q34280466-7F1DB0E3-FE29-45E3-B0E8-B225E0F835B7 Q34526179-8A80BA41-7AF0-4107-AFB6-06EB779F7D68 Q35011839-BC338940-ED76-4D60-89A4-E592F80850E6 Q35120811-BF110B35-3E6F-41C6-B7F9-009249F529D4 Q35237575-68EFA436-56B0-4A96-9C1C-4DE83918467D Q35942373-BDD840BB-DDE6-4131-BFD9-2CBDFBB5DB0E Q36099861-1BB487F5-8376-42BE-A170-B7D06BE29147 Q36232454-66F250D9-37AE-44DA-A7BC-D431342305E8 Q36378725-FDF0803F-9888-411F-A4F8-81F6CF9D84A8 Q36729996-BBAB00F8-96AE-47AC-B7B5-6C2050635089 Q36949865-916AA2FD-3DEA-4791-9812-27418FA47A7F Q37124113-5EA1EB05-CCBD-4AB9-B5B0-715586AECCC9 Q37400449-0EED07E6-D3A4-4DA3-BEE5-92D79A642268 Q37552860-BABEA820-6ECE-4A8A-8262-1198F9173DF8 Q37665027-7B63ECB1-7C08-4AB3-BEA6-627B08E97D3A Q37980084-ED604FCD-1ED4-4F78-9000-2966F4686E37 Q38227796-5CEC5ECB-2E29-4B20-8F83-C9DE0C270752 Q39092859-0A113313-E34E-4345-818A-D4D00113DE47 Q40039995-8710D1BF-12AA-4D7E-B47F-FF05CE6787B7 Q40336902-403B7614-5E91-43DB-BCBA-08C3109EC937 Q41096987-457B5999-64D6-4343-BABA-930E27837177 Q41844750-4B0EE480-8A33-4C1A-9FB4-81184C4A2BA6 Q42240414-8C88FDF2-7D1D-4759-ADB5-22F4D88F8D3D Q47810732-96C87688-EE44-444A-9468-68672225E8E3 Q47843515-EE929FCF-DCAC-4F21-B8A3-D9F3A35C1A61 Q50894892-499696FC-49BE-4F58-BB98-648D9C8CB3A1

P2860

Molecular Basis for Drug Resistance in HIV-1 Protease

http://www.wikidata.org/entity/Q35260370

description

2010 nî lūn-bûn

@nan

2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Molecular Basis for Drug Resistance in HIV-1 Protease

@ast

Molecular Basis for Drug Resistance in HIV-1 Protease

@en

type

label

Molecular Basis for Drug Resistance in HIV-1 Protease

@ast

Molecular Basis for Drug Resistance in HIV-1 Protease

@en

prefLabel

Molecular Basis for Drug Resistance in HIV-1 Protease

@ast

Molecular Basis for Drug Resistance in HIV-1 Protease

@en

P1433

Q35260370-919B7206-662A-42A6-9B2A-FD08364720F2

P1476

Q35260370-25FC5DF2-540B-4F9D-A48D-A377F63E6AF4

P2093

Q35260370-07A33D1E-D806-4B5B-9547-05BCC5725068

Q35260370-0BCB6623-E54C-41C7-989E-9FA05B0E2143

Q35260370-2E3E5908-8DE7-41D7-9F39-23ED19ECF662

Q35260370-33A34BC6-7449-4AB4-AB02-7BEE3038783B

Q35260370-3E260E24-2CB8-4BD9-AB60-C5F83C4CA166

Q35260370-4F81D953-E0B5-4ADB-94A4-60C0FAEE88FC

Q35260370-58E39121-812A-4829-8973-6A9E4D3512C6

Q35260370-6BAF9B5F-0D7E-4BB3-AC33-6354FB5FF7C4

Q35260370-A2C724C4-B025-4FFA-A487-05C4AD954566

Q35260370-AB10F032-8069-4FC4-A616-8DB548E405B1

P2860

Q35260370-0517C8DA-06C2-4253-94A8-F9D4ACDD7D3E

Q35260370-09C5A6E1-9E59-4389-BC27-FC83D0DA3793

Q35260370-0DDC8455-312C-4A3F-BB49-809E14CF5911

Q35260370-0F1B2BAA-BC6A-4E60-94A9-52F5AC2C71B1

Q35260370-110710A7-C68A-4656-ACB9-530BFB42CAE3

Q35260370-136B92C7-8012-4AE5-BFEC-170122C76A97

Q35260370-13D9816D-F93F-4D52-8688-BBD672B66D60

Q35260370-1452FA7C-BF49-4432-A2B7-ACB73B85BBE1

Q35260370-1777C0DD-455C-4251-B6EF-6C92E462B59B

Q35260370-1C0EB710-481A-42B7-A2BF-A3A2AF6C755E

P304

Q35260370-0ECF6B0F-765F-45F2-B57E-70A36311BC8F

P31

Q35260370-931CFA19-20E0-4D1D-931E-643B68275F9E

P356

Q35260370-1C0DD7B3-A5BB-40E9-8178-C74D74ABE120

P433

Q35260370-EBF70058-0059-41A2-85F5-5D51654D1EF0

P478

Q35260370-A08AE429-1BF1-40A1-9A8E-0AEF0F142F6E

P577

Q35260370-A1B0855C-39E1-458A-A24C-552737E90DED

P5875

Q35260370-17226C6A-775D-40C5-99C9-E610CF548C67

P698

Q35260370-ADBB553E-A3F5-4DD7-972A-0E74F5C1D13E

P932

Q35260370-10F385A7-C124-47B8-B5E9-0CE43F9EA0CB

P356

P1433

P1476

Molecular Basis for Drug Resistance in HIV-1 Protease

@en

P2093

Akbar Ali

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

Ayşegül Ozen

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

Celia A Schiffer

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

Ellen A Nalivaika

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

Jennifer F Murzycki

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

Kelly Thayer

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

Madhavi Kolli

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

Madhavi N L Nalam

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

Moses M Prabu-Jeyabalan

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

Nancy M King

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

P2860

Active human immunodeficiency virus protease is required for viral infectivity

Structural and kinetic analysis of drug resistant mutants of HIV-1 protease

An alternate binding site for the P1-P3 group of a class of potent HIV-1 protease inhibitors as a result of concerted structural change in the 80s loop of the protease

Structural implications of drug-resistant mutants of HIV-1 protease: high-resolution crystal structures of the mutant protease/substrate analogue complexes

Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes

Combining mutations in HIV-1 protease to understand mechanisms of resistance

Viability of a drug-resistant human immunodeficiency virus type 1 protease variant: structural insights for better antiviral therapy

Discovery of HIV-1 protease inhibitors with picomolar affinities incorporating N-aryl-oxazolidinone-5-carboxamides as novel P2 ligands

Design of mutation-resistant HIV protease inhibitors with the substrate envelope hypothesis

Computational design and experimental study of tighter binding peptides to an inactivated mutant of HIV-1 protease

P304

2509-2535

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

P31

scholarly article

P356

10.3390/V2112509

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

P433

11

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

P478

2

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

P577

2010-11-12T00:00:00Z

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

P5875

51711959

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

P698

21994628

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

P932

3185577

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