Tautomerism and magnesium chelation of HIV-1 integrase inhibitors: a theoretical study.

about

Software and resources for computational medicinal chemistry Computer tools in the discovery of HIV-1 integrase inhibitors Authentic HIV-1 integrase inhibitors.Quantum mechanics implementation in drug-design workflows: does it really help?

P2860

Q28728561-2E67E9D0-C312-483C-9E68-4C6B76567149 Q36145611-01F67738-326D-4A2A-B063-E133810B14B5 Q36145625-DD5C65A4-347B-4E54-820D-490C25B8CBDF Q41633463-6BDFDC35-C905-4990-A13A-76A4973BFDD5

P2860

Tautomerism and magnesium chelation of HIV-1 integrase inhibitors: a theoretical study.

Item

http://www.wikidata.org/entity/Q36249020

description

2010 nî lūn-bûn

@nan

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

2010年论文

@zh

2010年论文

@zh-cn

name

Tautomerism and magnesium chelation of HIV-1 integrase inhibitors: a theoretical study.

@ast

Tautomerism and magnesium chelation of HIV-1 integrase inhibitors: a theoretical study.

@en

type

Item

label

Tautomerism and magnesium chelation of HIV-1 integrase inhibitors: a theoretical study.

@ast

Tautomerism and magnesium chelation of HIV-1 integrase inhibitors: a theoretical study.

@en

prefLabel

Tautomerism and magnesium chelation of HIV-1 integrase inhibitors: a theoretical study.

@ast

Tautomerism and magnesium chelation of HIV-1 integrase inhibitors: a theoretical study.

@en

P1476

Tautomerism and magnesium chelation of HIV-1 integrase inhibitors: a theoretical study

@en

P2093

Chenzhong Liao

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

P2860

Retroviral intasome assembly and inhibition of DNA strand transfer

The 1.8-A crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognition

Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor: high level of similarity of the active site with other viral integrases

Inhibitors of strand transfer that prevent integration and inhibit HIV-1 replication in cells

The Cambridge Structural Database: a quarter of a million crystal structures and rising

Targeting Tn5 transposase identifies human immunodeficiency virus type 1 inhibitors.

HIV-1 integrase: structural organization, conformational changes, and catalysis.

Diketo acid inhibitor mechanism and HIV-1 integrase: implications for metal binding in the active site of phosphotransferase enzymes.

Integrase inhibitors to treat HIV/AIDS.

Tautomerism in computer-aided drug design.

P304

1053-1066

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

P31

scholarly article

P356

10.1002/CMDC.201000039

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

P433

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

P478

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

P50

Marc C Nicklaus

P577

2010-07-01T00:00:00Z

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

P5875

44659136

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

P698

20533499

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

P932

3447627

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

Tautomerism and magnesium chelation of HIV-1 integrase inhibitors: a theoretical study.

about

P2860

P2860

Tautomerism and magnesium chelation of HIV-1 integrase inhibitors: a theoretical study.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P932