Ligand Selectivity between the ADP-Ribosylating Toxins: An Inverse-Docking Study for Multitarget Drug Discovery.

about

Ligand Selectivity between the ADP-Ribosylating Toxins: An Inverse-Docking Study for Multitarget Drug Discovery.

Item

http://www.wikidata.org/entity/Q55691227

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

Ligand Selectivity between the ...... or Multitarget Drug Discovery.

@en

Ligand Selectivity between the ...... or Multitarget Drug Discovery.

@nl

type

Item

label

Ligand Selectivity between the ...... or Multitarget Drug Discovery.

@en

Ligand Selectivity between the ...... or Multitarget Drug Discovery.

@nl

prefLabel

Ligand Selectivity between the ...... or Multitarget Drug Discovery.

@en

Ligand Selectivity between the ...... or Multitarget Drug Discovery.

@nl

P1476

Ligand Selectivity between the ...... for Multitarget Drug Discovery

@en

P2093

Leif A Eriksson

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

Martin Eriksson

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

P2860

Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen

Structure-function analysis of water-soluble inhibitors of the catalytic domain of exotoxin A from Pseudomonas aeruginosa

DOCK 6: combining techniques to model RNA-small molecule complexes

The Father, Son and Cholix Toxin: The Third Member of the DT Group Mono-ADP-Ribosyltransferase Toxin Family

Shifting from the single to the multitarget paradigm in drug discovery

Cholix toxin, a novel ADP-ribosylating factor from Vibrio cholerae

Yeast as a tool for characterizing mono-ADP-ribosyltransferase toxins

Newly Discovered and Characterized Antivirulence Compounds Inhibit Bacterial Mono-ADP-Ribosyltransferase Toxins

The 1.8 A Cholix Toxin Crystal Structure in Complex with NAD+ and Evidence for a New Kinetic Model

The crystal structure of Pseudomonas aeruginosa exotoxin domain III with nicotinamide and AMP: conformational differences with the intact exotoxin

P304

1710-1719

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

P31

scholarly article

P356

10.1021/ACSOMEGA.7B00010

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

P433

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

P478

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

P50

Patricia Saenz-Méndez

P577

2017-04-28T00:00:00Z

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

P698

30023642

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

P932

6044789

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