Structural insights into betaine aldehyde dehydrogenase (BADH2) from Oryza sativa explored by modeling and simulations

about

Structural insights into betaine aldehyde dehydrogenase (BADH2) from Oryza sativa explored by modeling and simulations

Item

http://www.wikidata.org/entity/Q58701376

description

article publié dans la revue scientifique Scientific Reports

@fr

im August 2018 veröffentlichter wissenschaftlicher Artikel

@de

scientific article published in Scientific Reports

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована в серпні 2018

@uk

name

Structural insights into betai ...... ed by modeling and simulations

@en

Structural insights into betaine aldehyde dehydrogenase

@nl

type

Item

label

Structural insights into betai ...... ed by modeling and simulations

@en

Structural insights into betaine aldehyde dehydrogenase

@nl

prefLabel

Structural insights into betai ...... ed by modeling and simulations

@en

Structural insights into betaine aldehyde dehydrogenase

@nl

P1476

Structural insights into betai ...... ed by modeling and simulations

@en

P2093

Apisara Baicharoen

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

P2860

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Structure of betaine aldehyde dehydrogenase at 2.1 A resolution

Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes

The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold

VMD: visual molecular dynamics

Structure validation by Calpha geometry: phi,psi and Cbeta deviation

Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation

Human aldehyde dehydrogenase catalytic activity and structural interactions with coenzyme analogs

Comparative protein structure modeling using Modeller

Role of backbone solvation and electrostatics in generating preferred peptide backbone conformations: distributions of phi.

P304

12892

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

P31

scholarly article

P356

10.1038/S41598-018-31204-Z

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

P407

English

P433

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

P478

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

P50

Ranjit Vijayan

Prapasiri Pongprayoon

P577

2018-08-27T00:00:00Z

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

P698

30150624

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

P932

6110774

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