High-resolution crystal structure of human asparagine synthetase enables analysis of inhibitor binding and selectivity.
Computational models
Enzymes
Medicinal chemistry
X-ray crystallography
Journal
Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179
Informations de publication
Date de publication:
2019
2019
Historique:
received:
06
09
2018
accepted:
21
08
2019
entrez:
26
9
2019
pubmed:
26
9
2019
medline:
26
9
2019
Statut:
epublish
Résumé
Expression of human asparagine synthetase (ASNS) promotes metastatic progression and tumor cell invasiveness in colorectal and breast cancer, presumably by altering cellular levels of L-asparagine. Human ASNS is therefore emerging as a
Identifiants
pubmed: 31552298
doi: 10.1038/s42003-019-0587-z
pii: 587
pmc: PMC6748925
doi:
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Pagination
345Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM111695
Pays : United States
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/I003703/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/P018017/1
Pays : United Kingdom
Commentaires et corrections
Type : ErratumIn
Déclaration de conflit d'intérêts
Competing interestsThe authors declare no competing interests.
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