Glutamine 89 is a key residue in the allosteric modulation of human serine racemase activity by ATP

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2045-2322

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Glutamine 89 is a key residue in the allosteric modulation of human serine racemase activity by ATP ; volume:8 ; number:1 ; day:13 ; month:6 ; year:2018 ; pages:1-13 ; date:12.2018
Scientific reports ; 8, Heft 1 (13.6.2018), 1-13, 12.2018

Classification: Naturwissenschaften

Creator: Canosa, Andrea V.

Contributor: Faggiano, Serena
Marchetti, Marialaura
Armao, Stefano
Bettati, Stefano
Bruno, Stefano
Percudani, Riccardo
Campanini, Barbara
Mozzarelli, Andrea
SpringerLink (Online service)

DOI: 10.1038/s41598-018-27227-1

URN: urn:nbn:de:101:1-2018081215563254976603

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 15.08.2025, 7:27 AM CEST

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Associated

Canosa, Andrea V.
Faggiano, Serena
Marchetti, Marialaura
Armao, Stefano
Bettati, Stefano
Bruno, Stefano
Percudani, Riccardo
Campanini, Barbara
Mozzarelli, Andrea
SpringerLink (Online service)

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Allosteric effect of ATP on Na+,K+-ATPase conformational kinetics

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Loss of DJ-1 impairs antioxidant response by altered glutamine and serine metabolism

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Glutamine 89 is a key residue in the allosteric modulation of human serine racemase activity by ATP

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Other Objects (12)

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Allosteric inhibition of PPM1D serine/threonine phosphatase via an altered conformational state

Allosteric effect of ATP on Na+,K+-ATPase conformational kinetics

Loss of DJ-1 impairs antioxidant response by altered glutamine and serine metabolism

Allosteric activation unveils protein-mass modulation of ATP phosphoribosyltransferase product release

Allosteric probe initiated triple signal recycles for sensitive analysis of adenosine triphosphate (ATP)

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Analysis of Allosteric Communication Pathways in Class I Glutamine Amidotransferases

Allosteric inhibition of PPM1D serine/threonine phosphatase via an altered conformational state

Allosteric effect of ATP on Na+,K+-ATPase conformational kinetics

Loss of DJ-1 impairs antioxidant response by altered glutamine and serine metabolism

Allosteric activation unveils protein-mass modulation of ATP phosphoribosyltransferase product release

Allosteric probe initiated triple signal recycles for sensitive analysis of adenosine triphosphate (ATP)

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Allosteric probe initiated triple signal recycles for sensitive analysis of adenosine triphosphate (ATP)

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