- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
1550-2783
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
The Ergogenic Potential of Arginine ; volume:1 ; number:2 ; day:28 ; month:12 ; year:2004 ; pages:1-4 ; date:12.2004
Proceedings of the ... International Society of Sports Nutrition (ISSN) Conference and Expo ; 1, Heft 2 (28.12.2004), 1-4, 12.2004
- Creator
-
Campbell, Bill I.
La Bounty, Paul M.
Roberts, Mike
- Contributor
-
SpringerLink (Online service)
- DOI
-
10.1186/1550-2783-1-2-35
- URN
-
urn:nbn:de:101:1-2019010121230936198207
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 11:01 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Campbell, Bill I.
- La Bounty, Paul M.
- Roberts, Mike
- SpringerLink (Online service)
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The protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylation
The role of arginine and arginine-metabolizing enzymes during Giardia – host cell interactions in vitro
Author Correction: The protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylation
Arginine deprivation: a potential therapeutic for cancer cell metastasis? A review
The role of arginine methylation in alternative splicing
Screening of commonly prescribed drugs for effects on the CAT1-mediated transport of l-arginine and arginine derivatives
Hydrophobicity of arginine leads to reentrant liquid-liquid phase separation behaviors of arginine-rich proteins
Prediction of twin-arginine signal peptides
A potential late stage intermediate of twin-arginine dependent protein translocation in Escherichia coli
Arginine-dependent immune responses
Entamoeba histolytica: protein arginine transferase 1a methylates arginine residues and potentially modify the H4 histone
Intracellular arginine-dependent translation sensor reveals the dynamics of arginine starvation response and resistance in ASS1-negative cells
The protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylation
The role of arginine and arginine-metabolizing enzymes during Giardia – host cell interactions in vitro
Author Correction: The protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylation
Arginine deprivation: a potential therapeutic for cancer cell metastasis? A review
The role of arginine methylation in alternative splicing
Screening of commonly prescribed drugs for effects on the CAT1-mediated transport of l-arginine and arginine derivatives
Hydrophobicity of arginine leads to reentrant liquid-liquid phase separation behaviors of arginine-rich proteins
Prediction of twin-arginine signal peptides
A potential late stage intermediate of twin-arginine dependent protein translocation in Escherichia coli
Arginine-dependent immune responses
Entamoeba histolytica: protein arginine transferase 1a methylates arginine residues and potentially modify the H4 histone