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The Journal of Biological Chemistry
|
March 4, 2009
A type III protein arginine methyltransferase from the protozoan parasite Trypanosoma brucei
John C Fisk, Joyce Sayegh, Cecilia Zurita-Lopez, et al.
Archives of Biochemistry and Biophysics
|
February 11, 2015
The invertebrate Caenorhabditis elegans biosynthesizes ascorbate
Alexander N Patananan, Lauren M Budenholzer, Maria E Pedraza, et al.
Autoimmunity
|
November 23, 2023
Natural isoaspartyl protein modification of ZAP70 alters T cell responses in lupus
Mei-Ling Yang, TuKiet T Lam, Jean Kanyo, et al.
The Journal of Biological Chemistry
|
April 5, 2011
The ribosomal l1 protuberance in yeast is methylated on a lysine residue catalyzed by a seven-beta-strand methyltransferase
Kristofor J Webb, Qais Al-Hadid, Cecilia I Zurita-Lopez, et al.
Biochemistry
|
June 2, 2012
Identification of methylated proteins in the yeast small ribosomal subunit: a role for SPOUT methyltransferases in protein arginine methylation
Brian D Young, David I Weiss, Cecilia I Zurita-Lopez, et al.
The Journal of Biological Chemistry
|
September 19, 2014
Translational roles of elongation factor 2 protein lysine methylation
Maria C Dzialo, Kyle J Travaglini, Sean Shen, et al.
The Journal of Biological Chemistry
|
April 28, 2007
Arabidopsis VTC2 encodes a GDP-L-galactose phosphorylase, the last unknown enzyme in the Smirnoff-Wheeler pathway to ascorbic acid in plants
Carole L Linster, Tara A Gomez, Kathryn C Christensen, et al.
Biochemistry
|
November 19, 2019
Protein Methylation and Translation: Role of Lysine Modification on the Function of Yeast Elongation Factor 1A
Jonelle T White, Tieranee Cato, Neil Deramchi, et al.
Biochemistry
|
April 29, 2022
Human Protein-l-isoaspartate <i>O</i>-Methyltransferase Domain-Containing Protein 1 (PCMTD1) Associates with Cullin-RING Ligase Proteins
Rebeccah A Warmack, Eric Z Pang, Esther Peluso, et al.
Journal of Structural Biology
|
July 19, 2020
Human ARMT1 structure and substrate specificity indicates that it is a DUF89 family damage-control phosphatase
Taylor N Dennis, Nikola Kenjić, Amrik S Kang, et al.
Page
of 10
Search research articles
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Showing results (61-70 of 97) with videos related to
Sort By:
Page
of 10
The Journal of Biological Chemistry
|
March 4, 2009
A type III protein arginine methyltransferase from the protozoan parasite Trypanosoma brucei
John C Fisk, Joyce Sayegh, Cecilia Zurita-Lopez, et al.
Archives of Biochemistry and Biophysics
|
February 11, 2015
The invertebrate Caenorhabditis elegans biosynthesizes ascorbate
Alexander N Patananan, Lauren M Budenholzer, Maria E Pedraza, et al.
Autoimmunity
|
November 23, 2023
Natural isoaspartyl protein modification of ZAP70 alters T cell responses in lupus
Mei-Ling Yang, TuKiet T Lam, Jean Kanyo, et al.
The Journal of Biological Chemistry
|
April 5, 2011
The ribosomal l1 protuberance in yeast is methylated on a lysine residue catalyzed by a seven-beta-strand methyltransferase
Kristofor J Webb, Qais Al-Hadid, Cecilia I Zurita-Lopez, et al.
Biochemistry
|
June 2, 2012
Identification of methylated proteins in the yeast small ribosomal subunit: a role for SPOUT methyltransferases in protein arginine methylation
Brian D Young, David I Weiss, Cecilia I Zurita-Lopez, et al.
The Journal of Biological Chemistry
|
September 19, 2014
Translational roles of elongation factor 2 protein lysine methylation
Maria C Dzialo, Kyle J Travaglini, Sean Shen, et al.
The Journal of Biological Chemistry
|
April 28, 2007
Arabidopsis VTC2 encodes a GDP-L-galactose phosphorylase, the last unknown enzyme in the Smirnoff-Wheeler pathway to ascorbic acid in plants
Carole L Linster, Tara A Gomez, Kathryn C Christensen, et al.
Biochemistry
|
November 19, 2019
Protein Methylation and Translation: Role of Lysine Modification on the Function of Yeast Elongation Factor 1A
Jonelle T White, Tieranee Cato, Neil Deramchi, et al.
Biochemistry
|
April 29, 2022
Human Protein-l-isoaspartate <i>O</i>-Methyltransferase Domain-Containing Protein 1 (PCMTD1) Associates with Cullin-RING Ligase Proteins
Rebeccah A Warmack, Eric Z Pang, Esther Peluso, et al.
Journal of Structural Biology
|
July 19, 2020
Human ARMT1 structure and substrate specificity indicates that it is a DUF89 family damage-control phosphatase
Taylor N Dennis, Nikola Kenjić, Amrik S Kang, et al.
Page
of 10