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Molecular Endocrinology (Baltimore, Md.)
|
May 10, 2012
Research resource: identification of novel growth hormone-regulated phosphorylation sites by quantitative phosphoproteomics
Bridgette N Ray, Hye Kyong Kweon, Lawrence S Argetsinger, et al.
Molecular Endocrinology (Baltimore, Md.)
|
March 2, 2013
Identification of steroid-sensitive gene-1/Ccdc80 as a JAK2-binding protein
Erin E O'Leary, Anna M Mazurkiewicz-Muñoz, Lawrence S Argetsinger, et al.
Molecular and Cellular Biology
|
May 4, 2004
Tyrosine 813 is a site of JAK2 autophosphorylation critical for activation of JAK2 by SH2-B beta
Jason H Kurzer, Lawrence S Argetsinger, Yong-Jie Zhou, et al.
Molecular and Cellular Biology
|
April 15, 2009
Regulation of Jak2 function by phosphorylation of Tyr317 and Tyr637 during cytokine signaling
Scott A Robertson, Rositsa I Koleva, Lawrence S Argetsinger, et al.
Molecular and Cellular Biology
|
May 18, 2006
Phosphorylation of JAK2 at serine 523: a negative regulator of JAK2 that is stimulated by growth hormone and epidermal growth factor
Anna M Mazurkiewicz-Munoz, Lawrence S Argetsinger, Jean-Louis K Kouadio, et al.
Endocrinology
|
February 17, 2023
Role of the Beta and Gamma Isoforms of the Adapter Protein SH2B1 in Regulating Energy Balance
Lawrence S Argetsinger, Anabel Flores, Nadezhda Svezhova, et al.
Molecular Endocrinology (Baltimore, Md.)
|
March 23, 2010
Tyrosines 868, 966, and 972 in the kinase domain of JAK2 are autophosphorylated and required for maximal JAK2 kinase activity
Lawrence S Argetsinger, Jeanne A Stuckey, Scott A Robertson, et al.
Analytical Chemistry
|
April 15, 2005
Capillary electrophoresis and fluorescence anisotropy for quantitative analysis of peptide-protein interactions using JAK2 and SH2-Bbeta as a model system
Peilin Yang, Rebecca J Whelan, Emily E Jameson, et al.
Molecular and Cellular Biology
|
December 13, 2017
Phosphorylation of the Unique C-Terminal Tail of the Alpha Isoform of the Scaffold Protein SH2B1 Controls the Ability of SH2B1α To Enhance Nerve Growth Factor Function
Ray M Joe, Anabel Flores, Michael E Doche, et al.
Diabetes
|
November 20, 2008
Enhanced expression of Janus kinase-signal transducer and activator of transcription pathway members in human diabetic nephropathy
Celine C Berthier, Hongyu Zhang, MaryLee Schin, et al.
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of 3
Search research articles
Search
Showing results (11-20 of 25) with videos related to
Sort By:
Page
of 3
Molecular Endocrinology (Baltimore, Md.)
|
May 10, 2012
Research resource: identification of novel growth hormone-regulated phosphorylation sites by quantitative phosphoproteomics
Bridgette N Ray, Hye Kyong Kweon, Lawrence S Argetsinger, et al.
Molecular Endocrinology (Baltimore, Md.)
|
March 2, 2013
Identification of steroid-sensitive gene-1/Ccdc80 as a JAK2-binding protein
Erin E O'Leary, Anna M Mazurkiewicz-Muñoz, Lawrence S Argetsinger, et al.
Molecular and Cellular Biology
|
May 4, 2004
Tyrosine 813 is a site of JAK2 autophosphorylation critical for activation of JAK2 by SH2-B beta
Jason H Kurzer, Lawrence S Argetsinger, Yong-Jie Zhou, et al.
Molecular and Cellular Biology
|
April 15, 2009
Regulation of Jak2 function by phosphorylation of Tyr317 and Tyr637 during cytokine signaling
Scott A Robertson, Rositsa I Koleva, Lawrence S Argetsinger, et al.
Molecular and Cellular Biology
|
May 18, 2006
Phosphorylation of JAK2 at serine 523: a negative regulator of JAK2 that is stimulated by growth hormone and epidermal growth factor
Anna M Mazurkiewicz-Munoz, Lawrence S Argetsinger, Jean-Louis K Kouadio, et al.
Endocrinology
|
February 17, 2023
Role of the Beta and Gamma Isoforms of the Adapter Protein SH2B1 in Regulating Energy Balance
Lawrence S Argetsinger, Anabel Flores, Nadezhda Svezhova, et al.
Molecular Endocrinology (Baltimore, Md.)
|
March 23, 2010
Tyrosines 868, 966, and 972 in the kinase domain of JAK2 are autophosphorylated and required for maximal JAK2 kinase activity
Lawrence S Argetsinger, Jeanne A Stuckey, Scott A Robertson, et al.
Analytical Chemistry
|
April 15, 2005
Capillary electrophoresis and fluorescence anisotropy for quantitative analysis of peptide-protein interactions using JAK2 and SH2-Bbeta as a model system
Peilin Yang, Rebecca J Whelan, Emily E Jameson, et al.
Molecular and Cellular Biology
|
December 13, 2017
Phosphorylation of the Unique C-Terminal Tail of the Alpha Isoform of the Scaffold Protein SH2B1 Controls the Ability of SH2B1α To Enhance Nerve Growth Factor Function
Ray M Joe, Anabel Flores, Michael E Doche, et al.
Diabetes
|
November 20, 2008
Enhanced expression of Janus kinase-signal transducer and activator of transcription pathway members in human diabetic nephropathy
Celine C Berthier, Hongyu Zhang, MaryLee Schin, et al.
Page
of 3