Identification of single and double sites of phosphorylation by ECD FT-ICR/MS in peptides related to the phosphorylation site domain of the myristoylated alanine-rich c kinase protein-Reference-Cited by-同舟云学术

Identification of single and double sites of phosphorylation by ECD FT-ICR/MS in peptides related to the phosphorylation site domain of the myristoylated alanine-rich c kinase protein

Published:2007-12-01 Issue:12 Volume:18 Page:2137-2145
ISSN:1044-0305
Container-title:Journal of the American Society for Mass Spectrometry
language:en
Short-container-title:J. Am. Soc. Mass Spectrom.

Author:

Woodling Kellie A.¹,Eyler John R.¹,Tsybin Yury O.²,Nilsson Carol L.²,Marshall Alan G.³,Edison Arthur S.⁴,Al-Naggar Iman M.⁵,Bubb Michael R.⁵

Affiliation:

1. Department of Chemistry, University of Florida, 32611, Gainesville, FL, USA

2. National High Magnetic Field Laboratory, Tallahassee, Florida, USA

3. National High Magnetic Field Laboratory and Department of Chemistry and Biochemistry, Florida State University, Tallahassee, Florida, USA

4. Department of Biochemistry and Molecular Biology, McKnight Brain Institute, and National High Magnetic Field Laboratory, University of Florida, Gainesville, Florida, USA

5. Department of Medicine, University of Florida, Gainesville, Florida, USA

Publisher

American Chemical Society (ACS)

Subject

Spectroscopy,Structural Biology

Link

https://pubs.acs.org/doi/pdf/10.1016/j.jasms.2007.09.010

Reference54 articles.

1. MARCKS, a major protein kinase C substrate, assumes non-helical conformations both in solution and in complex with Ca2+-calmodulin

2. MARCKS deficiency in mice leads to abnormal brain development and perinatal death.

3. MARCKS, membranes, and calmodulin: kinetics of their interaction

4. The Role of 80K/MARCKS, a Specific Substrate of Protein Kinase C, in Cell Growth and Tumour Progression

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