Transduction of biologically active motifs of the small heat shock‐related protein, HSP20, leads to relaxation of vascular smooth muscle-Reference-Cited by-同舟云学术

Transduction of biologically active motifs of the small heat shock‐related protein, HSP20, leads to relaxation of vascular smooth muscle

Published:2003-05-08 Issue:10 Volume:17 Page:1358-1360
ISSN:0892-6638
Container-title:The FASEB Journal
language:en
Short-container-title:FASEB j.

Author:

Flynn Charles R.¹,Komalavilas Padmini¹²,Tessier Deron³,Thresher Jeffrey⁴,Niederkofler Eric E.⁵,Dreiza Catherine M.¹,Nelson Randall W.⁵,Panitch Alyssa¹,Joshi Lokesh⁶,Brophy Colleen M.¹²

Affiliation:

1. Department of BioengineeringArizona State University Tempe AZ 85287-9709

2. Carl T. Hayden Veterans Affairs Medical Center Phoenix AZ 85012

3. Mayo Clinic ScottsdaleDepartment of Surgery 13400 East Shea Boulevard Scottsdale AZ 85259

4. Department of KinesiologyArizona State University Tempe AZ 85287-0404

5. Intrinsic Bioprobes Inc. 625 S. Smith Road, Suite 22 Tempe AZ 85281

6. Department of Plant BiologyArizona State University Tempe AZ 85287-1601

Funder

National Institutes of Health

Publisher

Wiley

Subject

Genetics,Molecular Biology,Biochemistry,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.02-1028fje

Reference27 articles.

1. Cyclic Nucleotide-dependent Vasorelaxation Is Associated with the Phosphorylation of a Small Heat Shock-related Protein

2. Purification and characterization of a 20-kDa protein that is highly homologous to alphaB-crystallin;Kato K.;J. Biol. Chem.,1994

3. Selected Contribution: HSP20 phosphorylation in nitroglycerin- and forskolin-induced sustained reductions in swine carotid media tone

4. Phosphorylation events associated with cyclic nucleotidedependent inhibition of smooth muscle contraction

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