منابع مشابه
Structural and functional roles of deamidation of N146 and/or truncation of NH2- or COOH-termini in human αB-crystallin
PURPOSE The purpose of the study was to determine the relative effects of deamidation and/or truncation on the structural and functional properties of αB-crystallin. METHODS Using wild-type (WT) αB-crystallin and the αB deamidated mutant (i.e., αB N146D), we generated NH(2)-terminal domain deleted (residues no. 1-66; αB-NT), deamidated plus NH(2)-terminal domain deleted (αB N146D-NT), COOH-te...
متن کاملMimicking phosphorylation of αB-crystallin affects its chaperone activity
Heath ECROYD*, Sarah MEEHAN*, Joseph HORWITZ†, J. Andrew AQUILINA‡, Justin L. P. BENESCH§, Carol V. ROBINSON§, Cait E. MACPHEE‖ and John A. CARVER*1 *School of Chemistry and Physics, University of Adelaide, Adelaide, SA 5005, Australia, †Jules Stein Institute, University of California, Los Angeles, School of Medicine, Los Angeles, CA 90095-7008, U.S.A., ‡School of Biological Sciences, Universit...
متن کاملPhosphorylation-induced Change of the Oligomerization State of αB-crystallin*
aB-crystallin in cells can be phosphorylated at three serine residues in response to stress or during mitosis (Ito, H., Okamoto, K., Nakayama, H., Isobe, T., and Kato, K. (1997) J. Biol. Chem. 272, 29934–29941 and Kato, K., Ito, H., Kamei, K., Inaguma, Y., Iwamoto, I., and Saga, S. (1998) J. Biol. Chem. 273, 28346–28354). In the present study, we determined effects of phosphorylation of aBcryst...
متن کاملCorrection: In Vivo Substrates of the Lens Molecular Chaperones αA-Crystallin and αB-Crystallin
αA-crystallin and αB-crystallin are members of the small heat shock protein family and function as molecular chaperones and major lens structural proteins. Although numerous studies have examined their chaperone-like activities in vitro, little is known about the proteins they protect in vivo. To elucidate the relationships between chaperone function, substrate binding, and human cataract forma...
متن کاملNew insight into the dynamical system of αB-crystallin oligomers
α-Crystallin possesses a dynamic quaternary structure mediated by its subunit dynamics. Elucidation of a mechanism of subunit dynamics in homo-oligomers of αB-crystallin was tackled through deuteration-assisted small-angle neutron scattering (DA-SANS) and electrospray ionization (ESI) native mass spectrometry (nMS). The existence of subunit exchange was confirmed with DA-SANS, and monomers libe...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1993
ISSN: 0014-5793
DOI: 10.1016/0014-5793(93)81113-e