The patent badge is an abbreviated version of the USPTO patent document. The patent badge does contain a link to the full patent document.
The patent badge is an abbreviated version of the USPTO patent document. The patent badge covers the following: Patent number, Date patent was issued, Date patent was filed, Title of the patent, Applicant, Inventor, Assignee, Attorney firm, Primary examiner, Assistant examiner, CPCs, and Abstract. The patent badge does contain a link to the full patent document (in Adobe Acrobat format, aka pdf). To download or print any patent click here.
Patent No.:
Date of Patent:
Nov. 21, 2006
Filed:
Sep. 05, 2003
Alma L. Burlingame, Sausalito, CA (US);
Katalin F. Medzihradszky, San Francisco, CA (US);
Zsuzsanna Darula, Boulder, CO (US);
Eran Perlson, Givat Shmuel, IL;
Michael Fainzilber, Rehovot, IL;
Robert J. Chalkley, San Francisco, CA (US);
Darren Tyson, Aliso Viejo, CA (US);
Ralph A. Bradshaw, Lake Forest, CA (US);
Alma L. Burlingame, Sausalito, CA (US);
Katalin F. Medzihradszky, San Francisco, CA (US);
Zsuzsanna Darula, Boulder, CO (US);
Eran Perlson, Givat Shmuel, IL;
Michael Fainzilber, Rehovot, IL;
Robert J. Chalkley, San Francisco, CA (US);
Darren Tyson, Aliso Viejo, CA (US);
Ralph A. Bradshaw, Lake Forest, CA (US);
Regents of the University of California, Oakland, CA (US);
Yeda Research and Development Co. Ltd. at the Weizmann Institute of Science, Oakland, CA (US);
Abstract
Post-translational O-sulfonation of a serine or threonine residue of proteins is detected, optionally comparatively, wherein the detected O-sulfonation is detected under a first physiological condition, and is compared with a control O-sulfonation detected under a second physiological condition, and a difference between the detected and control O-sulfonations indicates a difference between the first and second physiological conditions. Predetermined changes in physiological conditions are used to infer specific changes in O-sulfonation. Proteins are modified by introducing a predetermined change in O-sulfonation at a serine or threonine residue of the protein, and optionally, detecting a resultant change in O-sulfonation. These methods include introducing or increasing O-sulfonation, eliminating or reducing O-sulfonation; and derivatizing or substituting O-sulfonation.