Robyn Reed

age ~27

from Knightdale, NC

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Connected to:

Robyn Reed Phones & Addresses

License #:

5145373 - Expired

Category:

Health Care

Issued Date:

Dec 13, 1999

Effective Date:

Sep 6, 2007

Expiration Date:

Jul 31, 2005

Type:

Licensed Practical Nurse

Characterization Of Grp94-Ligand Interactions And Purification, Screening, And Therapeutic Methods Relating Thereto
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US Patent:

8404805, Mar 26, 2013
Filed:

Oct 5, 2009
Appl. No.:

12/573618
Inventors:

Christopher V. Nicchitta - Durham NC, US
James J. Wassenberg - Durham NC, US
Robyn C. Reed - Durham NC, US
Assignee:

Duke University - Durham NC
International Classification:

C07K 14/435
US Classification:

530350, 5142631
Abstract:

The presently disclosed subject matter discloses characterization of interactions between ligands and Hsp90 proteins, including GRP94, wherein ligand binding to the N-terminal nucleotide binding domain of GRP94 elicits a conformational change that converts the GRP94 from an inactive to an active conformation, and wherein the chaperone and peptide-binding activities of the GRP94 are markedly stimulated. Also disclosed are purification, screening, and therapeutic methods pertaining to the biological activity of GRP94, and in some instances HSP90, based upon the characterization of ligand interactions of Hsp90 peptide-binding proteins, including GRP94.

Characterization Of Grp94-Ligand Interactions And Purification, Screening, And Therapeutic Methods Relating Thereto
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US Patent:

20030054996, Mar 20, 2003
Filed:

Aug 1, 2002
Appl. No.:

10/210333
Inventors:

Christopher Nicchitta - Durham NC, US
James Wassenberg - Durham NC, US
Meredith Rosser - Durham NC, US
Robyn Reed - Durham NC, US
International Classification:

A61K038/17
C12N009/22
US Classification:

514/012000, 435/199000
Abstract:

The present invention discloses characterization of interactions between ligands and Hsp90 proteins, including GRP94, wherein ligand binding to the N-terminal nucleotide binding domain of GRP94 elicits a conformational change that converts the GRP94 from an inactive to an active conformation, and wherein the chaperone and peptide-binding activities of the GRP94 are markedly stimulated. Also disclosed are purification, screening, and therapeutic methods pertaining to the biological activity of GRP94, and in some instances HSP90, based upon the characterization of ligand interactions of Hsp90 peptide-binding proteins, including GRP94.