Brian C Capell, 47736 Bainbridge St, Philadelphia, PA 19147

8257915, Sep 4, 2012

Oct 15, 2010

12/905838

Leslie B. Gordon - Foxboro MA, US
Francis S. Collins - Rockville MD, US
Thomas Glover - Ypsilanti MI, US
Michael W. Glynn - Darien CT, US
Brian C. Capell - Rumson NJ, US
Adrienne D. Cox - Chapel Hill NC, US
Channing J. Der - Chapel Hill NC, US

Progeria Research Foundation, Inc. - Peabody MA
The United States of America as represented by the Secretary of the Department of Health and Human Services - Washington DC
The University of North Carolina at Chapel Hill - Chapel Hill NC
The Regents of the University of Michigan - Ann Arbor MI

C12Q 1/00
C12Q 1/02

435 4, 435 29

Although it can be farnesylated, the mutant lamin A protein expressed in Hutchinson Gilford Progeria Syndrome (HGPS) cannot be defarnesylated because the characteristic mutation causes deletion of a cleavage site necessary for binding the protease ZMPSTE24 and effecting defarnesylation. The result is an aberrant farnesylated protein (called “progerin”) that alters normal lamin A function as a dominant negative, as well as assuming its own aberrant function through its association with the nuclear membrane. The retention of farnesylation, and potentially other abnormal properties of progerin and other abnormal lamin gene protein products, produces disease. Farnesyltransferase inhibitors (FTIs) (both direct effectors and indirect inhibitors) will inhibit the formation of progerin, cause a decrease in lamin A protein, and/or an increase prelamin A protein. Decreasing the amount of aberrant protein improves cellular effects caused by and progerin expression. Similarly, treatment with FTIs should improve disease status in progeria and other laminopathies.

2008013, Jun 5, 2008

Jul 25, 2007

11/828117

Leslie B. Gordon - Foxboro MA, US
Francis S. Collins - Rockville MD, US
Thomas Glover - Ypsilanti MI, US
Michael W. Glynn - Darien CT, US
Brian C. Capell - Rumson NJ, US
Adrienne D. Cox - Chapel Hill NC, US
Channing J. Der - Chapel Hill NC, US

A61K 49/00
A61K 31/4709
A61P 43/00
A61K 31/4545

424 92, 514312, 514316

Although it can be farnesylated, the mutant lamin A protein expressed in Hutchison Gilford Progeria Syndrome (HGPS) cannot be defarnesylated because the characteristic mutation causes deletion of a cleavage site necessary for binding the protease ZMPSTE24 and effecting defarnesylation. The result is an aberrant farnesylated protein (called “progerin”) that alters normal lamin A function as a dominant negative, as well as assuming its own aberrant function through its association with the nuclear membrane. The retention of farnesylation, and potentially other abnormal properties of progerin and other abnormal lamin gene protein products, produces disease. Farnesyltransferase inhibitors (FTIs) (both direct effectors and indirect inhibitors) will inhibit the formation of progerin, cause a decrease in lamin A protein, and/or an increase prelamin A protein. Decreasing the amount of aberrant protein improves cellular effects caused by and progerin expression. Similarly, treatment with FTIs should improve disease status in progeria and other laminopathies. In addition, elements of atherosclerosis and aging in non-laminopathy individuals will improve after treatment with farnesyltransferase inhibitors.

2012032, Dec 27, 2012

Aug 6, 2012

13/567432

Leslie B. Gordon - Foxboro MA, US
Francis S. Collins - Rockville MD, US
Thomas Glover - Ypsilanti MI, US
Michael W. Glynn - Darien CT, US
Brian C. Capell - Rumson NJ, US
Adrienne D. Cox - Chapel Hill NC, US
Channing J. Der - Chapel Hill NC, US

C12Q 1/68

435 613

Although it can be farnesylated, mutant lamin A expressed in Hutchinson Gilford Progeria Syndrome cannot be defarnesylated; the characteristic mutation causes deletion of a cleavage site necessary for binding the protease ZMPSTE24 and effecting defarnesylation. The result is an aberrant farnesylated protein (“progerin”) that alters normal lamin A function as a dominant negative, and assumes its own aberrant function through its association with the nuclear membrane. Retention of farnesylation, and potentially other abnormal properties of progerin and other abnormal lamin gene protein products, produces disease. Farnesyltransferase inhibitors (FTIs) will inhibit formation of progerin, cause a decrease in lamin A protein, and/or an increase prelamin A protein. Decreasing the amount of aberrant protein improves cellular effects caused by and progerin expression. Similarly, treatment with FTIs should improve disease status in progeria and other laminopathies. In addition, elements of atherosclerosis and aging in non-laminopathy individuals will improve after treatment with FTIs.

2013020, Aug 8, 2013

Apr 4, 2013

13/857052

The Government of the United States of America as represented by the Secretary of the Department - Rockville MD, US
The Regents of the University of Michigan - Ann Arbor MI, US
The University of North Carolina at Chapel Hill - Chapel Hill NC, US
Brian C. Capell - Philadelphia PA, US
Adrienne D. Cox - Chapel Hill NC, US
Channing J. Der - Chapel Hill NC, US

The Government of the United States of America as represented by the Secretary of the Department of - Rockville MD
The University of North Carolina at Chapel Hill - Chapel Hill NC
The Regents of the University of Michigan - Ann Arbor MI
Progeria Research Foundation, Inc. - Peabody MA

A61K 31/4545
A61K 31/4709
A61K 45/06

514290, 514303, 514312

Although it can be farnesylated, the mutant lamin A protein expressed in Hutchinson Gilford Progeria Syndrome (HGPS) cannot be defarnesylated because the characteristic mutation causes deletion of a cleavage site necessary for binding the protease ZMPSTE24 and effecting defarnesylation. The result is an aberrant farnesylated protein (called “progerin”) that alters normal lamin A function as a dominant negative, as well as assuming its own aberrant function through its association with the nuclear membrane. The retention of farnesylation, and potentially other abnormal properties of progerin and other abnormal lamin gene protein products, produces disease. Farnesyltransferase inhibitors (FTIs) (both direct effectors and indirect inhibitors) will inhibit the formation of progerin, cause a decrease in lamin A protein, and/or an increase prelamin A protein. Decreasing the amount of aberrant protein improves cellular effects caused by and progerin expression. Similarly, treatment with FTIs should improve disease status in progeria and other laminopathies. In addition, elements of atherosclerosis and aging in non-laminopathy individuals will improve after treatment with farnesyltransferase inhibitors.

2015001, Jan 15, 2015

Jul 21, 2014

14/336457

- Rockville MD, US
- Peabody MA, US
- Ann Arbor MI, US
- Chapel Hill NC, US
Brian C. CAPELL - Philadelphia PA, US
Adrienne D. COX - Chapel Hill NC, US
Channing J. DER - Chapel Hill NC, US

A61K 31/4545
A61K 31/4709

514290, 514303, 514312

Although it can be farnesylated, the mutant lamin A protein expressed in Hutchinson Gilford Progeria Syndrome (HGPS) cannot be defarnesylated because the characteristic mutation causes deletion of a cleavage site necessary for binding the protease ZMPSTE24 and effecting defarnesylation. The result is an aberrant farnesylated protein (called “progerin”) that alters normal lamin A function as a dominant negative, as well as assuming its own aberrant function through its association with the nuclear membrane. The retention of farnesylation, and potentially other abnormal properties of progerin and other abnormal lamin gene protein products, produces disease. Farnesyltransferase inhibitors (FTIs) (both direct effectors and indirect inhibitors) will inhibit the formation of progerin, cause a decrease in lamin A protein, and/or an increase prelamin A protein. Decreasing the amount of aberrant protein improves cellular effects caused by and progerin expression. Similarly, treatment with FTIs should improve disease status in progeria and other laminopathies. In addition, elements of atherosclerosis and aging in non-laminopathy individuals will improve after treatment with farnesyltransferase inhibitors.