Solomon H Snyder

Author:

Solomon H. Snyder

ISBN #:

0195015517

Author:

Solomon H. Snyder

ISBN #:

0195027159

Author:

Solomon H. Snyder

ISBN #:

0195028880

Author:

Solomon H. Snyder

ISBN #:

0070595208

Author:

Solomon H. Snyder

ISBN #:

0070595216

Author:

Solomon H. Snyder

ISBN #:

0070595232

Author:

Solomon H. Snyder

ISBN #:

0080179223

Author:

Solomon H. Snyder

ISBN #:

0262191326

US Patent:

6358975, Mar 19, 2002

Filed:

Feb 11, 2000

Appl. No.:

09/502046

Inventors:

Mikael J. Eliasson - Baltimore MD
Kenji Sampei - Baltimore MD
Allen S. Mandir - Baltimore MD
Patricia D. Hurn - Upperco MD
Richard J. Traystman - Ruxton MD
Jun Bao - Baltimore MD
Andrew Pieper - Baltimore MD
Ted M. Dawson - Baltimore MD
Solomon Snyder - Baltimore MD
Valina L. Dawson - Baltimore MD

Assignee:

Johns Hopkins University - Baltimore MD

International Classification:

A61K 3147

US Classification:

514309, 514617, 514619

Abstract:

Neutral tissue damage resulting for ischemia and reperfusion injury or neurodegenerative diseases can be prevented by administering therapeutically effective amounts of certain selective inhibitors of poly(ADP-ribose)polymerase. The inhibitors can be administered intravenously, intraperitoneally, intramuscularly, intraventricularly, or orally. They can be administered as a capsule or tablet containing single or divided dose. Alternatively, the inhibitors can be administered as a sterile solution, suspension or emulsion.

US Patent:

6362160, Mar 26, 2002

Filed:

Jun 30, 1993

Appl. No.:

08/082848

Inventors:

Ted M. Dawson - Baltimore MD
Joseph P. Steiner - Hampstead MD
Valina L. Dawson - Baltimore MD
George R. Uhl - Towson MD
Solomon H. Snyder - Baltimore MD

Assignee:

The Johns Hopkins University School of Medicine - Baltimore MD

International Classification:

A61K 3800

US Classification:

514 2, 514 8, 514 12, 514 31, 514 27

Abstract:

Immunophilin-binding agents inhibit the phosphatase calcineurin, leading to the increased phosphorylation of certain brain proteins, including nitric oxide synthase. The increased levels of phosphorylation of nitric oxide synthase inhibits the enzymatic production of nitric oxide. Thus the neurotoxic effects of glutamate, which are ordinarily the result of vascular strokes and other neurodegenerative diseases, are minimized, because the neurotoxic effects are at least partially mediated by nitric oxide. Thus immunophilin-binding drugs can be used therapeutically in the treatment of vascular stroke and neurodegenerative disorders such as Alzheimers disease and Huntingtons disease.

US Patent:

6444643, Sep 3, 2002

Filed:

May 28, 1999

Appl. No.:

09/321762

Inventors:

Joseph P. Steiner - Finksburg MD
Gregory S. Hamilton - Catonsville MD
Solomon H. Snyder - Baltimore MD

Assignee:

Guilford Pharmaceuticals Inc. - Baltimore MD
Johns Hopkins University School of Medicine - Baltimore MD

International Classification:

A61K 3803

US Classification:

514 11, 514 2, 514 12

Abstract:

This invention relates to the method of using neurotrophic cyclophilin inhibitor compounds having an affinity for cyclophilin-type immunophilins as inhibitors of the enzyme activity associated with immunophilin proteins, and particularly inhibitors of peptidyl-prolyl isomerase or rotamase enzyme activity.

US Patent:

6476200, Nov 5, 2002

Filed:

Jun 27, 1994

Appl. No.:

08/265967

Inventors:

David M. Sabatini - Baltimore MD
Mary Lui - Kew Gardens NY
Paul Tempst - New York NY
Solomon H. Snyder - Baltimore MD

Assignee:

The Johns Hopkins University - Baltimore MD

International Classification:

A23J 100

US Classification:

530413, 435 691

Abstract:

A protein complex containing 245 kDa and 35 kDa components, designated RAFT1 and RAFT2 (for Rapamycin And FKBP12 Target) interacts with FKBP12 in a rapamycin-dependent manner. This interaction has the pharmacological characteristics expected from the observed in vivo effects of rapamycin: it occurs at low nanomolar concentrations of rapamycin and is competed by excess FK506. Sequences (330 amino acids total) of tryptic peptides derived from the affinity purified 245 kDa RAFT1 reveals striking homologies to the predicted products of the yeast TOR genes, which were originally identified by mutations that confer rapamycin resistance in yeast. A RAFT1 cDNA was obtained and found to encode a 289 kDa protein (2550 amino acids) that is 43% and 39% identical to TOR2 and TOR1, respectively.

US Patent:

6492106, Dec 10, 2002

Filed:

Sep 14, 1994

Appl. No.:

08/305790

Inventors:

David M. Sabatini - Baltimore MD
Mary Lui - Kew Gardens NY
Paul Tempst - New York NY
Solomon H. Snyder - Baltimore MD

Assignee:

The Johns Hopkins University - Baltimore MD

International Classification:

C12Q 168

US Classification:

435 6, 536 231, 536 234, 536 235, 536 243

Abstract:

A protein complex containing 245 kDa and 35 kDa components, designated RAFT1 and RAFT2 (for apamycin nd KBP12 arget) interacts with FKBP12 in a rapamycin-dependent manner. This interaction has the pharmacological characteristics expected from the observed in vivo effects of rapamycin: it occurs at low nanomolar concentrations of rapamycin and is competed by excess FK506. Sequences (330 amino acids total) of tryptic peptides derived from the affinity purified 245 kDa RAFT1 reveals striking homologies to the predicted products of the yeast TOR genes, which were originally identified by mutations that confer rapamycin resistance in yeast. A RAFT1 cDNA was obtained and found to encode a 289 kDa protein (2550 amino acids) that is 43% and 39% identical to TOR2 and TOR1, respectively.

US Patent:

6500843, Dec 31, 2002

Filed:

Nov 5, 1999

Appl. No.:

09/435323

Inventors:

Joseph P. Steiner - Hampstead MD
Solomon Snyder - Baltimore MD
Gregory S. Hamilton - Catonsville MD
Ted Dawson - Baltimore MD

Assignee:

GPI NIL Holdings, Inc. - Wilmington DE
Johns Hopkins University School of Medicine - Baltimore MD

International Classification:

A31K 31445

US Classification:

514317

Abstract:

This invention relates to the method of using neurotrophic pipecolic acid derivative compounds having an affinity for FKBP-type immunophilins as inhibitors of the enzyme activity associated with immunophilin proteins, and particularly inhibitors of peptidyl-prolyl isomerase or rotamase enzyme activity to stimulate or promote neuronal growth or regeneration.

US Patent:

6774128, Aug 10, 2004

Filed:

Apr 19, 2001

Appl. No.:

09/840014

Inventors:

Crystal C. Watkins - Timonium MD
Solomon H. Snyder - Baltimore MD
Christopher D. Ferris - Franklin TN

Assignee:

Johns Hopkins University - Baltimore MD

International Classification:

A61K 31415

US Classification:

514258, 544262

Abstract:

Disclosed are methods for preventing or treating a gastrointestinal (GI) disorder in a mammal such as a human patient. In one embodiment, the methods include administering to the mammal a therapeutically effective amount of a compound that modulates a nitric oxide (NO) signaling pathway, particularly in GI neurons. Methods of the invention are particularly useful for the treatment (including prophylactic treatment) of diabetic gastropathies and other GI disorders.

US Patent:

6806057, Oct 19, 2004

Filed:

Oct 29, 2001

Appl. No.:

09/984345

Inventors:

Solomon H. Snyder - Baltimore MD
Samie R. Jaffrey - New York NY
Christopher D. Ferris - Franklin TN
Paul Tempst - New York NY

Assignee:

The Johns Hopkins University - Baltimore MD

International Classification:

G01N 3353

US Classification:

435 75, 514 91, 514562, 435 6, 435 71, 435 721, 435 26, 435188, 435 17, 435 12, 436107, 436116, 436173, 436518, 530402, 530408, 530409, 530412, 530413

Abstract:

Many of the effects of nitric oxide are mediated by the direct modification of cysteine residues resulting in an adduct called a nitrosothiol. A method to detect proteins which contain nitrosothiols involves several steps. Nitrosylated cysteines are converted to tagged cysteines. Tagged proteins can then be detected, for example, by immunoblotting and/or can be purified by affinity chromatography. The method is applicable to the detection of S-nitrosylated proteins in cell lysates following in vitro S-nitrosylation, as well as to the detection of endogenous S-nitrosothiols in selected protein substrates.