Inhibitors of IAPP fibril formation and uses thereof

Details Inhibitors of IAPP fibril formation and uses thereof Inhibitors of IAPP fibril formation and uses thereof

2007-05-15

2007-05-15

Gupta, Anish (Department: 1654)

Drug, bio-affecting and body treating compositions

Designated organic active ingredient containing

Peptide containing doai

C530S329000

Reexamination Certificate

active

09956625

ABSTRACT:
New antifibrillogenic agents and compositions containing same, methods of using the antifibrillogenic agents and compositions for inhibiting amyloid fibril formation, and effective therapeutics for preventing or delaying the progression of, e g., Alzheimer's disease and diabetes.

REFERENCES:
patent: 5124314 (1992-06-01), Cooper
patent: 6087334 (2000-07-01), Beeley et al.
patent: 6359112 (2002-03-01), Kapurniotu et al.
patent: 289287 (1988-11-01), None
File CAPLUS on STN. An No. 2003:208785. Scorcchi et al. ‘Identification of Minimal Peptide Sequences in the (8-20) Domain of Human Islet Amyloid Polypeptide Involved in Fibrillogenesis.’ Journal of Structural Biology. vol. 141. No. 3. pp. 218-227.
(CONT. from U)—2003. Abstract Only.
Nilsson et al. ‘Analysis of Amylin Cleavage products Provides New Insights inot the Amyloidogenic Region of Human Amylin.’ J. Mol. Biol. (1999) 294, 1375-1385.
Jaikaran et al. ‘Identification of a Novel Human Islet Amyloid Polypeptide Beta-Sheet Domain and Factors Influencing Fibrillogenesis.’ J. Mol. Biol. (2001) 308, 515-525.
Merlini et al. ‘The systemic amyloidoses: clearer understanding of the molecular mechanisms offers hope for more effective therapies’, Journal of Internal Medicine (Feb. 2004) 255(2) 159-78.
Redondo et al. ‘Designing transthyretin mutants affecting telrameric structure: implications in amyloidogenicity’ Biochemical journal, (May 15, 2000) 348 Pt 1 167-72.
Rudinger et al., “Peptide Hormones” (Jun. 1976) Ed. J.A. Parsons, Univ. Park Press, Baltimore, pp. 1-7.
Betsholtz et al. (1989).FEBS Lett 251: 261-264.
Clark et al. (1993).Diabetologia 36: A136 ABSTRACT No. 520.
Clodi et al. (1998).Am. J. Physiol. 274: E903-E908.
de Koning et al. (1993).Diabetologia 36: 378-384.
Fraser et al. (1994).J. Mol. Biol. 244(1): 64-73.
Glenner and Wong (1984).Biochem. Biophys. Res. Comm. 120: 885-890.
Glenner and Wong (1984).Biochem. Biophys. Res Comm. 122: 1131-1135.
Griffiths et al. (1995).J. of the Am. Chem. Soc. 12: 3539-3546.
Higham et al. (2000).Eur. J. Biochem. 267: 4998-5004.
Higham et al. (2000).FEBS Lett 470: 55-60.
Hubbard et al. (1991).Biochem. J. 275: 785-788.
Jarret et al. (1993).Biochemistry 32: 4693-4697.
Jarret and Lansbury (1993).Cell 73: 1055-1058.
Johnson et al. (1989).N. Engl. J. Med. 321: 513-518.
Kahn et al. (1997).Diabetes 46: 1725-1732.
Kayed et al. (1999).J. Mol. Biol. 287: 781-796.
Lorenzo et al. (1994).Nature 368: 756-760.
Moriarty and Raleigh (1999).Biochemistry 38: 1811-1818.
Nilsson and Raleigh (1999).J. Mol. Biol. 294: 1375-1385.
Opie (1900).J. Exp. Med. 5: 397-428.
Saldanha and Mahadevan (1991).Protein Eng. 4: 539-544.
Serpell et al. (2000).J. Mol. Biol. 300: 1033-1039.
Tjernberg et al. (1997).J. Biol. Chem. 272: 12601-12605.
Westermark and Grimelius (1973).Acta Path. Microbiol. Scand., sect. A. 81:291-300.
Wood et al. (1996).J. Biol. Chem. 271:4086-4092.

Affiliated with

Also associated with

Rating

Inhibitors of IAPP fibril formation and uses thereof does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Inhibitors of IAPP fibril formation and uses thereof, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Inhibitors of IAPP fibril formation and uses thereof will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3775985