Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2006-01-24
2006-01-24
Gupta, Anish (Department: 1654)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C530S316000, C530S350000, C514S002600
Reexamination Certificate
active
06989363
ABSTRACT:
The present invention relates to the discovery of novel genes encoding an angiotensin converting enzyme, Angiotensin Converting Enzyme-2 (ACE-2). The invention provides therapeutics, prognostic and diagnostics methods for treating blood pressure related disorders as well as various types of allergic conditions, among others. Also disclosed are screening assays for identifying compounds for treating and preventing these conditions.
REFERENCES:
patent: 5359045 (1994-10-01), Soubrier et al.
patent: 5480793 (1996-01-01), Soubrier et al.
patent: 974664 (2000-01-01), None
patent: WO 90/03435 (1990-04-01), None
patent: WO 91/00354 (1991-01-01), None
patent: WO 91/00354 (1991-10-01), None
patent: WO 97/48801 (1997-12-01), None
patent: WO 98/31835 (1998-07-01), None
“Computerized Drug Design: Still Promising, Not Yet Here” Science vol. 256, pp. 441, Apr. 24, 1992.
Ngo et al. “Computational Complexity, Protein Structure Prediction, and the Levinthal Paradox.” The Protein Folding Problem and Tertiary Structure Prediction (Ed. K. Merz, Jr. and S. Le Grand) Birkhouser Boston, pp. 491-495. 1994.
Rudinger, J. (1976). Peptide Hormones (ed. J.A. Parsons) University Park Press, Baltimore pp. 1-7.
GenBank Accession No.: AL110224 for Homo sapiens mRNA; cDNA DKFZp434A014 (from clone DKFZp434A014); partial cds.
Takeuchi, K. et al., “Purification of human lung angiotensin-converting enzyme by high-performance liquid chromatography: properties and N-terminal amino acid sequence,”J. Biochem(Tokyo), Sep 1989; 106(3):442-5.
Bernstein et al., “The isolation of angiotensin-converting enzyme cDNA,”J Biol Chem.Aug. 15, 1988;263(23):11021-4.
Bernstein et al., “Mouse angiotensin-converting enzyme is a protein composed of two homologous domains,”J Biol Chem.Jul 15, 1989;264(20):11945-51.
Erdos et al., “The angiotensin I-converting enzyme,”Lab Invest.Apr 1987;56(4):345-8.
Ehlers et al., “Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme,”Proc Natl Acad Sci U S A.Oct 1989;86(20):7741-5.
Howard et al., “Transcription of testicular angiotensin-converting enzyme (ACE) is initiated within the 12th intron of the somatic ACE gene,”Mol Cell Biol.Aug 1990;10(8):4294-302.
Lattion et al., “The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, non-duplicated form of the enzyme,”FEBS Lett.Jul 31, 1989;252(1-2):99-104.
Soubrier et al., “Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning,”Proc Natl Acad Sci U S A.Dec 1988;85(24):9386-90.
Genbank accession No. p22966 angiotensin-converting enzyme, testis-specific isoform precursor (ace-t) (dipeptidyl carboxypeptidase i) (kininase ii).
Genbank accession No. p22967 angiotensin-converting enzyme, testis-specific isoform precursor (ace-t) (dipeptidyl carboxypeptidase i) (kininase ii).
Genbank accession No. p22968 angiotensin-converting enzyme, testis-specific isoform precursor (ace-t) (dipeptidyl carboxypeptidase i) (kininase ii).
Genbank accession No. p12821 angiotensin-converting enzyme, somatic isoform precursor (ace) (dipeptidyl carboxypeptidase i) (kininase ii) (cd143 antigen).
Genbank accession No. p12822 angiotensin-converting enzyme, somatic isoform precursor (ace) (dipeptidyl carboxypeptidase i) (kininase ii).
Genbank accession No. p09470 angiotensin-converting enzyme precursor, somatic (ace) (dipeptidyl carboxypeptidase i) (kininase ii).
Genbank accession No. p47820 angiotensin-converting enzyme, somatic isoform precursor (ace) (dipeptidyl carboxypeptidase i) (kininase ii).
Genbank accession No. q10714 angiotensin converting enzyme precursor (dipeptidyl carboxypeptidase i) (kininase ii).
Genbank accession No. U56966 Caenorhabditis elegans cosmid C42D8.
Genbank Accession No. X16295 Human mRNA for angiotensin I converting enzyme (ACE).
Genbank Accession No. J04144 Human angiotensin I-converting enzyme mRNA, complete cds.
Genbank Accession No. A00914 H.sapiens gene for angiotensine conversion enzyme (ACE).
Genbank Accession No. A31567 H.sapiens testicular ECA gene.
Genbank Accession No. M26657 Human testicular angiotensin converting enzyme mRNA, complete cds.
Genbank Accession No. M26658 Human testicular angiotensin converting enzyme mRNA (5' variant), complete cds.
Genbank Accession No. J04946 Mouse angiotensin-converting enzyme mRNA, 3' end, clone ACE.5.
Genbank Accession No. J04947 Mouse angiotensin-converting enzyme mRNA, 3' end, clone ACE.11.
Genbank Accession No. M55333 Mouse testis-specific angiotensin-converting enzyme mRNA, complete cds.
Genbank Accession No. J03940 Mouse angiotensin-converting enzyme mRNA, 5' end.
Genbank Accession No. U03734Rattus norvegicusWistar-Kyoto (Heidelberg) angiotensin converting enzyme (ACE) mRNA, complete cds.
Genbank Accession No. U03708Rattus norvegicusHeidelberg angiotensin converting enzyme (ACE) mRNA, complete cds.
Genbank accession No. aa397955 zt79h12.r1 soares_testis_nht homo sapiens cdna clone image:728615 5', mrna sequence.
Genbank accession No. aa420969 zt79h12.s2 soares_testis_nht homo sapiens cdna clone image:728615 3', mrna sequence.
Genbank accession No. aa162058 ms31h11.r1 stratagene mouse skin (#937313) mus musculus cdna clone image:608613 5' similar to sw:ace_mouse p09470 angiotensin-converting enzyme precursor, somatic ;, mrna sequence.
Genbank accession No. aa416585 zu05f02.s1 soares_testis_nht homo sapiens cdna clone image:730971 3',mrna sequence.
Genbank accession No. aa421125 zu05f02.r1 soares_testis_nht homo sapiens cdna clone image:730971 5',mrna sequence.
Soubrier et al., “Two Putative Active Centers in Human Angiotensin I-converting Enzyme Revealed by Molecular Cloning”,Proc. Natl. Acad. Sci., USA, vol. 85, pp. 9386-9390 (1988).
Bernstein et al., “Mouse Angiotensin-Converting Enzyme is a Protein Composed of Two Homologous Domains”,The Journal of Biological Chemistry, vol. 264, No. 20, pp. 11945-11951 (Jul. 15, 1989).
Lattion et al., “The Testicular Transcript of the Angiotensin I-converting Enzyme Encodes for the Ancestral, Non-duplicated Form of the Enzyme”,FEBS Letters, vol. 252, No. 1, 2, pp. 99-104 (Jul. 1989).
Erdös, Ervin G. and Skidgel, Randal A., Editorial “The Angiotensin I-Converting Enzyme”,Laboratory Investigation, vol. 56, No. 4, pp. 345-348 (1987).
Ehlers et al., “Molecular Cloning of Human Testicular Angiotensin-Converting Enzyme: the Testis Isozyme is Identical to the C-Terminal Half of Enothelial Angiotensin-Converting Enzyme”,Proc. Natl. Acad. Sci. USA, vol. 86, pp. 7741-7745, (Oct. 1989).
Howard et al., “Transcription of Testicular Angiotensin-Converting Enzyme (ACE) is Initiated within the 12thIntron of the Somatic ACE Gene”,Molecular and Cellular Biology, vol. 10, No. 8, pp. 4294-4302 (Aug. 1990); and.
Bernstein et al., “The Isolation of Angiotensin-Converting Enzyme cDNA”,The Journal of Biological Biochemistry, vol. 263, No. 23, pp. 11021-11024 (Aug. 15, 1988).
Acton Susan L.
Hsieh Frank Y.
Robison Keith Earl
Gupta Anish
Millennium Pharmaceuticals Inc.
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