CA2554599A1 - Nouveaux variants de peptides cerebraux natriuretiques et leurs procede d'utilisation - Google Patents

Nouveaux variants de peptides cerebraux natriuretiques et leurs procede d'utilisation Download PDF

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Publication number: CA2554599A1
Authority: CA; Canada
Prior art keywords: humnatpep; pea; sequence; bnp; polypeptide
Prior art date: 2004-01-27
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Abandoned

Application number

CA002554599A

Other languages

English (en)

Inventor

Gad S. Cojocaru

Alexander Diber

Amit Novik

Sarah Pollock

Zurit Levine

Yossi Cohen

Michal Ayalon-Soffer

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Compugen USA Inc

Original Assignee

Individual

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

2004-01-27

Filing date

2005-01-27

Publication date

2005-08-11

2005-01-27 Application filed by Individual filed Critical Individual

2005-01-27 Priority claimed from US11/043,590 external-priority patent/US7332569B2/en

2005-08-11 Publication of CA2554599A1 publication Critical patent/CA2554599A1/fr

Status Abandoned legal-status Critical Current

Links

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238000004445 quantitative analysis Methods 0.000 description 1
108700042226 ras Genes Proteins 0.000 description 1
230000008707 rearrangement Effects 0.000 description 1
238000011084 recovery Methods 0.000 description 1
230000011514 reflex Effects 0.000 description 1
230000029865 regulation of blood pressure Effects 0.000 description 1
230000019705 regulation of vascular permeability Effects 0.000 description 1
230000024875 regulation of vasodilation Effects 0.000 description 1
238000007634 remodeling Methods 0.000 description 1
238000009877 rendering Methods 0.000 description 1
230000003252 repetitive effect Effects 0.000 description 1
230000000241 respiratory effect Effects 0.000 description 1
230000004043 responsiveness Effects 0.000 description 1
PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
229940100486 rice starch Drugs 0.000 description 1
210000003296 saliva Anatomy 0.000 description 1
238000003345 scintillation counting Methods 0.000 description 1
238000010187 selection method Methods 0.000 description 1
238000013207 serial dilution Methods 0.000 description 1
235000011803 sesame oil Nutrition 0.000 description 1
239000008159 sesame oil Substances 0.000 description 1
239000010703 silicon Substances 0.000 description 1
229910052710 silicon Inorganic materials 0.000 description 1
238000002603 single-photon emission computed tomography Methods 0.000 description 1
150000003384 small molecules Chemical class 0.000 description 1
235000019812 sodium carboxymethyl cellulose Nutrition 0.000 description 1
229920001027 sodium carboxymethylcellulose Polymers 0.000 description 1
239000007901 soft capsule Substances 0.000 description 1
239000012439 solid excipient Substances 0.000 description 1
239000002904 solvent Substances 0.000 description 1
230000037439 somatic mutation Effects 0.000 description 1
239000007921 spray Substances 0.000 description 1
210000003802 sputum Anatomy 0.000 description 1
208000024794 sputum Diseases 0.000 description 1
230000000087 stabilizing effect Effects 0.000 description 1
230000000638 stimulation Effects 0.000 description 1
210000002784 stomach Anatomy 0.000 description 1
230000004960 subcellular localization Effects 0.000 description 1
238000007920 subcutaneous administration Methods 0.000 description 1
239000005720 sucrose Substances 0.000 description 1
IIACRCGMVDHOTQ-UHFFFAOYSA-N sulfamic acid Chemical group NS(O)(=O)=O IIACRCGMVDHOTQ-UHFFFAOYSA-N 0.000 description 1
150000003456 sulfonamides Chemical group 0.000 description 1
BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 description 1
150000003457 sulfones Chemical group 0.000 description 1
150000003462 sulfoxides Chemical class 0.000 description 1
229910052717 sulfur Inorganic materials 0.000 description 1
229910021653 sulphate ion Inorganic materials 0.000 description 1
239000000829 suppository Substances 0.000 description 1
239000002511 suppository base Substances 0.000 description 1
230000001629 suppression Effects 0.000 description 1
238000001356 surgical procedure Methods 0.000 description 1
239000000375 suspending agent Substances 0.000 description 1
210000001258 synovial membrane Anatomy 0.000 description 1
239000006188 syrup Substances 0.000 description 1
235000020357 syrup Nutrition 0.000 description 1
230000009885 systemic effect Effects 0.000 description 1
230000008685 targeting Effects 0.000 description 1
229940124597 therapeutic agent Drugs 0.000 description 1
150000003568 thioethers Chemical class 0.000 description 1
125000003396 thiol group Chemical group [H]S* 0.000 description 1
150000003573 thiols Chemical class 0.000 description 1
RYYWUUFWQRZTIU-UHFFFAOYSA-K thiophosphate Chemical compound [O-]P([O-])([O-])=S RYYWUUFWQRZTIU-UHFFFAOYSA-K 0.000 description 1
230000002537 thrombolytic effect Effects 0.000 description 1
210000001685 thyroid gland Anatomy 0.000 description 1
239000010936 titanium Substances 0.000 description 1
239000004408 titanium dioxide Substances 0.000 description 1
230000001988 toxicity Effects 0.000 description 1
231100000419 toxicity Toxicity 0.000 description 1
FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 1
230000002103 transcriptional effect Effects 0.000 description 1
238000010361 transduction Methods 0.000 description 1
230000026683 transduction Effects 0.000 description 1
230000014621 translational initiation Effects 0.000 description 1
238000002054 transplantation Methods 0.000 description 1
150000003626 triacylglycerols Chemical class 0.000 description 1
QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
CYRMSUTZVYGINF-UHFFFAOYSA-N trichlorofluoromethane Chemical compound FC(Cl)(Cl)Cl CYRMSUTZVYGINF-UHFFFAOYSA-N 0.000 description 1
229940029284 trichlorofluoromethane Drugs 0.000 description 1
ZMANZCXQSJIPKH-UHFFFAOYSA-O triethylammonium ion Chemical compound CC[NH+](CC)CC ZMANZCXQSJIPKH-UHFFFAOYSA-O 0.000 description 1
239000001226 triphosphate Substances 0.000 description 1
235000011178 triphosphate Nutrition 0.000 description 1
125000002264 triphosphate group Chemical class [H]OP(=O)(O[H])OP(=O)(O[H])OP(=O)(O[H])O* 0.000 description 1
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
210000004881 tumor cell Anatomy 0.000 description 1
125000002948 undecyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
241001430294 unidentified retrovirus Species 0.000 description 1
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239000003071 vasodilator agent Substances 0.000 description 1
230000001196 vasorelaxation Effects 0.000 description 1
235000015112 vegetable and seed oil Nutrition 0.000 description 1
239000008158 vegetable oil Substances 0.000 description 1
229920002554 vinyl polymer Polymers 0.000 description 1
229940100445 wheat starch Drugs 0.000 description 1
229940075420 xanthine Drugs 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/58—Atrial natriuretic factor complex; Atriopeptin; Atrial natriuretic peptide [ANP]; Cardionatrin; Cardiodilatin
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/68—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids
- C12Q1/6876—Nucleic acid products used in the analysis of nucleic acids, e.g. primers or probes
- C12Q1/6883—Nucleic acid products used in the analysis of nucleic acids, e.g. primers or probes for diseases caused by alterations of genetic material
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q2600/00—Oligonucleotides characterized by their use
- C12Q2600/156—Polymorphic or mutational markers
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q2600/00—Oligonucleotides characterized by their use
- C12Q2600/158—Expression markers
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
- G01N2333/575—Hormones
- G01N2333/58—Atrial natriuretic factor complex; Atriopeptin; Atrial natriuretic peptide [ANP]; Brain natriuretic peptide [BNP, proBNP]; Cardionatrin; Cardiodilatin
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/52—Predicting or monitoring the response to treatment, e.g. for selection of therapy based on assay results in personalised medicine; Prognosis

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Organic Chemistry (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Engineering & Computer Science (AREA)
Genetics & Genomics (AREA)
Zoology (AREA)
General Health & Medical Sciences (AREA)
Molecular Biology (AREA)
Biochemistry (AREA)
Wood Science & Technology (AREA)
Medicinal Chemistry (AREA)
Analytical Chemistry (AREA)
Bioinformatics & Cheminformatics (AREA)
Cardiology (AREA)
Biophysics (AREA)
Veterinary Medicine (AREA)
Pathology (AREA)
Chemical Kinetics & Catalysis (AREA)
Gastroenterology & Hepatology (AREA)
Endocrinology (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Heart & Thoracic Surgery (AREA)
Public Health (AREA)
General Chemical & Material Sciences (AREA)
Toxicology (AREA)
Animal Behavior & Ethology (AREA)
Physics & Mathematics (AREA)
Biotechnology (AREA)
Immunology (AREA)
Microbiology (AREA)
Pharmacology & Pharmacy (AREA)
General Engineering & Computer Science (AREA)
Peptides Or Proteins (AREA)

CA002554599A 2004-01-27 2005-01-27 Nouveaux variants de peptides cerebraux natriuretiques et leurs procede d'utilisation Abandoned CA2554599A1 (fr)

Applications Claiming Priority (15)

Application Number	Priority Date	Filing Date	Title
US53912704P	2004-01-27	2004-01-27
US60/539,127		2004-01-27
US58785104P	2004-07-15	2004-07-15
US60/587,851		2004-07-15
US60724604P	2004-09-07	2004-09-07
US60/607,246		2004-09-07
US62201604P	2004-10-27	2004-10-27
US62232004P	2004-10-27	2004-10-27
US60/622,016		2004-10-27
US60/622,320		2004-10-27
US62819004P	2004-11-17	2004-11-17
US60/628,190		2004-11-17
PCT/IB2005/000995 WO2005072055A2 (fr)	2004-01-27	2005-01-27	Nouveaux variants de peptides cerebraux natriuretiques et leurs procede d'utilisation
US11/043,590 US7332569B2 (en)	2004-01-27	2005-01-27	Brain natriuretic peptide spliced variant
US11/043,590		2005-01-27

Publications (1)

Publication Number	Publication Date
CA2554599A1 true CA2554599A1 (fr)	2005-08-11

Family

ID=34831546

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
CA002554599A Abandoned CA2554599A1 (fr)	2004-01-27	2005-01-27	Nouveaux variants de peptides cerebraux natriuretiques et leurs procede d'utilisation

Country Status (4)

Country	Link
EP (1)	EP1730181A2 (fr)
AU (1)	AU2005207886A1 (fr)
CA (1)	CA2554599A1 (fr)
WO (1)	WO2005072055A2 (fr)

Families Citing this family (35)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CN101208353B (zh)	2003-06-20	2011-12-14	梅约医学教育与研究基金会	脑利尿钠肽的同种型
PL2348114T3 (pl)	2004-04-21	2019-08-30	Alexion Pharmaceuticals, Inc.	Koniugaty do dostarczania do kości i sposób ich wykorzystania do nakierowywania białek na kość
MX2008012663A (es)	2006-03-30	2008-10-13	Palatin Technologies Inc	Constructos ciclicos de peptidos natriureticos.
BRPI0716416A2 (pt) *	2006-08-08	2016-10-11	Mayo Foundation	polipeptídeo substancialmente puro entre 37 e 47 besíduos de aminoácido de comprimento, ácido nucléico isolado, vetor: célula hospedeira e composição farmacêutica
MX2009002504A (es)	2006-09-08	2009-05-22	Mayo Foundation	Polipeptidos acuareticos y natriureticos que carecen de actividad vasodilatadora.
WO2009014787A2 (fr)	2007-04-30	2009-01-29	Nanogen, Inc.	Dosage de plusieurs analytes
WO2009036448A2 (fr)	2007-09-15	2009-03-19	Mayo Foundation For Medical Education And Research	Agonistes des récepteurs peptidiques natriurétiques de type c
EP4209510B1 (fr)	2008-12-09	2024-01-31	F. Hoffmann-La Roche AG	Anticorps anti-pd-l1 et leur utilisation pour améliorer la fonction des lymphocytes t
KR101226165B1 (ko)	2009-07-23	2013-01-24	가부시키가이샤 이기스	피부 외용제 조성물
JP4790096B2 (ja)	2009-08-27	2011-10-12	株式会社イギス	鼻炎治療剤
EP2658979B1 (fr)	2010-12-27	2018-02-14	Alexion Pharmaceuticals, Inc.	Compositions contenant des peptides natriurétiques et leurs méthodes d'utilisation
DK2666475T3 (da)	2011-01-21	2017-11-20	Igisu Co Ltd	Terapeutisk middel til skaldethed
CA2845617A1 (fr) *	2011-08-18	2013-02-21	Otago Innovation Limited	Produits therapeutiques cardiovasculaires
CN107090028A (zh)	2011-08-30	2017-08-25	梅约医学教育与研究基金会	利钠多肽
WO2013103896A1 (fr)	2012-01-06	2013-07-11	Mayo Foundation For Medical Education And Research	Traitement de maladies cardiovasculaires ou rénales
US10052366B2 (en)	2012-05-21	2018-08-21	Alexion Pharmaceuticsl, Inc.	Compositions comprising alkaline phosphatase and/or natriuretic peptide and methods of use thereof
US10822596B2 (en)	2014-07-11	2020-11-03	Alexion Pharmaceuticals, Inc.	Compositions and methods for treating craniosynostosis
WO2016090251A1 (fr)	2014-12-05	2016-06-09	Alexion Pharmaceuticals, Inc.	Traitement de crise avec une phosphatase alcaline recombinée
US10603361B2 (en)	2015-01-28	2020-03-31	Alexion Pharmaceuticals, Inc.	Methods of treating a subject with an alkaline phosphatase deficiency
AU2016272282A1 (en)	2015-05-29	2018-01-25	Igisu Co., Ltd.	Cyclic peptide, and medicine, external preparation and cosmetic each containing said cyclic peptide
AU2016308624B2 (en)	2015-08-17	2022-06-23	Alexion Pharmaceuticals, Inc.	Manufacturing of alkaline phosphatases
EP3355904A4 (fr)	2015-09-28	2019-06-12	Alexion Pharmaceuticals, Inc.	Identification de régimes posologiques efficaces pour une thérapie de l'hypophosphatasie de remplacement de l'enzyme phosphatase alcaline non spécifique à des tissus (tnsalp)
JP2018533571A (ja)	2015-10-30	2018-11-15	アレクシオンファーマシューティカルズ，インコーポレイテッド	患者の頭蓋縫合早期癒合症を治療するための方法
EP3426286A4 (fr)	2016-03-08	2019-12-04	Alexion Pharmaceuticals, Inc.	Méthodes de traitement de l'hypophosphatasie chez l'enfant
KR20180125979A (ko)	2016-04-01	2018-11-26	알렉시온 파마슈티칼스, 인코포레이티드	알칼리성 포스파타아제로 근육 약화의 치료
WO2017173395A1 (fr)	2016-04-01	2017-10-05	Alexion Pharmaceuticals, Inc.	Méthodes de traitement de l'hypophosphatasie chez les adolescents et les adultes
US10988744B2 (en)	2016-06-06	2021-04-27	Alexion Pharmaceuticals, Inc.	Method of producing alkaline phosphatase
JP7018933B2 (ja)	2016-08-18	2022-02-14	アレクシオンファーマシューティカルズ，インコーポレイテッド	気管気管支軟化症の治療方法
US9611297B1 (en)	2016-08-26	2017-04-04	Thrasos Therapeutics Inc.	Compositions and methods for the treatment of cast nephropathy and related conditions
MX2019011508A (es)	2017-03-31	2019-11-01	Alexion Pharma Inc	Metodos para tratar la hipofosfatasia (hpp) en adultos y adolescentes.
US11913039B2 (en)	2018-03-30	2024-02-27	Alexion Pharmaceuticals, Inc.	Method for producing recombinant alkaline phosphatase
JP7820148B2 (ja)	2018-08-10	2026-02-25	アレクシオンファーマシューティカルズ，インコーポレイテッド	アルカリホスファターゼを用いて神経線維腫症１型および関連状態を治療する方法
MX2022007114A (es)	2019-12-09	2022-07-11	Alexion Pharma Inc	Polipeptidos de fosfatasa alcalina y metodos de uso de los mismos.
MX2023002673A (es)	2020-09-04	2023-05-12	Alexion Pharma Inc	Métodos para el tratamiento de trastornos de mineralización ósea.
EP4291224A4 (fr)	2021-02-12	2025-01-01	Alexion Pharmaceuticals, Inc.	Polypeptides de phosphatase alcaline et leurs méthodes d'utilisation

2005
- 2005-01-27 EP EP05718453A patent/EP1730181A2/fr not_active Withdrawn
- 2005-01-27 WO PCT/IB2005/000995 patent/WO2005072055A2/fr not_active Ceased
- 2005-01-27 CA CA002554599A patent/CA2554599A1/fr not_active Abandoned
- 2005-01-27 AU AU2005207886A patent/AU2005207886A1/en not_active Abandoned

Also Published As

Publication number	Publication date
WO2005072055A2 (fr)	2005-08-11
AU2005207886A1 (en)	2005-08-11
WO2005072055A9 (fr)	2011-02-17
EP1730181A2 (fr)	2006-12-13

Legal Events

Date	Code	Title	Description
2011-01-27	FZDE	Dead

Publication	Publication Date	Title
EP1730181A2 (fr)	2006-12-13	Nouveaux variants de peptides cerebraux natriuretiques et leurs procede d'utilisation
US20080182299A1 (en)	2008-07-31	Novel brain natriuretic peptide variants and methods of use thereof
US20060147946A1 (en)	2006-07-06	Novel calcium channel variants and methods of use thereof
US20090215042A1 (en)	2009-08-27	Novel nucleotide and amino acid sequences, and assays and methods of use thereof for diagnosis
US20080014590A1 (en)	2008-01-17	Novel nucleotide and amino acid sequences, and assays and methods of use thereof for diagnosis of prostate cancer
US20060046257A1 (en)	2006-03-02	Novel nucleotide and amino acid sequences, and assays and methods of use thereof for diagnosis of lung cancer
US20030129176A1 (en)	2003-07-10	Atherosclerosis-associated genes
US20090304680A1 (en)	2009-12-10	Diagnosis and treatment of kawasaki disease
US7332569B2 (en)	2008-02-19	Brain natriuretic peptide spliced variant
US7345142B2 (en)	2008-03-18	Nucleotide and amino acid sequences, and assays and methods of use thereof for diagnosis of cardiac disease
US7714100B2 (en)	2010-05-11	Nucleotide and amino acid sequences, and assays and methods of use thereof for diagnosis of cardiac disease
US7528243B2 (en)	2009-05-05	Nucleotide and amino acid sequences, and assays and methods of use thereof for diagnosis of breast cancer
US20050186600A1 (en)	2005-08-25	Polynucleotides encoding novel UbcH10 polypeptides and kits and methods using same
JP2007525213A (ja)	2007-09-06	新規の脳性ナトリウム利尿ペプチドの変異体及びその利用方法
CA2554703A1 (fr)	2005-12-08	Expression differentielle de marqueurs dans le cancer de l'ovaire
JP2008507261A (ja)	2008-03-13	肺癌診断のための新規のヌクレオチド配列およびアミノ酸配列、ならびにそのアッセイおよび使用方法
WO2006043271A1 (fr)	2006-04-27	Nouvelles sequences d'acides amines et sequences nucleotidiques et methodes d'utilisation de celles-ci pour le diagnostic
US20090317808A1 (en)	2009-12-24	Novel nucleotide and amino acid sequences and methods of use thereof for diagnosis
CA2554440A1 (fr)	2005-08-11	Nouvelles sequences nucleotidiques et d'acides amines, et leurs dosages et procedes d'utilisation pour le diagnostic du cancer du sein
AU2002330177B2 (en)	2008-06-26	Methods for diagnosing and treating diseases and conditions of the heart or digestive system, and cancer
CA2554585A1 (fr)	2005-08-04	Nouvelles sequences de nucleotides et d'acides amines, et leurs dosages et procedes d'utilisation pour le diagnostic de maladies cardiaques
EP1735342A2 (fr)	2006-12-27	Nouvelles sequences de nucleotides et d'acides amines, et leurs dosages et procedes d'utilisation pour le diagnostic
US20020115627A1 (en)	2002-08-22	Phosphatonin-related gene and methods of use thereof
CA2554707A1 (fr)	2006-03-02	Nouvelles sequences de nucleotides et d'acides amines; essais et methodes d'utilisation pour le diagnostic du cancer de a la prostate
AU2002330177A1 (en)	2003-06-26	Methods for diagnosing and treating diseases and conditions of the heart or digestive system, and cancer