UA68332C2 - Moraxeila catarrhalis outer membrane protein-106 (omp106) polypeptide, peptide fragment and encoding nucleotide sequences, antibodies binding omp106 polypeptide, vaccine and antigenic composition (variants), methods of inducing immune responses to m. catarrhalis in animals (variants), method for treatment and prevention of m. catarrhalis infection (variants) - Google Patents
Moraxeila catarrhalis outer membrane protein-106 (omp106) polypeptide, peptide fragment and encoding nucleotide sequences, antibodies binding omp106 polypeptide, vaccine and antigenic composition (variants), methods of inducing immune responses to m. catarrhalis in animals (variants), method for treatment and prevention of m. catarrhalis infection (variants) Download PDFInfo
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- UA68332C2 UA68332C2 UA98126370A UA98126370A UA68332C2 UA 68332 C2 UA68332 C2 UA 68332C2 UA 98126370 A UA98126370 A UA 98126370A UA 98126370 A UA98126370 A UA 98126370A UA 68332 C2 UA68332 C2 UA 68332C2
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- polypeptide
- omp106
- sequence
- catarrhalis
- variants
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/21—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Pseudomonadaceae (F)
- C07K14/212—Moraxellaceae, e.g. Acinetobacter, Moraxella, Oligella, Psychrobacter
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1203—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1203—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria
- C07K16/1214—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Pseudomonadaceae (F)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1203—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria
- C07K16/1217—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Neisseriaceae (F)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
- C07K2317/734—Complement-dependent cytotoxicity [CDC]
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Immunology (AREA)
- Gastroenterology & Hepatology (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Public Health (AREA)
- Communicable Diseases (AREA)
- Animal Behavior & Ethology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oncology (AREA)
- Veterinary Medicine (AREA)
- General Chemical & Material Sciences (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US08/642,712 US7341727B1 (en) | 1996-05-03 | 1996-05-03 | M. catarrhalis outer membrane protein-106 polypeptide, methods of eliciting an immune response comprising same |
PCT/US1997/007679 WO1997041731A1 (en) | 1996-05-03 | 1997-04-28 | Moraxella catarrhalis outer membrane protein-106 polypeptide, gene sequence and uses thereof |
Publications (1)
Publication Number | Publication Date |
---|---|
UA68332C2 true UA68332C2 (en) | 2004-08-16 |
Family
ID=24577687
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
UA98126370A UA68332C2 (en) | 1996-05-03 | 1997-04-28 | Moraxeila catarrhalis outer membrane protein-106 (omp106) polypeptide, peptide fragment and encoding nucleotide sequences, antibodies binding omp106 polypeptide, vaccine and antigenic composition (variants), methods of inducing immune responses to m. catarrhalis in animals (variants), method for treatment and prevention of m. catarrhalis infection (variants) |
Country Status (26)
Country | Link |
---|---|
US (6) | US7341727B1 (no) |
EP (1) | EP0900025B1 (no) |
JP (2) | JP4401437B2 (no) |
CN (2) | CN100415871C (no) |
AR (1) | AR006999A1 (no) |
AT (1) | ATE244016T1 (no) |
AU (1) | AU723528B2 (no) |
BG (1) | BG64832B1 (no) |
BR (1) | BR9711090A (no) |
CA (1) | CA2253636C (no) |
CZ (1) | CZ298034B6 (no) |
DE (1) | DE69723254T2 (no) |
EA (1) | EA002743B1 (no) |
EE (1) | EE04684B1 (no) |
ES (1) | ES2202624T3 (no) |
GE (1) | GEP20022695B (no) |
HK (2) | HK1021299A1 (no) |
HU (1) | HU223004B1 (no) |
NO (2) | NO324816B1 (no) |
NZ (1) | NZ332896A (no) |
PL (3) | PL189995B1 (no) |
SK (1) | SK284812B6 (no) |
TW (1) | TW541314B (no) |
UA (1) | UA68332C2 (no) |
WO (1) | WO1997041731A1 (no) |
ZA (1) | ZA973809B (no) |
Families Citing this family (71)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6440425B1 (en) * | 1995-05-01 | 2002-08-27 | Aventis Pasteur Limited | High molecular weight major outer membrane protein of moraxella |
US6335018B1 (en) * | 1995-05-01 | 2002-01-01 | Aventis Pasteur Limited | High molecular weight major outer membrane protein of moraxella |
US7341727B1 (en) * | 1996-05-03 | 2008-03-11 | Emergent Product Development Gaithersburg Inc. | M. catarrhalis outer membrane protein-106 polypeptide, methods of eliciting an immune response comprising same |
AUPO652897A0 (en) | 1997-04-30 | 1997-05-29 | University Of Melbourne, The | Synthetic peptide constructs for the diagnosis and treatment of periodontitis |
GB9714276D0 (en) | 1997-07-08 | 1997-09-10 | Univ Dundee | Peptides and related compounds |
US8129500B2 (en) * | 1997-12-10 | 2012-03-06 | Csl Limited | Porphyromonas gingivalis polypeptides and nucleotides |
GB9808720D0 (en) | 1998-04-23 | 1998-06-24 | Smithkline Beecham Biolog | Novel compounds |
GB9810084D0 (en) | 1998-05-11 | 1998-07-08 | Cortecs Uk Ltd | Proteins |
US6627728B1 (en) | 1998-05-12 | 2003-09-30 | Smithkline Beecham Biologicals S.A. | Compounds from moraxella catarrhalis |
GB9810193D0 (en) * | 1998-05-12 | 1998-07-08 | Smithkline Beecham Biolog | Novel compounds |
GB9810285D0 (en) | 1998-05-13 | 1998-07-15 | Smithkline Beecham Biolog | Novel compounds |
US6541616B1 (en) | 1998-10-01 | 2003-04-01 | Antex Biologics Inc. | Moraxella catarrhalis protein, gene sequence and uses thereof |
HU228499B1 (en) | 1999-03-19 | 2013-03-28 | Smithkline Beecham Biolog | Streptococcus vaccine |
US6673910B1 (en) | 1999-04-08 | 2004-01-06 | Genome Therapeutics Corporation | Nucleic acid and amino acid sequences relating to M. catarrhalis for diagnostics and therapeutics |
WO2000071724A2 (en) * | 1999-05-24 | 2000-11-30 | Smithkline Beecham Biologicals S.A. | Novel compounds from moraxella catarrhalis |
GB9915031D0 (en) * | 1999-06-25 | 1999-08-25 | Smithkline Beecham Biolog | Novel compounds |
AU1383901A (en) * | 1999-09-14 | 2001-04-17 | Smithkline Beecham Biologicals (Sa) | Novel compounds |
GB9921691D0 (en) * | 1999-09-14 | 1999-11-17 | Smithkline Beecham Sa | Novel compounds |
GB0022742D0 (en) | 2000-09-15 | 2000-11-01 | Smithkline Beecham Biolog | Vaccine |
GB0103171D0 (en) | 2001-02-08 | 2001-03-28 | Smithkline Beecham Biolog | Vaccine composition |
SE0102410D0 (sv) | 2001-07-04 | 2001-07-04 | Arne Forsgren | Novel surface exposed immunoglobulin D-binding protein from moraxella catarrhalis |
WO2004015099A2 (en) | 2002-08-02 | 2004-02-19 | Glaxosmithkline Biologicals Sa | Vaccine composition comprising lipooligosaccharide with reduced phase variability |
EP2425855A1 (en) | 2005-04-08 | 2012-03-07 | Wyeth LLC | Multivalent pneumococcal polysaccharide-protein conjugate composition |
CN100357318C (zh) * | 2005-10-11 | 2007-12-26 | 中山大学 | 美人鱼发光杆菌外膜蛋白w和编码序列及其制备方法和应用 |
TWI457133B (zh) | 2005-12-13 | 2014-10-21 | Glaxosmithkline Biolog Sa | 新穎組合物 |
LT3017827T (lt) | 2005-12-22 | 2019-01-10 | Glaxosmithkline Biologicals S.A. | Pneumokokinė polisacharidinė konjuguota vakcina |
GB0607088D0 (en) | 2006-04-07 | 2006-05-17 | Glaxosmithkline Biolog Sa | Vaccine |
ZA200805602B (en) | 2006-01-17 | 2009-12-30 | Arne Forsgren | A novel surface exposed haemophilus influenzae protein (protein E; pE) |
CA2652957A1 (en) | 2006-06-27 | 2008-01-03 | Oral Health Australia Pty Ltd. | Porphyromonas gingivalis polypeptides useful in the prevention of periodontal disease |
KR20100045445A (ko) | 2007-06-26 | 2010-05-03 | 글락소스미스클라인 바이오로지칼즈 에스.에이. | 스트렙토코쿠스 뉴모니애 캡슐 다당류 컨쥬게이트를 포함하는 백신 |
EP2176413A4 (en) | 2007-07-12 | 2012-08-01 | Oral Health Australia Pty Ltd | IMMUNOLOGY TREATMENT FOR BIOFILMS |
WO2009006699A1 (en) * | 2007-07-12 | 2009-01-15 | Oral Health Australia Pty Ltd | Biofilm treatment |
US8642046B2 (en) * | 2007-10-09 | 2014-02-04 | Tufts University | Cholera vaccines |
CN107266582B (zh) | 2008-08-29 | 2021-09-10 | 口腔健康澳洲私人有限公司 | 牙龈卟啉单胞菌感染的预防、治疗和诊断 |
US8140041B2 (en) * | 2009-08-27 | 2012-03-20 | Mediatek Inc. | Tunable capacitive device with linearization technique employed therein |
ES2366735B1 (es) * | 2009-10-08 | 2012-09-13 | Fundación Pública Andaluza Para La Gestión De La Investigación En Salud De Sevilla | Vacuna frente a acinetobacter baumannii. |
US9700889B2 (en) | 2009-11-23 | 2017-07-11 | Cyvek, Inc. | Methods and systems for manufacture of microarray assay systems, conducting microfluidic assays, and monitoring and scanning to obtain microfluidic assay results |
US10065403B2 (en) | 2009-11-23 | 2018-09-04 | Cyvek, Inc. | Microfluidic assay assemblies and methods of manufacture |
US9855735B2 (en) | 2009-11-23 | 2018-01-02 | Cyvek, Inc. | Portable microfluidic assay devices and methods of manufacture and use |
US9759718B2 (en) | 2009-11-23 | 2017-09-12 | Cyvek, Inc. | PDMS membrane-confined nucleic acid and antibody/antigen-functionalized microlength tube capture elements, and systems employing them, and methods of their use |
CN102713621B (zh) | 2009-11-23 | 2016-10-19 | 西维克公司 | 用于施行化验的方法和设备 |
US10022696B2 (en) | 2009-11-23 | 2018-07-17 | Cyvek, Inc. | Microfluidic assay systems employing micro-particles and methods of manufacture |
WO2013134742A2 (en) | 2012-03-08 | 2013-09-12 | Cyvek, Inc | Micro-tube particles for microfluidic assays and methods of manufacture |
US9500645B2 (en) | 2009-11-23 | 2016-11-22 | Cyvek, Inc. | Micro-tube particles for microfluidic assays and methods of manufacture |
GB201003924D0 (en) | 2010-03-09 | 2010-04-21 | Glaxosmithkline Biolog Sa | Immunogenic composition |
GB201003922D0 (en) | 2010-03-09 | 2010-04-21 | Glaxosmithkline Biolog Sa | Conjugation process |
JP2013521770A (ja) | 2010-03-10 | 2013-06-13 | グラクソスミスクライン バイオロジカルズ ソシエテ アノニム | ワクチン組成物 |
WO2011130434A2 (en) | 2010-04-13 | 2011-10-20 | Celldex Therapeutics Inc. | Antibodies that bind human cd27 and uses thereof |
US8501197B2 (en) | 2010-04-30 | 2013-08-06 | The Research Foundation for The State of New York | Compositions and methods for stimulating immune response against Moraxella catarrhalis |
GB201103836D0 (en) | 2011-03-07 | 2011-04-20 | Glaxosmithkline Biolog Sa | Conjugation process |
WO2012129455A2 (en) | 2011-03-22 | 2012-09-27 | Cyvek, Inc | Microfluidic devices and methods of manufacture and use |
RU2481401C2 (ru) * | 2011-07-15 | 2013-05-10 | Государственное образовательное учреждение высшего профессионального образования "Уральская государственная медицинская академия Министерства здравоохранения и социального развития Российской Федерации" (ГОУ ВПО УГМА Минздравсоцразвития России) | СПОСОБ ВЫЯВЛЕНИЯ β-ЛАКТАМАЗОПРОДУЦИРУЮЩИХ ОКСИДАЗОПОЗИТИВНЫХ ГРАМОТРИЦАТЕЛЬНЫХ ДИПЛОКОККОВ, ПОДОЗРИТЕЛЬНЫХ НА ПРИНАДЛЕЖНОСТЬ К MORAХELLA (BRANCHAMELLA) CATARRHALIS |
US11210432B2 (en) * | 2013-08-20 | 2021-12-28 | Janus Technologies, Inc. | Method and apparatus for selectively snooping and capturing data for secure computer interfaces |
EP3268037B1 (en) | 2015-03-09 | 2022-08-31 | Celldex Therapeutics, Inc. | Cd27 agonists |
GB201518684D0 (en) | 2015-10-21 | 2015-12-02 | Glaxosmithkline Biolog Sa | Vaccine |
US10228367B2 (en) | 2015-12-01 | 2019-03-12 | ProteinSimple | Segmented multi-use automated assay cartridge |
EP3445783A2 (en) | 2016-04-18 | 2019-02-27 | Celldex Therapeutics, Inc. | Agonistic antibodies that bind human cd40 and uses thereof |
GB201621686D0 (en) | 2016-12-20 | 2017-02-01 | Glaxosmithkline Biologicals Sa | Novel methods for inducing an immune response |
JP7291633B2 (ja) | 2017-05-30 | 2023-06-15 | グラクソスミスクライン バイオロジカルズ ソシエテ アノニム | アジュバントを製造する方法 |
CA3083078A1 (en) | 2017-12-01 | 2019-06-06 | Glaxosmithkline Biologicals Sa | Saponin purification |
BR112020021271A2 (pt) | 2018-04-17 | 2021-01-26 | Celldex Therapeutics, Inc. | construtos bispecíficos e anticorpos anti- cd27 e anti-pd-l1 |
MX2021001479A (es) | 2018-08-07 | 2021-04-28 | Glaxosmithkline Biologicals Sa | Novedosos procesos y vacunas. |
CN111157735B (zh) * | 2018-11-07 | 2023-02-07 | 广州万孚生物技术股份有限公司 | 凝集性卡他莫拉菌单克隆抗体及其制备方法和应用 |
US20220339282A1 (en) | 2018-11-29 | 2022-10-27 | Glaxosmithkline Biologicals Sa | Methods for manufacturing an adjuvant |
WO2020123444A1 (en) | 2018-12-11 | 2020-06-18 | Celldex Therapeutics, Inc. | Methods of using cd27 antibodies as conditioning treatment for adoptive cell therapy |
US20220235095A1 (en) | 2019-06-05 | 2022-07-28 | Glaxosmithkline Biologicals Sa | Saponin purification |
CN111778226B (zh) * | 2020-07-21 | 2022-04-05 | 东北师范大学 | 一种水稻耐碱胁迫相关的质膜H+-ATPase蛋白及其应用 |
AU2022253269A1 (en) | 2021-04-09 | 2023-11-23 | Celldex Therapeutics, Inc. | Antibodies against ilt4, bispecific anti-ilt4/pd-l1 antibody and uses thereof |
WO2023077521A1 (en) | 2021-11-08 | 2023-05-11 | Celldex Therapeutics, Inc | Anti-ilt4 and anti-pd-1 bispecific constructs |
GB202205833D0 (en) | 2022-04-21 | 2022-06-08 | Glaxosmithkline Biologicals Sa | Bacteriophage |
WO2024017827A1 (en) | 2022-07-19 | 2024-01-25 | Glaxosmithkline Biologicals Sa | Continuous process for vaccine production |
Family Cites Families (9)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4675176A (en) * | 1983-12-12 | 1987-06-23 | Norden Laboratories | Moraxella bovis protease vaccine |
US4879213A (en) * | 1986-12-05 | 1989-11-07 | Scripps Clinic And Research Foundation | Synthetic polypeptides and antibodies related to Epstein-Barr virus early antigen-diffuse |
US5552146A (en) * | 1991-08-15 | 1996-09-03 | Board Of Regents, The University Of Texas System | Methods and compositions relating to useful antigens of Moraxella catarrhalis |
US5607846A (en) | 1994-05-17 | 1997-03-04 | Research Foundation Of State University Of New York | Vaccine for moraxella catarrhalis |
US6440425B1 (en) | 1995-05-01 | 2002-08-27 | Aventis Pasteur Limited | High molecular weight major outer membrane protein of moraxella |
US6335018B1 (en) * | 1995-05-01 | 2002-01-01 | Aventis Pasteur Limited | High molecular weight major outer membrane protein of moraxella |
US7341727B1 (en) * | 1996-05-03 | 2008-03-11 | Emergent Product Development Gaithersburg Inc. | M. catarrhalis outer membrane protein-106 polypeptide, methods of eliciting an immune response comprising same |
GB9809683D0 (en) * | 1998-05-06 | 1998-07-01 | Smithkline Beecham Biolog | Novel compounds |
GB9812163D0 (en) * | 1998-06-05 | 1998-08-05 | Smithkline Beecham Biolog | Novel compounds |
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1996
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1997
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- 1997-04-28 NZ NZ332896A patent/NZ332896A/en not_active IP Right Cessation
- 1997-04-28 UA UA98126370A patent/UA68332C2/uk unknown
- 1997-04-28 DE DE69723254T patent/DE69723254T2/de not_active Expired - Lifetime
- 1997-04-28 CZ CZ0352498A patent/CZ298034B6/cs not_active IP Right Cessation
- 1997-04-28 PL PL97330935A patent/PL189995B1/pl not_active IP Right Cessation
- 1997-04-28 EA EA199800973A patent/EA002743B1/ru not_active IP Right Cessation
- 1997-04-28 BR BR9711090A patent/BR9711090A/pt not_active Application Discontinuation
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- 1997-04-28 AU AU31180/97A patent/AU723528B2/en not_active Ceased
- 1997-04-28 ES ES97926409T patent/ES2202624T3/es not_active Expired - Lifetime
- 1997-04-28 EP EP97926409A patent/EP0900025B1/en not_active Expired - Lifetime
- 1997-04-28 JP JP54015697A patent/JP4401437B2/ja not_active Expired - Fee Related
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- 1997-04-28 AT AT97926409T patent/ATE244016T1/de not_active IP Right Cessation
- 1997-04-28 SK SK1509-98A patent/SK284812B6/sk not_active IP Right Cessation
- 1997-04-28 EE EE9800373A patent/EE04684B1/xx not_active IP Right Cessation
- 1997-04-28 HU HU9902695A patent/HU223004B1/hu not_active IP Right Cessation
- 1997-05-01 TW TW086105809A patent/TW541314B/zh not_active IP Right Cessation
- 1997-05-02 ZA ZA9703809A patent/ZA973809B/xx unknown
- 1997-05-05 AR ARP970101850A patent/AR006999A1/es active IP Right Grant
- 1997-11-12 US US08/968,685 patent/US6214981B1/en not_active Expired - Fee Related
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1998
- 1998-11-02 NO NO19985113A patent/NO324816B1/no not_active IP Right Cessation
- 1998-12-02 BG BG102983A patent/BG64832B1/bg unknown
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2000
- 2000-01-18 HK HK00100316A patent/HK1021299A1/xx not_active IP Right Cessation
-
2001
- 2001-03-20 US US09/813,214 patent/US7128910B2/en not_active Expired - Fee Related
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2006
- 2006-08-18 NO NO20063711A patent/NO20063711L/no not_active Application Discontinuation
- 2006-10-16 US US11/580,854 patent/US7576179B2/en not_active Expired - Fee Related
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2007
- 2007-01-12 HK HK07100467.7A patent/HK1095358A1/xx not_active IP Right Cessation
- 2007-10-26 US US11/925,586 patent/US20080145916A1/en not_active Abandoned
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2008
- 2008-01-10 JP JP2008003407A patent/JP2008161194A/ja active Pending
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2009
- 2009-08-14 US US12/541,701 patent/US7914795B2/en not_active Expired - Fee Related
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