IL102294A - Soluble proteins comprising sequences from ctla4 receptor reactive with b7 antigen - Google Patents

Soluble proteins comprising sequences from ctla4 receptor reactive with b7 antigen

Info

Publication number: IL102294A
Authority: IL; Israel
Prior art keywords: amino acid; cells; ctla4; cell; acid sequence
Prior art date: 1991-06-27

Application number

IL10229492A

Other languages

English (en)

Other versions

IL102294A0 (en

Original Assignee

Bristol Myers Squibb Co

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.)

1991-06-27

Filing date

1992-06-24

Publication date

2004-09-27

Family has litigation

First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=24907003&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=IL102294(A) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.

1992-06-24 Application filed by Bristol Myers Squibb Co filed Critical Bristol Myers Squibb Co

1992-06-24 Priority to IL15936492A priority Critical patent/IL159364A/xx

1993-01-14 Publication of IL102294A0 publication Critical patent/IL102294A0/xx

2003-12-15 Priority to IL15936403A priority patent/IL159364A0/xx

2004-09-27 Publication of IL102294A publication Critical patent/IL102294A/en

Links

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IL10229492A 1991-06-27 1992-06-24 Soluble proteins comprising sequences from ctla4 receptor reactive with b7 antigen IL102294A (en)

Priority Applications (2)

Application Number	Priority Date	Filing Date	Title
IL15936492A IL159364A (en)	1991-06-27	1992-06-24	B7 ligand for use in a method for regulating functional ctla4 positive t cell interactions with b7 positive cells
IL15936403A IL159364A0 (en)	1991-06-27	2003-12-15	A b7 ligand for use in a method for regulating functional ctla4 positive t cell interactions with b7 positive cells

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
US72361791A	1991-06-27	1991-06-27

Publications (2)

Publication Number	Publication Date
IL102294A0 IL102294A0 (en)	1993-01-14
IL102294A true IL102294A (en)	2004-09-27

Family

ID=24907003

Family Applications (4)

Application Number	Title	Priority Date	Filing Date
IL10229492A IL102294A (en)	1991-06-27	1992-06-24	Soluble proteins comprising sequences from ctla4 receptor reactive with b7 antigen
IL15936492A IL159364A (en)	1991-06-27	1992-06-24	B7 ligand for use in a method for regulating functional ctla4 positive t cell interactions with b7 positive cells
IL15936403A IL159364A0 (en)	1991-06-27	2003-12-15	A b7 ligand for use in a method for regulating functional ctla4 positive t cell interactions with b7 positive cells
IL16243004A IL162430A0 (en)	1991-06-27	2004-06-10	Soluble proteins comprising sequences from ctla4 receptor reactive with b7 antigen

Family Applications After (3)

Application Number	Title	Priority Date	Filing Date
IL15936492A IL159364A (en)	1991-06-27	1992-06-24	B7 ligand for use in a method for regulating functional ctla4 positive t cell interactions with b7 positive cells
IL15936403A IL159364A0 (en)	1991-06-27	2003-12-15	A b7 ligand for use in a method for regulating functional ctla4 positive t cell interactions with b7 positive cells
IL16243004A IL162430A0 (en)	1991-06-27	2004-06-10	Soluble proteins comprising sequences from ctla4 receptor reactive with b7 antigen

Country Status (21)

Country	Link
US (1)	US5434131A (nl)
EP (1)	EP0606217B2 (nl)
JP (6)	JP3722375B2 (nl)
KR (1)	KR100238712B1 (nl)
AT (1)	ATE170562T1 (nl)
AU (1)	AU661854B2 (nl)
CA (2)	CA2110518C (nl)
DE (2)	DE122007000078I2 (nl)
DK (1)	DK0606217T4 (nl)
ES (1)	ES2123001T5 (nl)
FI (2)	FI112082B (nl)
IE (2)	IE922111A1 (nl)
IL (4)	IL102294A (nl)
LU (1)	LU91375I2 (nl)
MX (1)	MX9203605A (nl)
NL (1)	NL300303I1 (nl)
NO (4)	NO312465B1 (nl)
NZ (2)	NZ264712A (nl)
PT (1)	PT100637B (nl)
WO (1)	WO1993000431A1 (nl)
ZA (1)	ZA924782B (nl)

Families Citing this family (201)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CA2003455C (en) *	1988-11-23	2000-02-22	Craig B. Thompson	Immunotherapy involving cd28 stimulation
US6685941B1 (en) *	1988-11-23	2004-02-03	The Regents Of The University Of Michigan	Methods of treating autoimmune disease via CTLA-4Ig
US6406696B1 (en)	1989-10-27	2002-06-18	Tolerance Therapeutics, Inc.	Methods of stimulating the immune system with anti-CD3 antibodies
ATE168272T1 (de) *	1989-10-27	1998-08-15	Arch Dev Corp	Zusammensetzungen und deren verwendung zur förderung der immunopotentiation
US6887471B1 (en)	1991-06-27	2005-05-03	Bristol-Myers Squibb Company	Method to inhibit T cell interactions with soluble B7
US5637481A (en)	1993-02-01	1997-06-10	Bristol-Myers Squibb Company	Expression vectors encoding bispecific fusion proteins and methods of producing biologically active bispecific fusion proteins in a mammalian cell
US5851795A (en) *	1991-06-27	1998-12-22	Bristol-Myers Squibb Company	Soluble CTLA4 molecules and uses thereof
US5770197A (en) *	1991-06-27	1998-06-23	Bristol-Myers Squibb Company	Methods for regulating the immune response using B7 binding molecules and IL4-binding molecules
US6090914A (en) *	1991-06-27	2000-07-18	Bristol-Myers Squibb Company	CTLA4/CD28Ig hybrid fusion proteins and uses thereof
US5962406A (en) *	1991-10-25	1999-10-05	Immunex Corporation	Recombinant soluble CD40 ligand polypeptide and pharmaceutical composition containing the same
IL104684A0 (en) *	1992-02-14	1993-06-10	Bristol Myers Squibb Co	The cd40cr receptor and ligands therefor
US6472510B1 (en) *	1992-02-14	2002-10-29	Bristol-Myers Squibb Company	CD40 receptor ligands
EP0637963B1 (en) *	1992-04-07	2004-08-04	The Regents of the University of Michigan	Cd28 pathway immunoregulation
US5397703A (en) *	1992-07-09	1995-03-14	Cetus Oncology Corporation	Method for generation of antibodies to cell surface molecules
US5747034A (en) *	1992-07-09	1998-05-05	Chiron Corporation	Methods and materials for the induction of T cell anergy
US5773253A (en) *	1993-01-22	1998-06-30	Bristol-Myers Squibb Company	MYPPPY variants of CTL A4 and uses thereof
US6491916B1 (en)	1994-06-01	2002-12-10	Tolerance Therapeutics, Inc.	Methods and materials for modulation of the immunosuppresive activity and toxicity of monoclonal antibodies
US6106834A (en) *	1993-06-02	2000-08-22	Research Corporation Technologies, Inc.	Use of anti-CD45 leukocyte antigen antibodies for immunomodulation
US6024957A (en) *	1993-06-02	2000-02-15	Research Corporation Technologies, Inc.	Immunomodulators and methods for the prevention and reversal of organ transplant rejection using same
WO1995001994A1 (en) *	1993-07-09	1995-01-19	Synergen, Inc.	Recombinant ctla4 polypeptides and methods for making the same
US5861310A (en) *	1993-11-03	1999-01-19	Dana-Farber Cancer Institute	Tumor cells modified to express B7-2 with increased immunogenicity and uses therefor
WO1995003408A1 (en)	1993-07-26	1995-02-02	Dana-Farber Cancer Institute	B7-2: ctl a4/cd 28 counter receptor
US20050129670A1 (en) *	1993-07-26	2005-06-16	Genetics Institute, Llc.	Tumor cells modified to express B7-2 with increased immunogenicity and uses therefor
US6824779B1 (en)	1993-07-26	2004-11-30	Dana-Farber Cancer Institute, Inc.	Methods for inhibiting the interaction of B7-2 with its natural ligand
US6084067A (en)	1993-07-26	2000-07-04	Dana-Farber Cancer Institute	CTLA4/CD28 ligands and uses therefor
US6723705B1 (en)	1993-08-19	2004-04-20	Gentics Institute, Inc.	Tumor cells modified to express B7-2 with increased immunogenicity and uses therefor
US6130316A (en) *	1993-07-26	2000-10-10	Dana Farber Cancer Institute	Fusion proteins of novel CTLA4/CD28 ligands and uses therefore
AU7526894A (en) *	1993-08-16	1995-03-14	Arch Development Corporation	B7-2: ctla4/cd28 counter receptor
AU7638894A (en) *	1993-09-03	1995-03-22	Miyuki Azuma	B70(b7-2):ctla-4 bonding protein
ES2153895T3 (es) *	1994-03-08	2001-03-16	Dana Farber Cancer Inst Inc	Metodos para modular la insensibilidad de celulas t.
AU784510B2 (en) *	1994-03-08	2006-04-13	Dana-Farber Cancer Institute, Inc.	Methods for modulating T cell unresponsiveness
US6719972B1 (en) *	1994-06-03	2004-04-13	Repligen Corporation	Methods of inhibiting T cell proliferation or IL-2 accumulation with CTLA4- specific antibodies
EP0787188A1 (en) *	1994-11-01	1997-08-06	Targeted Genetics Corporation	Chimeric receptors for the generation of selectively-activatable t h?-independent cytotoxic t cells
AU4365196A (en) *	1994-12-02	1996-06-19	Schering Corporation	Purified genes encoding mammalian cell surface antigens; proteins and antibodies
US5576423A (en)	1994-12-02	1996-11-19	Schering Corporation	Antibodies to the slam protein expressed on activated T cells
US6251957B1 (en)	1995-02-24	2001-06-26	Trustees Of The University Of Pennsylvania	Method of reducing an immune response to a recombinant virus
US5652224A (en)	1995-02-24	1997-07-29	The Trustees Of The University Of Pennsylvania	Methods and compositions for gene therapy for the treatment of defects in lipoprotein metabolism
US6372208B1 (en)	1999-09-28	2002-04-16	The Trustees Of The University Of Pennsylvania	Method of reducing an immune response to a recombinant virus
US5872154A (en) *	1995-02-24	1999-02-16	The Trustees Of The University Of Pennsylvania	Method of reducing an immune response to a recombinant adenovirus
WO1996031229A1 (en) *	1995-04-05	1996-10-10	Beth Israel Hospital Association	Inhibiting rejection of a graft
US7175847B1 (en) *	1995-06-07	2007-02-13	Biogen Idec Inc.	Treating intestinal inflammation with anti-CD80 antibodies that do not inhibit CD80 binding to CTLA-4
US7153508B2 (en) *	1995-06-07	2006-12-26	Biogen Idec Inc.	Treatment of B cell lymphoma using anti-CD80 antibodies that do not inhibit the binding of CD80 to CTLA-4
US6113898A (en) *	1995-06-07	2000-09-05	Idec Pharmaceuticals Corporation	Human B7.1-specific primatized antibodies and transfectomas expressing said antibodies
US6051227A (en)	1995-07-25	2000-04-18	The Regents Of The University Of California, Office Of Technology Transfer	Blockade of T lymphocyte down-regulation associated with CTLA-4 signaling
US5811097A (en) *	1995-07-25	1998-09-22	The Regents Of The University Of California	Blockade of T lymphocyte down-regulation associated with CTLA-4 signaling
US5855887A (en) *	1995-07-25	1999-01-05	The Regents Of The University Of California	Blockade of lymphocyte down-regulation associated with CTLA-4 signaling
US7041634B2 (en)	1995-09-27	2006-05-09	Emory University	Method of inhibiting immune system destruction of transplanted viable cells
US6750334B1 (en)	1996-02-02	2004-06-15	Repligen Corporation	CTLA4-immunoglobulin fusion proteins having modified effector functions and uses therefor
US6107056A (en) *	1996-02-22	2000-08-22	Oaks; Martin K.	SCTLA-4 gene and product
WO1997034633A1 (en) *	1996-03-20	1997-09-25	Bristol-Myers Squibb Company	Methods for inhibiting an immune response by blocking the gp39/cd40 and ctla4/cd28/b7 pathways and compositions for use therewith
US5786152A (en) *	1996-04-26	1998-07-28	Amgen Inc.	Methods of inhibiting syp binding to a CTLA-4 receptor
AU739058B2 (en) *	1996-11-08	2001-10-04	Biogen Idec Inc.	Identification of unique binding interactions between certain antibodies and the human B7.1 and B7.2 co-stimulatory antigens
US20060034844A1 (en) *	1996-12-04	2006-02-16	The Regents Of The University Of California	Stimulation of T cells against self antigens using CTLA-4 blocking agents
US7235653B2 (en) *	1996-12-31	2007-06-26	Isis Pharmaceuticals, Inc.	Oligonucleotide compositions and methods for the modulation of the expression of B7 protein
US20040023917A1 (en) *	1996-12-31	2004-02-05	Bennett C. Frank	Oligonucleotide compositions and methods for the modulation of the expression of B7 protein
US6319906B1 (en)	1996-12-31	2001-11-20	Isis Pharmaceuticals	Oligonucleotide compositions and methods for the modulation of the expression of B7 protein
US6077833A (en) *	1996-12-31	2000-06-20	Isis Pharmaceuticals, Inc.	Oligonucleotide compositions and methods for the modulation of the expression of B7 protein
KR19980066046A (ko) *	1997-01-18	1998-10-15	정용훈	고역가의 CTLA4-Ig 융합단백질
ZA98533B (en) *	1997-01-31	1999-07-22	Bristol Myers Squibb Co	Soluble CTLA4 mutant molecules and uses thereof.
US20030219863A1 (en) *	1997-01-31	2003-11-27	Bristol-Myers Squibb Company	Soluble CTLA4 mutant molecules and uses thereof
WO1998042752A1 (en)	1997-03-21	1998-10-01	Brigham And Women's Hospital Inc.	Immunotherapeutic ctla-4 binding peptides
SE9701127D0 (sv) *	1997-03-26	1997-03-26	Karolinska Innovations Ab	Antigenic fusionprotein carrying GALal, 3GAL epitopes
EP0972054B1 (en) *	1997-03-27	2008-12-10	Csl Limited	Enhancement of immune response using targeting molecules
DE69837085T3 (de)	1997-04-16	2012-01-12	Millennium Pharmaceuticals, Inc.	Crsp-proteine (cystein-reiche, sekretierte proteine), die dafür kodierenden nukleinsäuren und ihre verwendungen
DE69823352T2 (de) *	1997-06-12	2004-09-02	Applied Research Systems Ars Holding N.V.	Cd28/ctla-4 inhibierende peptidomimetika und diese enthaltende pharmazeutische zusammensetzungen
AU9095498A (en) *	1997-09-19	1999-04-12	Yoshitomi Pharmaceutical Industries, Ltd.	Oligopeptide compounds
US7223729B2 (en) *	1997-11-07	2007-05-29	Trillium Therapeutics Inc.	Methods of treating allergy by administering a CD200 protein
US6955811B2 (en) *	1997-11-07	2005-10-18	Trillium Therapeutics Inc.	Methods of inhibiting immune response suppression by administering antibodies to OX-2
WO1999024565A1 (en) *	1997-11-07	1999-05-20	Transplantation Technologies Inc.	Methods and compositions for immunomodulation
AUPP221098A0 (en) *	1998-03-06	1998-04-02	Diatech Pty Ltd	V-like domain binding molecules
WO1999052552A1 (en) *	1998-04-15	1999-10-21	Brigham & Women's Hospital, Inc.	T cell inhibitory receptor compositions and uses thereof
US7279168B2 (en)	1998-05-01	2007-10-09	Texas A & M University System	Recombinant virus expressing foreign DNA encoding feline CD86 and uses thereof
NZ507794A (en) *	1998-05-01	2003-10-31	Texas A & M Univ Sys	Feline CD80, feline CD86, feline CD28, and feline CTLA- 4 nucleic acid and polypeptides
US7078512B2 (en)	1998-05-01	2006-07-18	Schering-Plough Animal Health Corporation	Nucleic acid encoding feline CD86
US20050031611A1 (en) *	1998-05-08	2005-02-10	Beth Israel Deaconess Medical Center	Transplant tolerance by costimulation blockade and T-cell activation-induced apoptosis
US6682741B1 (en) *	1998-06-10	2004-01-27	The United States Of America As Represented By The Department Of Health And Human Services	β2 microglobulin fusion proteins and high affinity variants
US20050181482A1 (en) *	2004-02-12	2005-08-18	Meade Harry M.	Method for the production of an erythropoietin analog-human IgG fusion proteins in transgenic mammal milk
CA2330527A1 (en) *	1998-06-15	1999-12-23	Genzyme Transgenics Corporation	Erythropoietin analog-human serum albumin fusion
US6593133B1 (en)	1998-07-06	2003-07-15	Nsgene A/S	Neurotrophic factors
CA2343916A1 (en)	1998-09-21	2000-03-30	Genetics Institute, Inc.	Methods of downmodulating the immune response to therapeutic proteins
US6800457B2 (en)	1998-09-22	2004-10-05	Bristol-Myers Squibb Company	Expression vectors containing hot spot for increased recombinant protein expression in transfected cells
US6521419B1 (en)	1998-09-22	2003-02-18	Kanakaraju Koduri	Expression vectors containing hot spot for increased recombinant protein expression in transfected cells
US7109003B2 (en)	1998-12-23	2006-09-19	Abgenix, Inc.	Methods for expressing and recovering human monoclonal antibodies to CTLA-4
CA2356215C (en)	1998-12-23	2015-11-24	Pfizer Inc.	Human monoclonal antibodies to ctla-4
US6682736B1 (en)	1998-12-23	2004-01-27	Abgenix, Inc.	Human monoclonal antibodies to CTLA-4
US7011833B1 (en)	1999-05-06	2006-03-14	Genetics Institute, Inc.	Enhancing immune responses with B7-1 or B7-2 in the absence of a crosslinking agent
WO2001008700A1 (en) *	1999-07-28	2001-02-08	Genetics Institute, Inc.	Preventing immune-mediated abortion by inhibiting costimulation
ATE354655T1 (de)	1999-08-24	2007-03-15	Medarex Inc	Humane antikörper gegen ctla-4 und deren verwendungen
US7605238B2 (en)	1999-08-24	2009-10-20	Medarex, Inc.	Human CTLA-4 antibodies and their uses
ATE360031T1 (de) *	2000-01-03	2007-05-15	Tr Associates L L C	Chimäre proteine und anwendungen
US7572631B2 (en) *	2000-02-24	2009-08-11	Invitrogen Corporation	Activation and expansion of T cells
US7541184B2 (en)	2000-02-24	2009-06-02	Invitrogen Corporation	Activation and expansion of cells
HU228137B1 (en) *	2000-05-26	2012-12-28	Bristol Myers Squibb Co	Soluble ctla4 mutant molecules and uses thereof
US7094874B2 (en)	2000-05-26	2006-08-22	Bristol-Myers Squibb Co.	Soluble CTLA4 mutant molecules
CA2411962A1 (en) *	2000-06-09	2001-12-20	Bristol-Myers Squibb Company	Methods for regulating a cell-mediated immune response by blockinglymphocytic signals and by blocking lfa-1 mediated adhesion
US20040034193A1 (en) *	2001-06-13	2004-02-19	Samy Ashkar	Biosynthetic oncolytic molecules and uses therefor
US20050048614A1 (en) *	2000-06-13	2005-03-03	Children's Medical Center Corporation	Biosynthetic oncolytic molecules and uses therefor
US20040022787A1 (en)	2000-07-03	2004-02-05	Robert Cohen	Methods for treating an autoimmune disease using a soluble CTLA4 molecule and a DMARD or NSAID
TWI322153B (en)	2000-07-03	2010-03-21	Bristol Myers Squibb Co	Methods for treating rheumatic diseases using a soluble ctla4 molecule
US6875904B2 (en) *	2000-09-20	2005-04-05	The Ohio State University Research Foundation	Animal model for identifying agents that inhibit or enhance CTLA4 signaling
US7014998B2 (en) *	2000-09-30	2006-03-21	Yale University	Screening immunomodulatory agents by CTLA-4 upregulation
US20040198661A1 (en) *	2000-12-08	2004-10-07	Bowdish Katherine S.	Polypeptides and antibodies derived from chronic lymphocytic leukemia cells and uses thereof
US20060057651A1 (en) *	2000-12-08	2006-03-16	Bowdish Katherine S	Polypeptides and antibodies derived from chronic lymphocytic leukemia cells and uses thereof
US7408041B2 (en)	2000-12-08	2008-08-05	Alexion Pharmaceuticals, Inc.	Polypeptides and antibodies derived from chronic lymphocytic leukemia cells and uses thereof
US9249229B2 (en) *	2000-12-08	2016-02-02	Alexion Pharmaceuticals, Inc.	Polypeptides and antibodies derived from chronic lymphocytic leukemia cells and uses thereof
AU2002246632B2 (en) *	2000-12-08	2007-04-05	Alexion Pharmaceuticals, Inc.	Chronic lymphocytic leukemia cell line and its use for producing an antibody
US20030133939A1 (en) *	2001-01-17	2003-07-17	Genecraft, Inc.	Binding domain-immunoglobulin fusion proteins
US7754208B2 (en) *	2001-01-17	2010-07-13	Trubion Pharmaceuticals, Inc.	Binding domain-immunoglobulin fusion proteins
US7829084B2 (en)	2001-01-17	2010-11-09	Trubion Pharmaceuticals, Inc.	Binding constructs and methods for use thereof
AU2002243905B2 (en) *	2001-01-26	2007-11-08	Emory University	Methods of inducing organ transplant tolerance and correcting hemoglobinopathies
TWI329129B (en) *	2001-02-08	2010-08-21	Wyeth Corp	Modified and stabilized gdf propeptides and uses thereof
CA2442159C (en)	2001-03-28	2011-08-23	Biogen, Inc.	Treatment using neublastin polypeptides
US20040058445A1 (en) *	2001-04-26	2004-03-25	Ledbetter Jeffrey Alan	Activation of tumor-reactive lymphocytes via antibodies or genes recognizing CD3 or 4-1BB
DK1397153T3 (da)	2001-05-23	2008-05-26	Bristol Myers Squibb Co	Fremgangsmåde til beskyttelse af allogent ö-celle-transplantat ved anvendelse af oplöselige CTLA4-mutantmolekyler
KR100453877B1 (ko)	2001-07-26	2004-10-20	메덱스젠 주식회사	연쇄체화에 의한 면역 글로블린 융합 단백질의 제조 방법 및 이 방법에 의해 제조된 ＴＮＦＲ/Ｆｃ 융합 단백질, 상기 단백질을 코딩하는 ＤＮＡ, 상기 ＤＮＡ를 포함하는벡터, 및 상기 벡터에 의한 형질전환체
US20030086940A1 (en) *	2001-08-10	2003-05-08	Cristina Costa	Engineered recombinant molecule that regulates humoral and cellular effector functions of the immune system
US20040116675A1 (en) *	2001-12-14	2004-06-17	Tso J. Jun	Silenced anti-cd28 antibodies and use thereof
JP2005527191A (ja) *	2001-12-18	2005-09-15	アンドキューブソシエタパーアクシオンシンプリフィー	新規の細胞死関連タンパク質ならびにアポトーシス制御におけるｔｈａｐ１およびｐａｒ４の経路
US7858297B2 (en) *	2001-12-18	2010-12-28	Centre National De La Recherche Scientifique Cnrs	Chemokine-binding protein and methods of use
US6578724B1 (en) *	2001-12-29	2003-06-17	United States Can Company	Connector for use in packaging aerosol containers
WO2003070823A2 (en)	2002-02-20	2003-08-28	The General Hospital Corporation	Conjugates comprising a biodegradable polymer and uses therefor
US20030219436A1 (en) *	2002-03-15	2003-11-27	Ledbetter Jeffrey A.	Compositions and methods to regulate an immune response using CD83 gene expressed in tumors and using soluble CD83-Ig fusion protein
AU2003234736B2 (en)	2002-04-12	2008-09-25	E. R. Squibb & Sons, L.L.C.	Methods of treatment using CTLA-4 antibodies
WO2003092624A2 (en) *	2002-05-02	2003-11-13	University Of Connecticut Health Center	Use of heat shock proteins to enhance efficacy of antibody therapeutics
WO2004034995A2 (en) *	2002-10-15	2004-04-29	University Of Pittsburgh Of The Commonwealth System Of Higher Education	Methods and reagents for inducing immunity
AU2003303394B2 (en) *	2002-12-23	2009-02-19	Bristol-Myers Squibb Company	Product quality enhancement in mammalian cell culture processes for protein production
CA2511520A1 (en) *	2002-12-23	2004-07-15	Bristol-Myers Squibb Company	Mammalian cell culture processes for protein production
CA2514510C (en)	2003-01-31	2013-10-01	Biogen Idec Ma Inc.	Polymer conjugates of mutated neublastin
GB0303663D0 (en) *	2003-02-18	2003-03-19	Lorantis Ltd	Assays and medical treatments
US7897582B2 (en) *	2003-05-23	2011-03-01	Isis Pharmaceuticals, Inc.	Oligonucleotide compositions and methods for the modulation of the expression of B7 protein
US7960355B2 (en) *	2003-05-23	2011-06-14	Isis Pharmaceuticals, Inc.	Compositions and methods for the modulation of the expression of B7 protein
US6971600B2 (en) *	2003-06-30	2005-12-06	Heligear Engineering (H.K.) Co., Ltd.	Oscillation mechanism for fishing reel
US7754209B2 (en)	2003-07-26	2010-07-13	Trubion Pharmaceuticals	Binding constructs and methods for use thereof
BRPI0413326A (pt) *	2003-08-04	2006-10-10	Bristol Myers Squibb Co	métodos para tratar doença cardiovasculares empregando-se uma molécula ctla4 solúvel
WO2005044188A2 (en) *	2003-10-27	2005-05-19	Amgen Inc.	Compositions and methods to modulate an immune response to an immunogenic therapeutic agent
US20080152655A1 (en) *	2004-09-08	2008-06-26	The Ohio State University Research Foundation	Combination Therapy With Anti-Ctla4 and Anti-4-1BB Antibodies
US20090252741A1 (en) *	2004-09-08	2009-10-08	Ohio State University Research Foundation	Human monoclonal anti-ctla4 antibodies in cancer treatment
GB0421465D0 (en) *	2004-09-27	2004-10-27	Chiron Srl	Group A streptococcus protein
ES2634260T3 (es) *	2005-04-06	2017-09-27	Bristol-Myers Squibb Company	Métodos para tratar trastornos inmunitarios asociados a trasplante de injertos con moléculas de CTLA4 mutantes solubles
SG177944A1 (en)	2005-07-11	2012-02-28	Macrogenics Inc	Methods for the treatment of autoimmune disorders using immunosuppressive monoclonal antibodies with reduced toxicity
US10307481B2 (en)	2005-07-25	2019-06-04	Aptevo Research And Development Llc	CD37 immunotherapeutics and uses thereof
JP4899083B2 (ja) *	2005-08-29	2012-03-21	Ｓｍｃ株式会社	減速比自動切換装置
AU2006311586A1 (en) *	2005-11-08	2007-05-18	Avi Biopharma, Inc.	Immunosuppression compound and treatment method
AU2013202533B2 (en) *	2005-11-08	2015-11-12	Sarepta Therapeutics, Inc.	Immunosuppression Compound and Treatment Method
US8501704B2 (en)	2005-11-08	2013-08-06	Sarepta Therapeutics, Inc.	Immunosuppression compound and treatment method
CN101325971A (zh)	2005-12-07	2008-12-17	米德列斯公司	Ctla-4抗体剂量递增方案
ES2439641T3 (es)	2005-12-20	2014-01-24	Bristol-Myers Squibb Company	Composiciones y procedimientos de producción de una composición
ES2709672T3 (es)	2006-01-12	2019-04-17	Alexion Pharma Inc	Anticuerpos para OX-2/CD200 y usos de los mismos
JP2009531324A (ja)	2006-03-20	2009-09-03	ザリージェンツオブザユニバーシティオブカリフォルニア	癌標的化のための操作された抗前立腺幹細胞抗原（ｐｓｃａ）抗体
US7528111B2 (en) *	2006-05-12	2009-05-05	Bristol-Myers Squibb Company	Method of vaccinating subjects receiving immune modulating therapy
RU2487888C2 (ru)	2006-06-12	2013-07-20	ЭМЕРДЖЕНТ ПРОДАКТ ДИВЕЛОПМЕНТ СИЭТЛ, ЭлЭлСи	Одноцепочечные мультивалентные связывающие белки с эффекторной функцией
MX2008015771A (es)	2006-06-14	2009-01-27	Macrogenics Inc	Metodos para el tratamiento de padecimientos autoinmunes usando anticuerpos monoclonales con toxicidad reducida.
US8986684B2 (en) *	2007-07-25	2015-03-24	Alexion Pharmaceuticals, Inc.	Methods and compositions for treating autoimmune disease
JP6126773B2 (ja)	2007-09-04	2017-05-10	ザリージェンツオブザユニバーシティオブカリフォルニア	癌のターゲッティングおよび検出のための高親和性抗前立腺幹細胞抗原（ｐｓｃａ）抗体
EP2612867A1 (en)	2007-11-01	2013-07-10	Perseid Therapeutics LLC	Immunosuppressive polypeptides and nucleic acids
NZ603059A (en)	2008-04-11	2014-07-25	Emergent Product Dev Seattle	Cd37 immunotherapeutic and combination with bifunctional chemotherapeutic thereof
US7915222B2 (en) *	2008-05-05	2011-03-29	Bristol-Myers Squibb Company	Method of preventing the development of rheumatoid arthritis in subjects with undifferentiated arthritis
CN107056951A (zh)	2008-10-02	2017-08-18	阿帕特夫研究和发展有限公司	Cd86拮抗物多靶点结合蛋白
NZ620326A (en) *	2008-11-13	2015-07-31	Emergent Product Dev Seattle	Cd37 immunotherapeutic combination therapies and uses thereof
JP5883384B2 (ja) *	2009-08-13	2016-03-15	ザジョンズホプキンスユニバーシティー	免疫機能を調節する方法
US9540426B2 (en)	2009-10-06	2017-01-10	Bristol-Myers Squibb Company	Mammalian cell culture processes for protein production
US8435516B2 (en)	2009-10-12	2013-05-07	Pfizer Inc.	Cancer treatment
US8642557B2 (en)	2010-03-12	2014-02-04	Abbvie Biotherapeutics Inc.	CTLA4 proteins and their uses
ES2993140T3 (en)	2010-04-02	2024-12-23	Amunix Pharmaceuticals Inc	Binding fusion proteins, binding fusion protein-drug conjugates, xten-drug conjugates and methods of making and using same
WO2012042480A1 (en)	2010-09-28	2012-04-05	Kahr Medical Ltd.	Compositions and methods for treatment of hematological malignancies
WO2013010537A1 (en)	2011-07-20	2013-01-24	Aarhus Universitet	Method of treating morphea
US9758566B2 (en)	2012-03-29	2017-09-12	The General Hospital Corporation	Recombinant cytotoxic T-lymphocyte-associated protein 4 (CTLA4)
US20150118244A1 (en)	2012-05-10	2015-04-30	Bristol-Myers Squibb Company	Anti-tumor antibodies as predictive or prognostic biomarkers of efficacy and survival in ipilimumab-treated patients
AU2013260172B2 (en)	2012-05-11	2017-11-23	Medimmune Limited	CTLA-4 variants
US8735359B2 (en)	2012-05-24	2014-05-27	Orban Biotech Llc	Combinations of modalities for the treatment of diabetes
KR20150033703A (ko)	2012-06-27	2015-04-01	오르반 바이오테크 엘엘씨	당뇨병 치료를 위한 ctla4 융합 단백질
US20140112958A1 (en)	2012-10-24	2014-04-24	Mwm Biomodels Gmbh	Pancreatic islets of transgenic LEA29Y animals for treating diabetes
WO2014138188A1 (en)	2013-03-07	2014-09-12	The General Hospital Corporation	Human ctla4 mutants and use thereof
WO2015048312A1 (en)	2013-09-26	2015-04-02	Costim Pharmaceuticals Inc.	Methods for treating hematologic cancers
EP2883883A1 (en)	2013-12-16	2015-06-17	Cardio3 Biosciences S.A.	Therapeutic targets and agents useful in treating ischemia reperfusion injury
JOP20200094A1 (ar)	2014-01-24	2017-06-16	Dana Farber Cancer Inst Inc	جزيئات جسم مضاد لـ pd-1 واستخداماتها
JOP20200096A1 (ar)	2014-01-31	2017-06-16	Children’S Medical Center Corp	جزيئات جسم مضاد لـ tim-3 واستخداماتها
GB2523399B (en)	2014-02-25	2019-03-13	Orban Tihamer	A composition comprising ten overlapping peptide fragments of the entire preproinsulin sequence
LT3116909T (lt)	2014-03-14	2020-02-10	Novartis Ag	Antikūno molekulės prieš lag-3 ir jų panaudojimas
CA2960824A1 (en)	2014-09-13	2016-03-17	Novartis Ag	Combination therapies of alk inhibitors
EP3240801B1 (en)	2014-12-31	2021-01-20	Checkmate Pharmaceuticals, Inc.	Combination tumor immunotherapy
US11319359B2 (en)	2015-04-17	2022-05-03	Alpine Immune Sciences, Inc.	Immunomodulatory proteins with tunable affinities
UA126278C2 (uk)	2015-09-21	2022-09-14	Аптево Рісьорч Енд Девелопмент Ллс	Поліпептиди, які зв'язують cd3
EP3192805A1 (en)	2016-01-15	2017-07-19	Humanitas Mirasole S.p.A.	Inhibitors of t cell activation or stimulation and uses thereof
SG11201907867TA (en)	2017-02-28	2019-09-27	Bristol Myers Squibb Co	Use of anti-ctla-4 antibodies with enhanced adcc to enhance immune response to a vaccine
WO2018187227A1 (en)	2017-04-03	2018-10-11	Concologie, Inc.	Methods for treating cancer using ps-targeting antibodies with immuno-oncology agents
US11761963B2 (en)	2017-09-27	2023-09-19	Alexion Pharmaceuticals, Inc.	Biomarker signature for predicting tumor response to anti-CD200 therapy
KR102813968B1 (ko)	2017-10-10	2025-05-29	알파인 이뮨 사이언시즈, 인코포레이티드	Ctla-4 변이체 면역조절 단백질 및 이의 용도
CA3087149A1 (en)	2018-01-03	2019-07-11	Alpine Immune Sciences, Inc.	Multi-domain immunomodulatory proteins and methods of use thereof
WO2019160866A2 (en)	2018-02-13	2019-08-22	Checkmate Pharmaceuticals, Inc.	Compositions and methods for tumor immunotherapy
EP3775218A1 (en)	2018-04-09	2021-02-17	Checkmate Pharmaceuticals	Packaging oligonucleotides into virus-like particles
EP3617230A1 (en)	2018-09-03	2020-03-04	BioInvent International AB	Novel antibodies and nucleotide sequences, and uses thereof
AU2019387218A1 (en)	2018-11-26	2021-06-03	Massachusetts Institute Of Technology	Compositions and methods for immune tolerance
CN114981659A (zh)	2019-11-21	2022-08-30	百时美施贵宝公司	无标记n-聚糖定量方法
AU2022223409A1 (en)	2021-02-19	2023-09-21	Theripion, Inc.	Dnase fusion polypeptides and related compositions and methods
GB202115803D0 (en)	2021-11-03	2021-12-15	Ducentis Biotherapeutics Ltd	Novel proteins
AU2023265174A1 (en)	2022-05-06	2024-12-12	Ducentis Biotherapeutics Limited	Novel cd200 fusion proteins
CN119365483A (zh)	2022-05-06	2025-01-24	杜森蒂斯生物治疗有限公司	新型cd200融合蛋白
CN114686427B (zh) *	2022-05-23	2022-07-29	中国人民解放军总医院第一医学中心	一种脾脏调节型b淋巴细胞及其制备方法与应用
GB202306711D0 (en)	2023-05-05	2023-06-21	Ducentis Biotherapeutics Ltd	Novel proteins
WO2024259220A1 (en)	2023-06-15	2024-12-19	Theripion, Inc.	Pon3 and evolved pon1 fusion polypeptides

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US4399216A (en) *	1980-02-25	1983-08-16	The Trustees Of Columbia University	Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials
US4683202A (en) *	1985-03-28	1987-07-28	Cetus Corporation	Process for amplifying nucleic acid sequences
US4683195A (en) *	1986-01-30	1987-07-28	Cetus Corporation	Process for amplifying, detecting, and/or-cloning nucleic acid sequences

1992
- 1992-06-16 DE DE122007000078C patent/DE122007000078I2/de active Active
- 1992-06-16 CA CA002110518A patent/CA2110518C/en not_active Expired - Lifetime
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1993
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2001
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2003
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2004
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2007
- 2007-11-02 NL NL300303C patent/NL300303I1/nl unknown
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Also Published As

Publication number	Publication date
ATE170562T1 (de)	1998-09-15
NO2012001I2 (no)	2016-02-29
LU91375I2 (fr)	2008-01-07
ES2123001T3 (es)	1999-01-01
KR100238712B1 (ko)	2000-01-15
PT100637A (pt)	1994-05-31
MX9203605A (es)	1993-11-01
DE69226871T2 (de)	1999-05-12
KR940701445A (ko)	1994-05-28
IL159364A (en)	2005-08-31
DE122007000078I2 (de)	2011-01-13
DK0606217T4 (da)	2009-03-30
NL300303I2 (nl)	2008-01-02
JP2002017349A (ja)	2002-01-22
DK0606217T3 (da)	1998-11-09
FI115057B (fi)	2005-02-28
FI935795A0 (fi)	1993-12-22
IL162430A0 (en)	2005-11-20
FI935795L (fi)	1993-12-22
DE69226871T3 (de)	2009-09-24
JP2003012546A (ja)	2003-01-15
NO20020491D0 (no)	2002-01-30
JP2003096097A (ja)	2003-04-03
JP2002003399A (ja)	2002-01-09
IL102294A0 (en)	1993-01-14
EP0606217A1 (en)	1994-07-20
NO2007013I1 (no)	2007-11-26
DE69226871D1 (de)	1998-10-08
IL159364A0 (en)	2004-06-01
NO20020491L (no)	1994-02-21
NZ264712A (en)	1996-03-26
EP0606217B2 (en)	2008-12-03
NO934801L (no)	1994-02-21
US5434131A (en)	1995-07-18
JPH06508989A (ja)	1994-10-13
AU2240092A (en)	1993-01-25
ZA924782B (en)	1993-12-27
FI112082B (fi)	2003-10-31
JP3722375B2 (ja)	2005-11-30
CA2110518C (en)	2007-05-22
NO934801D0 (no)	1993-12-23
NO318806B1 (no)	2005-05-09
IE20010097A1 (en)	2002-03-20
PT100637B (pt)	1999-06-30
NZ243286A (en)	1996-03-26
NL300303I1 (nl)	2008-01-02
ES2123001T5 (es)	2009-04-16
WO1993000431A1 (en)	1993-01-07
NO2012001I1 (no)	2012-01-09
DE122007000078I1 (de)	2008-02-14
NO2007013I2 (no)	2011-02-21
AU661854B2 (en)	1995-08-10
JP2003174872A (ja)	2003-06-24
CA2110518A1 (en)	1993-01-07
JP4159266B2 (ja)	2008-10-01
CA2580812A1 (en)	1993-01-07
NO312465B1 (no)	2002-05-13
EP0606217B1 (en)	1998-09-02
FI20022285L (fi)	2002-12-30
IE922111A1 (en)	1992-12-30

Publication	Publication Date	Title
EP0606217B1 (en)	1998-09-02	Ctl4a receptor, fusion proteins containing it and uses thereof
CA2113744C (en)	2008-12-30	Methods for regulating the immune response using ctla4-binding molecules and il4-binding molecules
US6090914A (en)	2000-07-18	CTLA4/CD28Ig hybrid fusion proteins and uses thereof
US5844095A (en)	1998-12-01	CTLA4 Ig fusion proteins
US5885796A (en)	1999-03-23	CTLA4 receptor and uses thereof
US7572772B2 (en)	2009-08-11	Soluble CTLA4 mutant molecules
MXPA95001794A (en)	1999-05-31	Ctla4 molecules and il-4 link molecules and uses of mis

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2005-02-20	FF	Patent granted
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2010-11-30	KB	Patent renewed
2013-02-03	EXP	Patent expired