Patents Assigned to Oklahoma Medical Research Foundation
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Patent number: 6008018Abstract: ELL2 polypeptides and polynucleotides and methods for producing such polypeptides by recombinant techniques are disclosed. Also disclosed are methods for utilizing ELL2 polypeptides and polynucleotides in the design of protocols for the treatment of neoplastic disorders, among others and diagnostic assays for such conditions.Type: GrantFiled: February 19, 1998Date of Patent: December 28, 1999Assignees: Human Genome Sciences, Inc., Oklahoma Medical Research FoundationInventors: D. Roxanne Duan, Ali Shilatifard, Joan W. Conaway, Ronald C. Conway
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Patent number: 6002001Abstract: Spin trapping compositions in general have now been discovered to be effective in treating a variety of disorders, including disorders such as those arising from ischemia, infection, inflammation, exposure to radiation or cytotoxic compounds, not just of the central and peripheral nervous systems but of peripheral organ disease having a wide variety of etiologies. In the preferred embodiment, the compositions for treating tissue damage from ischemia contain PBN, or active derivatives thereof, in a suitable pharmaceutical carrier for intravenous, oral, topical, or nasal/pulmonary administration. Other preferred spin-trapping agents include 5,5-dimethyl pyrroline N-oxide, (DMPO), .alpha.-(4-pyridyl-1-oxide)-N-tert-butylnitrone, (POBN), and (TEMPO) spin-trapping derivatives thereof. Examples of derivatives of PBN include halogenated derivatives, bifunctional derivatives, conjugates with drugs or targeting molecules, dimers and cyclodextran polymers of PBN.Type: GrantFiled: November 28, 1997Date of Patent: December 14, 1999Assignees: Oklahoma Medical Research Foundation, University of Kentucky Research FoundationInventors: John M. Carney, Robert A. Floyd
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Patent number: 5998473Abstract: The present invention is directed to compositions comprising N-L-alpha-aspartyl-L-phenylalanine and esters thereof as well as to method of treating pain which comprises administering such a composition to a patient in need thereof.Type: GrantFiled: December 22, 1997Date of Patent: December 7, 1999Assignee: Oklahoma Medical Research FoundationInventors: Allen B. Edmundson, Carl V. Manion
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Patent number: 5955441Abstract: A method and means for protecting cells and transplanted organs from the effects of activated complement proteins generated in blood serum or plasma by introducing the gene for CD59 into the cells to be protected is described. In an example of the method, protection against the pore-forming activity of the human C5b-9 proteins was conferred on CHO cells by transfection with cDNA encoding the human complement regulatory protein CD59.Type: GrantFiled: August 13, 1996Date of Patent: September 21, 1999Assignees: Oklahoma Medical Research Foundation, Yale UniversityInventors: Peter J. Sims, Alfred L.M. Bothwell
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Patent number: 5922852Abstract: The 3' untranslated region of the human prohibitin gene has been isolated for use in a cancer susceptibility screen and as a therapeutic agent for the treatment of cancer.Type: GrantFiled: June 7, 1995Date of Patent: July 13, 1999Assignee: Oklahoma Medical Research FoundationInventors: Robert Thomas Dell'Orco, Sr., J. Keith MClung, Eldon Jupe, Xiao-Tie Liu, Robert King
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Patent number: 5900227Abstract: Multicyclic nitrone spin trapping compounds capable of forming stable free radical spin adducts are provided as well as methods for their synthesis. The multicyclic nitrone spin trapping compounds can be reacted with a free radical, such as a hydroxy or hydroperoxy radical, in solution to form a spin adduct which is stable and readily detectable by electron paramagnetic resonance (EPR) spectroscopy. The multicyclic nitrone spin traps can be used to detect free radicals in a sample such as a biological system. In one embodiment, the spin trapping compound, 1,3,3-trimethyl-6-azabicyclo-?3.2.1!oct-6-ene-N-oxide ("TRAZON") is provided, as well as methods for the synthesis of TRAZON and of modified forms of TRAZON. TRAZON can react with a wide range of different free radicals in solution to form free radical spin adducts which are readily detectable by EPR.Type: GrantFiled: June 17, 1996Date of Patent: May 4, 1999Assignee: Oklahoma Medical Research FoundationInventors: Edward G. Janzen, Nagaraju Sankuratri
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Patent number: 5852171Abstract: Human protein C and activated protein C were shown to bind to endothelium specifically, selectively and saturably (Kd=30 nM, 7000 sites per cell) in a Ca.sup.2+ dependent fashion. Expression cloning revealed a 1.3 kb CDNA that coded for a novel type I transmembrane glycoprotein capable of binding protein C. This protein appears to be a member of the CD1/MHC superfamily. Like thrombomodulin, the receptor involved in protein C activation, the endothelial cell protein C receptor (EPCR) function and message are both down regulated by exposure of endothelium to TNF. Identification of EPCR as a member of the CD1/MHC superfamily provides insights into the role of protein C in regulating the inflammatory response, and determination of methods for pharmaceutical use in manipulating the inflammatory response.Type: GrantFiled: June 18, 1997Date of Patent: December 22, 1998Assignee: Oklahoma Medical Research FoundationInventors: Kenji Fukudome, Charles T. Esmon
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Patent number: 5847085Abstract: Modified Protein C molecules have been made which substitute the gamma carboxylglutamic acid (Gla) region of another Vitamin K dependent protein, most preferably prothrombin, for the native region of the Protein C. A modified protein C molecules has been made which substitutes the gamma carboxyglutamic acid (Gla) region with the corresponding region of prothrombin. The modified or chimeric protein C has advantages over the wild-type protein C since it is less sensitive to inhibition by some natural antibody inhibitors of protein C (which would otherwise decrease the ability of the protein C to act as an anticoagulant) and which do not need the same cofactors or same amounts of cofactors, and can therefore be effective in patients with lowered levels of the cofactors such as protein S or the lipids present in elevated levels in platelets such as phosphatidyl ethanolamine (PE). The anticoagulant activity of the chimera was tested in normal and factor V Leiden plasma.Type: GrantFiled: November 7, 1997Date of Patent: December 8, 1998Assignee: Oklahoma Medical Research FoundationInventors: Charles T. Esmon, Mikhail D. Smirnov
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Patent number: 5843884Abstract: Pharmaceutical compositions are designed based on the criticality of a portion of C9 for assembly of the C5b9 complex, which specifically modulate binding of CD59 to C9, either molecules structurally mimicking C9 amino acid residues 359 to 384 which bind to CD59 or molecules binding to C9 amino acid residues 359 to 384. Molecules which inhibit CD59 binding include peptides containing residues 359-384 which compete for binding with the other components of the C5b9 complex and anti-idiotypic antibodies immunoreactive with C9 amino acid residues 359 to 384. Molecules which prevent assembly of the C5b-9 complex include antibodies and antibody fragments immunoreactive with amino acid residues 359 to 384 of C9, peptides that bind to amino acid residues 359 to 384 of C9, and nucleotide molecules that bind to amino acid residues 359 to 384 of C9.Type: GrantFiled: November 15, 1995Date of Patent: December 1, 1998Assignee: Oklahoma Medical Research FoundationInventor: Peter J. Sims
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Patent number: 5837843Abstract: Modified Protein C molecules have been made which substitute the gamma carboxylglutamic acid (Gla) region of another Vitamin K dependent protein, most preferably prothrombin, for the native region of the Protein C. The modified or chimeric protein C has advantages over the wild-type protein C since it is less sensitive to inhibition by natural inhibitors of protein C (which would otherwise decrease the ability of the protein C to act as an anticoagulant) and which does not need the same cofactors or same amounts of cofactors, and can therefore be effective in patients with lowered levels of the cofactors such as protein S or the lipids present in activated platelets such as phosphatidyl ethanolamine (PE).Type: GrantFiled: November 8, 1996Date of Patent: November 17, 1998Assignee: Oklahoma Medical Research FoundationInventors: Mikhail D. Smirnov, Charles T. Esmon
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Patent number: 5821226Abstract: Drug delivery conjugates of including a BAL C-tail peptide including all or a portion of the carboxy terminal region of human bile salt-activated lipase (BAL) conjugated to a biologically active substance are described. The C-tail peptide-drug conjugates, when orally ingested, compete with native BAL in binding to the intestinal surface, and, as a result, permit drug compositions to be delivered specifically to the intestine. Useful C-tail peptides are derivatives of the carboxy terminal region of BAL derived from all or portion of the region containing amino acid residues 539 to 722, and have a mucin-like structure containing at least three of the repeating proline-rich units of eleven amino acid residues each.Type: GrantFiled: June 7, 1995Date of Patent: October 13, 1998Assignee: Oklahoma Medical Research FoundationInventors: Jordan J. N. Tang, Chi-Sun Wang
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Patent number: 5804392Abstract: Plasma EPCR has been isolated, characterized and shown to block cellular protein C activation and APC anticoagulant activity. Plasma EPCR appears to be about 43,000 daltons and circulates at approximately 100 ng/ml (98.4.+-.27.8 ng/ml, n=22). Plasma EPCR bound activated protein C with an affinity similar to that of recombinant soluble EPCR (Kd.sub.app approximately 30 nM), and inhibits both protein C activation on an endothelial cell line and APC anticoagulant activity in a one-stage factor Xa clotting assay. Soluble plasma EPCR appears to attenuate the membrane-bound EPCR augmentation of protein C activation and the anticoagulant function of activated protein C. Soluble EPCR has also been detected in urine. Levels of soluble EPCR can rise in inflammatory disease associated with vascular injury and appear to be correlated with inflammation and disease states associated with abnormal coagulation.Type: GrantFiled: June 27, 1997Date of Patent: September 8, 1998Assignee: Oklahoma Medical Research FoundationInventors: Charles T. Esmon, Deborah J. Stearns-Kurosawa, Shinichiro Kurosawa
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Patent number: 5800814Abstract: Human procathepsin D was demonstrated to be mitogenic for breast cancer cells but not normal cells. The activation peptide of the procathepsin D appears to be responsible, since inhibition of enhancement of proliferation of breast cancer cells can be obtained by inhibition of the activation peptide through the use of an agent such as an antibody immunoreactive with the activation peptide.Type: GrantFiled: April 22, 1994Date of Patent: September 1, 1998Assignee: Oklahoma Medical Research FoundationInventors: Martin Fusek, Vaclav Vetvicka
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Patent number: 5792634Abstract: A new RNA polymerase transcription factor has been discovered. The enzyme significantly increases the rate of transcription elongation by RNA polymerase II.Type: GrantFiled: September 7, 1995Date of Patent: August 11, 1998Assignee: Oklahoma Medical Research FoundationInventors: Ronald Charles Conaway, Joan Weliky Conaway, John N. Bradsher
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Patent number: 5780510Abstract: 2,4-disulfonyl .alpha.-phenyl-tert-butyl nitrone and its pharmaceutically acceptable salts are disclosed. These materials are useful as pharmaceutical agents for oral or parenteral, e.g. intravenous administration to patients suffering from acute central nervous system oxidation as occurs in a stroke or from gradual central nervous system oxidation which can exhibit itself as progressive central nervous system function loss. The materials are also used to ameliorate the side effects of oxidative-damage causing antineoplastic disease treatments.Type: GrantFiled: June 19, 1997Date of Patent: July 14, 1998Assignees: Oklahoma Medical Research Foundation, University of Kentucky Research FoundationInventor: John M. Carney
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Patent number: 5776738Abstract: The 3' untranslated region of the human prohibitin gene has been isolated for use in a cancer susceptibility screen and as a therapeutic agent for the treatment of cancer.Type: GrantFiled: October 8, 1996Date of Patent: July 7, 1998Assignee: Oklahoma Medical Research FoundationInventors: Robert Thomas Dell'Orco, Sr., J. Keith MClung, Eldon Jupe, Xiao-Tie Liu, Robert King
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Patent number: 5766841Abstract: A kit for visually detecting the presence of a virus in a direct clinical specimen is provided. The kit employs a rapid and direct assay for visually detecting a virus having a characteristic enzyme in a direct clinical sample without the need for any culturing step, This assay contains the following steps: (1) the clinical sample is contacted in solution with a substrate for the enzyme which includes a chromogen that is cleaved from the substrate by the enzyme and a precipitating agent which reacts with the liberated chromogen to form a precipitate, (2) the precipitate is concentrated, and (3) the concentrated precipitate is visually observed for the characteristic color of the chromogen. The observance of the characteristic color confirms the presence of the virus in the clinical specimen.Type: GrantFiled: June 7, 1995Date of Patent: June 16, 1998Assignee: Oklahoma Medical Research FoundationInventors: Avraham Liav, Craig D. Shimasaki, James F. Maher, C. Worth Clinkscales, Michael D. Roark
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Patent number: 5750358Abstract: An assay for activated factor VII (factor VIIa) has been developed using truncated tissue factor (tTF), a soluble mutant form of tissue factor (TF) that retains the cofactor function of TF toward factor VIIa. Unlike full-length TF, however, tTF appears not to support the conversion of factor VII to VIIa. As a result, the tTF assay for factor VIIa is free from interference from factor VII in the plasma and is therefore specific for factor VIIa. The assay is much simpler than existing assays, because it is a single-stage clotting assay performed almost identically to a prothrombin time (PT) assay. It is also considerably more sensitive than current assays for factor VIIa in plasma. Since the tTF assay is calibrated against a factor VIIa standard, it yields an absolute concentration of factor VIIa in ng/ml.Type: GrantFiled: June 5, 1995Date of Patent: May 12, 1998Assignee: Oklahoma Medical Research FoundationInventor: James H. Morrissey
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Patent number: 5741658Abstract: An kit for an assay for measuring activated factor VII (factor VIIa) is disclosed which employs a reagent comprising truncated tissue factor (tTF), a soluble mutant form of tissue factor (TF) that retains the cofactor function of TF toward factor VIIa, but does not support the conversion of factor VII to VIIa. As a result, the tTF assay for factor VIIa is free from interference from factor VII in the plasma and is therefore specific for factor VIIa. The assay is much simpler than existing assays, because it is a single-stage clotting assay performed almost identically to a prothrombin time (PT) assay. It is also considerably more sensitive than current assays for factor VIIa in plasma. Since the tTF assay is calibrated against a factor VIIa standard, it yields an absolute concentration of factor VIIa in ng/ml.Type: GrantFiled: June 5, 1995Date of Patent: April 21, 1998Assignee: Oklahoma Medical Research FoundationInventor: James H. Morrissey
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Patent number: RE36594Abstract: The invention is the use of nitronyl substituted hindered phenols as antioxidants in therapeutic applications. In the preferred embodiment the compositions have the general formula: ##STR1## Wherein R1 is hydrogen, an alkyl or an aryl and R2 is an alkyl or an aryl; R.sub.3 is an alkyl; and R.sub.4 is an alkyl. Further, the invention relates to novel compositions useful as antioxidants. The novel compounds include: 2,6-di-tert-butyl-4-(N-tert-octyl)nitronyl phenol (DBONP); 2,6-dimethyl-4-(N-tert-octyl)nitronyl phenol (DMONP); N-tert-octyl-C-phenyl nitrone (OPN).Type: GrantFiled: October 2, 1997Date of Patent: February 29, 2000Assignee: Oklahoma Medical Research FoundationInventors: Edward G. Janzen, Allan L. Wilcox