Patents Assigned to Arizona Biomedical Research Commission
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Patent number: 8552066Abstract: Antimitotic agents comprising a modified chalcone or modified chalcone derivative are disclosed. The modified chalcone or modified chalcone derivative compounds are of the general formula CHAL-LIN-COV, wherein CHAL is a chalcone or chalcone derivative portion, LIN is an optional linker portion, and COV is a covalent bonding portion (e.g., an ?,?-unsaturated thiol ester group). The modified chalcone or modified chalcone derivative compounds provide an improved method of interference with tubulin polymerization, for example by covalent (and essentially irreversible) bonding between tubulin and the covalent bonding portion, potentially resulting in a decrease in tumor size and/or disappearance of the cancer, to the benefit of cancer patients.Type: GrantFiled: May 10, 2010Date of Patent: October 8, 2013Assignee: Arizona Biomedical Research CommissionInventors: Seth D. Rose, Rosemarie F. Hartman
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Publication number: 20130251727Abstract: Observations regarding the role of MUC1 in promoting the nuclear accumulation of EGFR led us to propose the development of peptides to block nuclear accumulation of EGFR as a means to block breast cancer progression. One exemplary peptide, the ENLS1 peptide, promotes cell death in breast cancer cell lines. Studies in the MMTV-pyMT mouse model of breast cancer demonstrate significant anti-tumor activity.Type: ApplicationFiled: October 12, 2011Publication date: September 26, 2013Applicant: ARIZONA BIOMEDICAL RESEARCH COMMISSIONInventors: Joyce A. Schroeder, Benjamin G. Bitler, Aarthi Goverdhan
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Patent number: 8178649Abstract: The present invention provides novel immuno-stimulatory polypeptides, and methods for their use and identification.Type: GrantFiled: December 6, 2005Date of Patent: May 15, 2012Assignee: Arizona Biomedical Research CommissionInventors: Laura Eggink, Valerie Jacobs, Srilakshmi Bysani, Kenneth J. Hoober
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Publication number: 20120108521Abstract: The present invention provides novel immune-stimulatory polypeptides, and methods for their use and identification.Type: ApplicationFiled: October 10, 2011Publication date: May 3, 2012Applicant: ARIZONA BIOMEDICAL RESEARCH COMMISSIONInventors: LAURA L. EGGINK, VALERIE JACOBS, KENNETH HOOBER
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Patent number: 8093208Abstract: Interaction between MUC1 and ?-catenin can be interrupted using polypeptides or antibodies that specifically bind to the binding site on MUC1. Interruption provides the beneficial effect of inhibiting, reducing, and/or retarding invasiveness and metastasis. Fusion polypeptides and antibodies are provided to achieve a therapeutic effect.Type: GrantFiled: July 30, 2010Date of Patent: January 10, 2012Assignee: Arizona Biomedical Research CommissionInventor: Joyce A. Schroeder
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Patent number: 8034773Abstract: The present invention provides novel immuno-stimulatory polypeptides, and methods for their use and identification.Type: GrantFiled: February 4, 2005Date of Patent: October 11, 2011Assignee: Arizona Biomedical Research CommissionInventors: Laura L. Eggink, Valerie Jacobs, Kenneth Hoober
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Patent number: 7977315Abstract: Conjugated nitro alkene compounds hamper or prevent proliferation of cancer cells in cell culture and in cancer patients, which can result in a decrease in tumor size and/or disappearance of the cancer. The compounds may act by interference with cancer cell biochemistry, in which isoprenoid groups such as farnesyl and geranylgeranyl become bonded to various oncogenic proteins such as Ras, RhoA, RhoB, or some other growth-related cellular protein(s).Type: GrantFiled: November 16, 2007Date of Patent: July 12, 2011Assignee: Arizona Biomedical Research CommissionInventors: Seth D. Rose, Karl J. Okolotowicz, Rosemarie F. Hartman, Jason Houtchens
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Patent number: 7943665Abstract: Oncoproteins such as Ras and RhoB are known to induce cell division in an unrestrained manner when such proteins are localized at the inner surface of a cancer cell membrane. The localization is effected by the prenylation reaction, whereby a hydrophobic group (e.g. a farnesyl group) is attached to the protein in the presence of an enzyme (e.g. farnesyl protein transferase). Deactivation of the prenylation enzyme through covalent modification can therefore ultimately result in the mitigation and/or cessation of cancer cell growth. Various prenylation inhibitors having the necessary structural groups to bond covalently, or essentially irreversibly, to the prenylation enzyme include carbonyl or thiocarbonyl compounds (or masked versions of these compounds) and alpha oxo-epoxides bonded to a hydrophobic, substrate-mimicking group. The carbonyl or thiocarbonyl compounds also contain a nucleofugal atom or group to enhance the tendency to form covalent bonds.Type: GrantFiled: September 4, 2008Date of Patent: May 17, 2011Assignee: Arizona Biomedical Research CommissionInventors: Seth D. Rose, Scott R. Lefler, Steven R. Ottersberg, Ann Y. Kim, Karl J. Okolotowicz, Rosemarie F. Hartman
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Publication number: 20110014195Abstract: MUC1 (DF3, CD227, episialin, PEM) is a heavily O-glycosylated heterodimeric protein of >300 kDa, normally expressed abundantly on the apical surface of glandular epithelia. MUC1 mimetic peptides are selectively retained in mammary gland tumors, colon and skin after systemic administration. Moreover, MUC1 mimetic peptides reduce tumor initiation. In addition, MUC1 mimetic peptides can be used in conjunction with other anti-EGFR treatments in the adjuvant context, i.e., after surgery.Type: ApplicationFiled: February 19, 2009Publication date: January 20, 2011Applicant: ARIZONA BIOMEDICAL RESEARCH COMMISSIONInventor: Joyce A. Schroeder
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Publication number: 20100291096Abstract: Interaction between MUC1 and ?-catenin can be interrupted using polypeptides or antibodies that specifically bind to the binding site on MUC1. Interruption provides the beneficial effect of inhibiting, reducing, and/or retarding invasiveness and metastasis. Fusion polypeptides and antibodies are provided to achieve a therapeutic effect.Type: ApplicationFiled: July 30, 2010Publication date: November 18, 2010Applicant: ARIZONA BIOMEDICAL RESEARCH COMMISSIONInventor: Joyce A. Schroeder
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Publication number: 20100222380Abstract: Antimitotic agents comprising a modified chalcone or modified chalcone derivative are disclosed. The modified chalcone or modified chalcone derivative compounds are of the general formula CHAL-LIN-COV, wherein CHAL is a chalcone or chalcone derivative portion, LIN is an optional linker portion, and COV is a covalent bonding portion (e.g., an ?,?-unsaturated thiol ester group). The modified chalcone or modified chalcone derivative compounds provide an improved method of interference with tubulin polymerization, for example by covalent (and essentially irreversible) bonding between tubulin and the covalent bonding portion, potentially resulting in a decrease in tumor size and/or disappearance of the cancer, to the benefit of cancer patients.Type: ApplicationFiled: May 10, 2010Publication date: September 2, 2010Applicant: ARIZONA BIOMEDICAL RESEARCH COMMISSIONInventors: Seth D. Rose, Rosemarie F. Hartman
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Patent number: 7767642Abstract: Interaction between MUC1 and ?-catenin can be interrupted using polypeptides or antibodies that specifically bind to the binding site on MUC1. Interruption provides the beneficial effect of inhibiting, reducing, and/or retarding invasiveness and metastasis. Fusion polypeptides and antibodies are provided to achieve a therapeutic effect.Type: GrantFiled: April 17, 2006Date of Patent: August 3, 2010Assignee: Arizona Biomedical Research CommissionInventor: Joyce A. Schroeder
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Patent number: 7714025Abstract: Antimitotic agents comprising a modified chalcone or modified chalcone derivative are disclosed. The modified chalcone or modified chalcone derivative compounds are of the general formula CHAL-LIN—COV, wherein CHAL is a chalcone or chalcone derivative portion, LIN is an optional linker portion, and COV is a covalent bonding portion (e.g., an ?,?-unsaturated thiol ester group). The modified chalcone or modified chalcone derivative compounds provide an improved method of interference with tubulin polymerization, for example by covalent (and essentially irreversible) bonding between tubulin and the covalent bonding portion, potentially resulting in a decrease in tumor size and/or disappearance of the cancer, to the benefit of cancer patients.Type: GrantFiled: May 3, 2007Date of Patent: May 11, 2010Assignee: Arizona Biomedical Research CommissionInventors: Seth D. Rose, Rosemarie F. Hartman
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Patent number: 7423170Abstract: Oncoproteins such as Ras and RhoB are known to induce cell division in an unrestrained manner when such proteins are localized at the inner surface of a cancer cell membrane. The localization is effected by the prenylation reaction, whereby a hydrophobic group (e.g. a farnesyl group) is attached to the protein in the presence of an enzyme (e.g. farnesyl protein transferase). Deactivation of the prenylation enzyme through covalent modification can therefore ultimately result in the mitigation and/or cessation of cancer cell growth. Various prenylation inhibitors having the necessary structural groups to bond covalently, or essentially irreversibly, to the prenylation enzyme include carbonyl or thiocarbonyl compounds (or masked versions of these compounds) and alpha oxo-epoxides bonded to a hydrophobic, substrate-mimicking group. The carbonyl or thiocarbonyl compounds also contain a nucleofugal atom or group to enhance the tendency to form covalent bonds.Type: GrantFiled: January 23, 2006Date of Patent: September 9, 2008Assignee: Arizona Biomedical Research CommissionInventors: Seth D. Rose, Scott R. Lefler, Steven R. Ottersberg, Ann Y. Kim, Karl J. Okolotowicz, Rosemarie F. Hartman
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Publication number: 20080113919Abstract: Conjugated nitro alkene compounds hamper or prevent proliferation of cancer cells in cell culture and in cancer patients, which can result in a decrease in tumor size and/or disappearance of the cancer. The compounds may act by interference with cancer cell biochemistry, in which isoprenoid groups such as farnesyl and geranylgeranyl become bonded to various oncogenic proteins such as Ras, RhoA, RhoB, or some other growth-related cellular protein(s).Type: ApplicationFiled: November 16, 2007Publication date: May 15, 2008Applicant: ARIZONA BIOMEDICAL RESEARCH COMMISSIONInventors: Seth D. ROSE, Karl J. OKOLOTOWICZ, Rosemarie F. HARTMAN, Jason HOUTCHENS
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Patent number: 7344851Abstract: Prenylating enzymes are involved in modifying oncoproteins, such as RAS, so that growth of neoplastic cells becomes uncontrolled. Inactivation of such enzymes can prevent uncontrolled growth. ?-Dicarbonyl compounds can be used to covalently modify and thereby inactivate prenylating enzymes such as protein farnesyltransferase and protein geranylgeranyltransferase. The compounds can be designed to enhance affinity and/or specificity for a particular protein substrate.Type: GrantFiled: October 11, 2005Date of Patent: March 18, 2008Assignee: Arizona Biomedical Research CommissionInventors: Seth D. Rose, Steven R. Ottersberg, Karl J. Okolotowicz, Dale E. Robinson, Rosemarie F. Hartman, Scott Lefler
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Patent number: 7312191Abstract: Conjugated nitro alkene compounds hamper or prevent proliferation of cancer cells in cell culture and in cancer patients, which can result in a decrease in tumor size and/or disappearance of the cancer. The compounds may act by interference with cancer cell biochemistry, in which isoprenoid groups such as farnesyl and geranylgeranyl become bonded to various oncogenic proteins such as Ras, RhoA, RhoB, or some other growth-related cellular protein(s).Type: GrantFiled: July 29, 2004Date of Patent: December 25, 2007Assignee: Arizona Biomedical Research CommissionInventors: Seth D. Rose, Karl J. Okolotowicz, Rosemarie F. Hartman, Jason Houtchens
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Publication number: 20070265317Abstract: Antimitotic agents comprising a modified chalcone or modified chalcone derivative are disclosed. The modified chalcone or modified chalcone derivative compounds are of the general formula CHAL-LIN—COV, wherein CHAL is a chalcone or chalcone derivative portion, LIN is an optional linker portion, and COV is a covalent bonding portion (e.g., an ?,?-unsaturated thiol ester group). The modified chalcone or modified chalcone derivative compounds provide an improved method of interference with tubulin polymerization, for example by covalent (and essentially irreversible) bonding between tubulin and the covalent bonding portion, potentially resulting in a decrease in tumor size and/or disappearance of the cancer, to the benefit of cancer patients.Type: ApplicationFiled: May 3, 2007Publication date: November 15, 2007Applicant: ARIZONA BIOMEDICAL RESEARCH COMMISSIONInventors: Seth D. ROSE, Rosemarie F. HARTMAN
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Publication number: 20060111329Abstract: Oncoproteins such as Ras and RhoB are known to induce cell division in an unrestrained manner when such proteins are localized at the inner surface of a cancer cell membrane. The localization is effected by the prenylation reaction, whereby a hydrophobic group (e.g. a farnesyl group) is attached to the protein in the presence of an enzyme (e.g. farnesyl protein transferase). Deactivation of the prenylation enzyme through covalent modification can therefore ultimately result in the mitigation and/or cessation of cancer cell growth. Various prenylation inhibitors having the necessary structural groups to bond covalently, or essentially irreversibly, to the prenylation enzyme include carbonyl or thiocarbonyl compounds (or masked versions of these compounds) and alpha oxo-epoxides bonded to a hydrophobic, substrate-mimicking group. The carbonyl or thiocarbonyl compounds also contain a nucleofugal atom or group to enhance the tendency to form covalent bonds.Type: ApplicationFiled: January 23, 2006Publication date: May 25, 2006Applicant: ARIZONA BIOMEDICAL RESEARCH COMMISSIONInventors: Seth Rose, Scott Lefler, Steven Ottersberg, Ann Kim, Karl Okolotowicz, Rosemarie Hartman