The protein ras is an important part of signaling cells to proliferate and differentiate however, it has also been linked to a few types of human cancers. Such cancers occur when ras has been activated for normal activity but it does not naturally deactivate. Ras is activated through the post-translational modification by protein farnesyltransferase. Protein farnesyltransferase activates ras via prenylation with the tri-isoprenoid called farnesyl diphosphate. It was from the farnesyl diphosphate compound that a non-natural substrate was modeled. The mimicking substrate contained a single isoprenoid group with norbornene attached. This non-natural substrate was synthesized with the potential to be prenylated onto ras via protein farnesyltran...
Protein farnesylation is a lipid posttranslational modification required for the cancer-causing acti...
A study was performed on the structure-activity relationships of a series of phenol derivs., CVFM an...
Prenylation is a post-translational, covalent modification of a protein by the attachment of a lipop...
The protein ras is an important part of signaling cells to proliferate and differentiate however, it...
Mutant RAS proteins are associated with 30% of all human cancers. Unregulated cell growth caused by ...
Mutant RAS proteins have been linked to over 30 of all human cancers. It has been shown that mutant...
Protein farnesylation is an essential post-translational modification required for the function of n...
Prenylated proteins play key roles in several human diseases including cancer, atherosclerosis and A...
Over the last decades, knowledge on the genetic defects involved in tumor formation and growth has i...
This research was supported by the Undergraduate Research Opportunities Program (UROP)
Farnesylation is the post-translational lipid modification that results in a C15 farnesyl isoprenoid...
AbstractProteins that transmit abnormal growth signals offer enticing points of intervention for the...
Lipopeptides carrying a farnesyl thioether or a palmitic acid thioester and a farnesyl thioether wer...
Ras proteins are plasma membrane\u2013bound GTP-binding proteins which play an important role in nor...
Additional contributors: Mohammad Rashidian; Dr. Mark Distefano (faculty mentor)Protein farnesylatio...
Protein farnesylation is a lipid posttranslational modification required for the cancer-causing acti...
A study was performed on the structure-activity relationships of a series of phenol derivs., CVFM an...
Prenylation is a post-translational, covalent modification of a protein by the attachment of a lipop...
The protein ras is an important part of signaling cells to proliferate and differentiate however, it...
Mutant RAS proteins are associated with 30% of all human cancers. Unregulated cell growth caused by ...
Mutant RAS proteins have been linked to over 30 of all human cancers. It has been shown that mutant...
Protein farnesylation is an essential post-translational modification required for the function of n...
Prenylated proteins play key roles in several human diseases including cancer, atherosclerosis and A...
Over the last decades, knowledge on the genetic defects involved in tumor formation and growth has i...
This research was supported by the Undergraduate Research Opportunities Program (UROP)
Farnesylation is the post-translational lipid modification that results in a C15 farnesyl isoprenoid...
AbstractProteins that transmit abnormal growth signals offer enticing points of intervention for the...
Lipopeptides carrying a farnesyl thioether or a palmitic acid thioester and a farnesyl thioether wer...
Ras proteins are plasma membrane\u2013bound GTP-binding proteins which play an important role in nor...
Additional contributors: Mohammad Rashidian; Dr. Mark Distefano (faculty mentor)Protein farnesylatio...
Protein farnesylation is a lipid posttranslational modification required for the cancer-causing acti...
A study was performed on the structure-activity relationships of a series of phenol derivs., CVFM an...
Prenylation is a post-translational, covalent modification of a protein by the attachment of a lipop...