Oklahoma Medical Research Foundation

Other

Human Genome Sciences, Inc.

Joan W Conaway

Ronald C Conaway

D Roxanne Duan

Ali Shilatifard

Takumi Kamura

John N Bradsher

Ronald C Conway

Rbx1, an evolutionarily conserved Cullin-interacting RING-H2 finger protein, has been discovered. Mammalian Rbx1 has been identified as a component of the CUL2-containing VHL complex. An Rbx1 homolog fromhas also been identified as a subunit and activator of the Cdc53-containing SCFubiquitin ligase required for ubiquitination of the cdk inhibitor Sic1 and for the G1/S cell cycle transition in yeast, providing a link between the multiprotein VHL tumor suppressor complex and cellular ubiquitination. The Rbx1 protein acts as a cellular marker useful (1) in detecting a possible predisposition to certain carcinomas, (2) as a molecular target for treating those carcinomas therapeutically. (3) as a target for inhibition by drugs that manipulate the growth of cells, and (4) as a research tool to better understand the various complex mechanisms of cell ubiquitination, binding of certain activator proteins, fibronectin deposition and other aspects of the cellular division process.

Component of von Hippel-Lindau tumor suppressor complex and SCF ubiquitin ligase

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.

ELL2, a new member of an ELL family of RNA polymerase II elongation factors

The functional domains of Elongin A having transcriptional activation activity and Elongin BC binding activity and the functional domains of Elongin C having Elongin A activation activity and Elongin A and/or Elongin C binding activity have now been identified and isolated.

Elongin A and C functional domains

ELL2, a new member of an ELL family of RNA polymerase II elongation

A new RNA polymerase transcription factor has been discovered. The enzyme significantly increases the rate of transcription elongation by RNA polymerase II.

Growing community of inventors

Oklahoma City, OK, United States of America

Joan W Conaway