Human E3 ubiquitin protein ligase

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for...

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

435243, 4352542, 4353201, 435325, 435410, 435455, 536 231, 536 232, 536 243, 536 2431, 536 2433, C12N 900, C12N 1552, C12N 1511, C07H 2104

Patent

active

059768495

ABSTRACT:
A novel human E3 ubiquitin protein ligase is provided as well as a nucleic acid structural region which encodes the polypeptide and the amino acid residue sequence of the human biomolecule. Methods are provided to identify compounds that modulate the biological activity of the molecule and hence regulate cellular and tissue physiology.

REFERENCES:
Hochstrasser, Mark; Ubiquitin-Dependent Protein Degragation, Annu. Rev. Genet. 1996, 30:405-39.
Weissman, Alan M.; Regulating Degradation by Ubiquitination, Review Immunology Today, vol. 18, No. 4 189, Apr. 1997.
Pahl, Heike L. et al.; Control of Gene Expression by Proteolysis, Current Opinion in Cell Biology 1996, 8:340-347.
Rolfe, Mark et al.; The Ubiquitin-Mediated Proteolytic Pathway as a Therapeutic Area, J. Mol. Med. (1997) 75:5-17.
Perry, William L. et al.; The Itchy Locus Encodes a Novel Ubiquitin Protein Ligase That is Disrupted in a .sup.18h Mice, Nature Genetics, vol. 18, Feb. 1998.
D'Andrea, Alan D., Relieving the Itch, Nature Genetics, vol. 18, Feb. 1998.

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Human E3 ubiquitin protein ligase does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Human E3 ubiquitin protein ligase, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Human E3 ubiquitin protein ligase will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-2133590

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.