Physical Address
IGBB
Portera HPC Building
2 Research Boulevard
Starkville, MS 39759
Mailing Address
IGBB
Portera HPC Building
Box 9627
Mississippi State, MS 39762
Phone/Fax
Phone: 662-325-8278
Fax: 662-325-7692
We highly recommend that anyone wishing to contact the IGBB via the Internet/e-mail do so by submitting a HelpDesk ticket. Submitting a HelpDesk ticket ensures that your question is directed to the appropriate IGBB staff member(s) and is not left unanswered. In order to submit a HelpDesk ticket, you must first register for a free MyIGBB account. Registration is simple, takes less than a minute, and obligates you to absolutely nothing.
If you do not wish to use the IGBB HelpDesk, you may send an e-mail to one of the following IGBB employees: Dr. Olga Pechanova (Proteomics Lead), Dr. Chuan-Yu Hsu (Genomics Lead), Mr. Tony Arick (Computational Biology Lead), or Ms. Kelsey Stewart (Contract & Grant Specialist).
See Personnel for more contact names/numbers/e-mail addresses.

PTMs in Conversation: Activity and Function of Deubiquitinating Enzymes Regulated via Post-Translational Modifications
IGBB Authors:
Mariola J. EdelmannPUBLICATION YEAR:
2011IMPACT FACTOR:
4.906CITATION COUNT:
55Kessler BM, Edelmann MJ (2011) PTMs in Conversation: Activity and Function of Deubiquitinating Enzymes Regulated via Post-Translational Modifications.
Cell Biochemistry and Biophysics 60(1-2): 21-38.
DOI:
10.1007/s12013-011-9176-6EID:
2-s2.0-79955941973PMID: 21480003
DOWNLOAD PDFABSTRACTDeubiquitinating enzymes (DUBs) constitute a diverse protein family and their impact on numerous biological and pathological processes has now been widely appreciated. Many DUB functions have to be tightly controlled within the cell, and this can be achieved in several ways, such as substrate-induced conformational changes, binding to adaptor proteins, proteolytic cleavage, and post-translational modifications (PTMs). This review is focused on the role of PTMs including monoubiquitination, sumoylation, acetylation, and phosphorylation as characterized and putative regulative factors of DUB function. Although this aspect of DUB functionality has not been yet thoroughly studied, PTMs represent a versatile and reversible method of controlling the role of DUBs in biological processes. In several cases PTMs might constitute a feedback mechanism insuring proper functioning of the ubiquitin proteasome system and other DUB-related pathways.

Dr. Wen-Hsing ChengAssociate Professor
Food Science, Nutrition & Health PromotionIGBB Affiliate
email(662) 325-3200
website Dr. Margaret L. KhaitsaProfessor
CVM Pathobiology & Population MedicineIGBB Affiliate
email(662) 325-1365
website
The IGBB is supported, in part, by the following units:
The IGBB is an HPC² member center.