Hartmut Wohlrab, Ph.D.
Senior Scientist
Membrane transport proteins, type II diabetes, aging
Email: wohlrab at bbri.org
Phone: 617.658.7775
Fax: 617.972.1753

Research Summary
Type 2 diabetes is unfortunately increasing among adults at an alarming rate and thus not unexpectedly also among children.  Aging is a universal disease.  We carry out structure research on novel membrane proteins (PTP, UCP2, glucose-6-phosphatase) that will lead to increased insulin output by the pancreatic beta cells of the type 2 diabetic and to a better understanding of hepatic carbohydrate metabolism.  The aging research focuses on proteins in metabolic pathways that undergo enormous changes or that are critical to these changes when organisms age.  Results may lead to the identification of causes for diseases that afflict older adults. More.

Four stages of transport catalyzed by homodimeric PTP
and how PTP may be folded in the membrane.

Selected Publications
Wohlrab H. The human mitochondrial transport/carrier protein family. Nonsynonymous single nucleotide polymorphisms (nsSNPs) and mutations that lead to human diseases. Biochim Biophys Acta. 2006;1757(9-10):1263-70.

Wohlrab H. The human mitochondrial transport protein family: identification and protein regions significant for transport function and substrate specificity. Biochim Biophys Acta. 2005;1709(2):157-68.

Wohlrab H. Novel inter- and intrasubunit contacts between transport-relevant residues of the homodimeric mitochondrial phosphate transport protein. Biochem Biophys Res Commun. 2004;320:685-688.

Phelps A, Wohlrab H. Homodimeric mitochondrial phosphate transport protein. Transient subunit/subunit contact site between the transport relevant transmembrane helices A. Biochemistry. 2004;43(20):6200-6207.

Berezhna S, Wohlrab H, Champion PM. Resonance Raman investigations of cytochrome c conformational change upon interaction with the membranes of intact and Ca2+-exposed mitochondria. Biochemistry. 2003;42(20):6149-6158.

Wohlrab H, Annese V, Haefele A. Single replacement constructs of all hydroxyl, basic, and acidic amino acids identify new function and structure-sensitive regions of the mitochondrial phosphate transport protein. Biochemistry. 2002;41(9):3254-3261.

Phelps A, Briggs C, Haefele A, Mincone L, Ligeti E, Wohlrab H. Mitochondrial phosphate transport protein. Reversions of inhibitory conservative mutations identify four helices and a nonhelix protein segment with transmembrane interactions and Asp39, Glu137, and Ser158 as nonessential for transport. Biochemistry. 2001;40(7):2080-2086.

PubMed:
Click here for a list of publications (searches the National Library of Medicine's PubMed database.)