Vishu Lingappa , M.D.
Email: LingapV@cpmcri.org
Introduction
According to Dr. Lingappa, many cells have the ability to fold up specific proteins in diverse shapes and therefore access diverse functions depending on circumstances. Once again, his group has used their slow-motion technique to search for the alternatively folded proteins as well as the cell enzymes and factors that regulate protein folding. The results are preliminary but provocative. He speculates, for example, that some alternative protein forms may be useful in an organism’s early development or under certain cell conditions like stress. As an adult, however, these vestigial protein shapes are not needed and may in fact take on harmful roles, as they apparently do in neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and perhaps even amyotrophic lateral sclerosis (ALS).
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Publications
Click here for List of publications by Vishu Lingappa, M.D. in PubMed.
Recent publications include:
1: Akhavan A, Crivelli SN, Singh M, Lingappa VR, Muschler JL. SEA domain proteolysis determines the functional composition of dystroglycan.
FASEB J. 2008 Feb;22(2):612-21. Epub 2007 Sep 28.
2: Gruzman A, Wood WL, Alpert E, Prasad MD, Miller RG, Rothstein JD, Bowser R, Hamilton R, Wood TD, Cleveland DW, Lingappa VR, Liu J. Common molecular signature in SOD1 for both sporadic and familial amyotrophic
lateral sclerosis.
Proc Natl Acad Sci U S A. 2007 Jul 24;104(30):12524-9. Epub 2007 Jul 16.
3: Karpuj MV, Giles K, Gelibter-Niv S, Scott MR, Lingappa VR, Szoka FC, Peretz D, Denetclaw W, Prusiner SB. Phosphorothioate oligonucleotides reduce PrP levels and prion infectivity in cultured cells.
Mol Med. 2007 Mar-Apr;13(3-4):190-8.
4: Ott CM, Akhavan A, Lingappa VR. Specific features of the prion protein transmembrane domain regulate nascent
chain orientation.
J Biol Chem. 2007 Apr 13;282(15):11163-71. Epub 2007 Feb 2.
5: Marzi A, Akhavan A, Simmons G, Gramberg T, Hofmann H, Bates P, Lingappa VR, Pöhlmann S. The signal peptide of the ebolavirus glycoprotein influences interaction with the cellular lectins DC-SIGN and DC-SIGNR.
J Virol. 2006 Jul;80(13):6305-17.
6: Lingappa VR, Lingappa JR. Recent insights into biological regulation from cell-free protein-synthesizing systems.
Mt Sinai J Med. 2005 May;72(3):141-60. Review.
7: Ott CM, Lingappa VR. Signal sequences influence membrane integration of the prion protein.
Biochemistry. 2004 Sep 28;43(38):11973-82.
8: Rutkowski DT, Ott CM, Polansky JR, Lingappa VR. Signal sequences initiate the pathway of maturation in the endoplasmic reticulum lumen.
J Biol Chem. 2003 Aug 8;278(32):30365-72. Epub 2003 May 27.
9: Lipschutz JH, Lingappa VR, Mostov KE. The exocyst affects protein synthesis by acting on the translocation machinery of
the endoplasmic reticulum.
J Biol Chem. 2003 Jun 6;278(23):20954-60. Epub 2003 Mar 28.
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