Epernicus: Martin L Duennwald, Ph.D.

Martin L Duennwald, Ph.D.

Position:
Scientist (Assistant Professor)

Boston Biomedical Research Institute, Inc. (Watertown, MA)
Degrees:

Ph.D., Biology, Max Planck Institute for Breeding Research/Univ of Cologne
Past Advisors:

Susan Lindquist (as Post Doctoral Fellow)

Nils Johnsson (as Graduate Student - Ph.D.)
Research:

Communities:

Martin Duennwald's Genealogy

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Martin Duennwald's Publications (10)

Chaperone-dependent amyloid assembly protects cells from prion toxicity.
Douglas PM, Treusch S, Ren HY, Halfmann R, Duennwald ML, Lindquist S, Cyr DM

Proceedings of the National Academy of Sciences of the United States of America. 2008 May 20;105(20):7206-11
Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs.
Wang H, Duennwald ML, Roberts BE, Rozeboom LM, Zhang YL, Steele AD, Krishnan R, Su LJ, Griffin D, Mukhopadhyay S, Hennessy EJ, Weigele P, Blanchard BJ, King J, Deniz AA, Buchwald SL, Ingram VM, Lindquist S, Shorter J

Proceedings of the National Academy of Sciences of the United States of America. 2008 May 20;105(20):7159-64
Chaperones and polyglutamine expansion disorders
Martin L Duennwald

In Heat Shock Proteins and the Brain: Implications for Neurodegenerative Diseases and Neuroprotection Asea, A. A. & Brown, I. R., eds. . 2008;3:3-23
A network of protein interactions determines polyglutamine toxicity.
Duennwald ML, Jagadish S, Giorgini F, Muchowski PJ, Lindquist S

Proceedings of the National Academy of Sciences of the United States of America. 2006 Jul 18;103(29):11051-6
Flanking sequences profoundly alter polyglutamine toxicity in yeast.
Duennwald ML, Jagadish S, Muchowski PJ, Lindquist S

Proceedings of the National Academy of Sciences of the United States of America. 2006 Jul 18;103(29):11045-50
A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104.
Cashikar AG, Duennwald M, Lindquist SL

The Journal of biological chemistry. 2005 Jun 24;280(25):23869-75
Potent inhibition of huntingtin aggregation and cytotoxicity by a disulfide bond-free single-domain intracellular antibody.
Colby DW, Chu Y, Cassady JP, Duennwald M, Zazulak H, Webster JM, Messer A, Lindquist S, Ingram VM, Wittrup KD

Proceedings of the National Academy of Sciences of the United States of America. 2004 Dec 21;101(51):17616-21
Recognition of a subset of signal sequences by Ssh1p, a Sec61p-related protein in the membrane of endoplasmic reticulum of yeast Saccharomyces cerevisiae.
Wittke S, Dünnwald M, Albertsen M, Johnsson N

Molecular biology of the cell. 2002 Jul;13(7):2223-32
Sec62p, a component of the endoplasmic reticulum protein translocation machinery, contains multiple binding sites for the Sec-complex.
Wittke S, Dünnwald M, Johnsson N

Molecular biology of the cell. 2000 Nov;11(11):3859-71
Detection of transient in vivo interactions between substrate and transporter during protein translocation into the endoplasmic reticulum.
Dünnwald M, Varshavsky A, Johnsson N

Molecular biology of the cell. 1999 Feb;10(2):329-44

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Martin L Duennwald, Ph.D.

Scientist (Assistant Professor)

Martin Duennwald's Genealogy

Martin Duennwald's Publications (10)