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B. Nelson Chau

Researcher at Johns Hopkins University

Publications -  7
Citations -  962

B. Nelson Chau is an academic researcher from Johns Hopkins University. The author has contributed to research in topics: Apoptosis & Bcl-xL. The author has an hindex of 5, co-authored 7 publications receiving 930 citations.

Papers
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Journal ArticleDOI

Aven, a novel inhibitor of caspase activation, binds Bcl-xL and Apaf-1.

TL;DR: Aven as mentioned in this paper is a new class of cell death regulator that targets both Bcl-x(L) and the caspase regulator, Apaf-1, in a yeast two-hybrid screen.
Journal ArticleDOI

Pro-apoptotic cleavage products of Bcl-xL form cytochrome c-conducting pores in pure lipid membranes.

TL;DR: Data are consistent with the hypothesis that Bax-like proteins oligomerize to form lipid-containing pores in the outer mitochondrial membrane, thereby releasing intermembrane apoptogenic factors into the cytosol.
Journal ArticleDOI

Survival motor neuron protein modulates neuron-specific apoptosis

TL;DR: It is shown that SMN protects primary neurons and differentiated neuron-like stem cells, but not cultured cell lines from virus-induced apoptotic death, and increases survival of virus-infected mice.
Patent

Inhibitor of programmed cell death

Abstract: The present invention provides a human apoptosis regulator protein (Aven) and polynucleotides which identify and encode Aven. The invention also provides genetically engineered expression vectors and host cells comprising the nucleic acid sequences encoding Aven, and a method for producing Aven. The invention also provides for agonists, antibodies, or antagonists specifically binding Aven, and their use, in the prevention and treatment of diseases associated with expression of Aven. Additionally, the invention provides for the use of antisense molecules to polynucleotides encoding Aven for the treatment of diseases associated with the expression of Aven. The invention also provides diagnostic assays which utilize the polynucleotide, or fragments or the complement thereof, and antibodies specifically binding Aven.