Search

Your search keyword '"Hersh, Louis B."' showing total 644 results
Start Over Author "Hersh, Louis B."
644 results on '"Hersh, Louis B."'

9. Structure of puromycin-sensitive aminopeptidase and polyglutamine binding.

Author

Madabushi, Sowmya, Chow, K. Martin, Song, Eun Suk, Goswami, Anwesha, Hersh, Louis B., and Rodgers, David W.

Subjects
POLYGLUTAMINE, PEPTIDES, PEPTIDASE, AMINOPEPTIDASES, CATALYTIC domains, TUBULINS, CRYSTAL structure
Abstract

Puromycin-sensitive aminopeptidase (E.C. 3.4.11.14, UniProt P55786), a zinc metallopeptidase belonging to the M1 family, degrades a number of bioactive peptides as well as peptides released from the proteasome, including polyglutamine. We report the crystal structure of PSA at 2.3 Ǻ. Overall, the enzyme adopts a V-shaped architecture with four domains characteristic of the M1 family aminopeptidases, but it is in a less compact conformation compared to most M1 enzymes of known structure. A microtubule binding sequence is present in a C-terminal HEAT repeat domain of the enzyme in a position where it might serve to mediate interaction with tubulin. In the catalytic metallopeptidase domain, an elongated active site groove lined with aromatic and hydrophobic residues and a large S1 subsite may play a role in broad substrate recognition. The structure with bound polyglutamine shows a possible interacting mode of this peptide, which is supported by mutation. [ABSTRACT FROM AUTHOR]

Published
2023
Full Text
View/download PDF

11. BACE2 Expression Increases in Human Neurodegenerative Disease

Author

Holler, Christopher J., Webb, Robin L., Laux, Ashley L., Beckett, Tina L., Niedowicz, Dana M., Ahmed, Rachel R., Liu, Yinxing, Simmons, Christopher R., Dowling, Amy L.S., Spinelli, Angela, Khurgel, Moshe, Estus, Steven, Head, Elizabeth, Hersh, Louis B., and Murphy, M. Paul

Published
2012
Full Text
View/download PDF

31. Toxoplasma gondii Toxolysin 4 Contributes to Efficient Parasite Egress from Host Cells

Author

Huynh, My-Hang, primary, Roiko, Marijo S., additional, Gomes, Angelica O., additional, Schinke, Ellyn N., additional, Schultz, Aric J., additional, Agrawal, Swati, additional, Oellig, Christine A., additional, Sexton, Travis R., additional, Beauchamp, Jessica M., additional, Laliberté, Julie, additional, Sivaraman, Komagal Kannan, additional, Hersh, Louis B., additional, McGowan, Sheena, additional, and Carruthers, Vern B., additional

Published
2021
Full Text
View/download PDF

34. Environmental enrichment reduces A-beta levels and amyloid deposition in transgenic mice

Author

Lazarov, Orly, Robinson, John, Ya-ping Tang, Hariston, IIana S., Zelka Korade-Mirnics, Lee, Virginia M. Y., Hersh, Louis B., Sapolsky, Robert M., Mirnics, Karoly, and Sisodia, Sangram S.

Subjects
Biological sciences
Abstract

Studies provide evidence that environmental enrichment leads to reductions in steady-state levels of cerebral amyloid-beta peptides and amyloid deposition and selective upregulation in levels of specific transcripts in brains of trangenic mice. The enzymatic activity of an amyloid-beta degrading endopeptidase, nephrilysin, is elevated in the brains of 'enriched' mice and inversely correlated with amyloid burden.

Published
2005

37. Amyloid-[beta] peptide levels in brain are inversely correlated with insulysin activity levels in vivo

Author

Miller, Bonnie C., Eckman, Elizabeth A., Sambamurti, Kumar, Dobbs, Nicole, Chow, K. Martin, Eckman, Christopher B., Hersh, Louis B., and Thiele, Dwain L.

Subjects
Alzheimer's disease -- Physiological aspects, Science and technology, National Academy of Sciences -- Research
Abstract

Factors that elevate amyloid-[beta] (A[beta]) peptide levels are associated with an increased risk for Alzheimer's disease. Insulysin has been identified as one of several proteases potentially involved in A[beta] degradation based on its hydrolysis of A[beta] peptides in vitro. In this study, in vivo levels of brain A[beta]40 and A[beta]42 peptides were found to be increased significantly (1.6- and 1.4-fold, respectively) in an insulysin-deficient gene-trap mouse model. A 6-fold increase in the level of the [gamma]-secretase-generated C-terminal fragment of the A[beta] precursor protein in the insulysin-deficient mouse also was found. In mice heterozygous for the insulysin gene trap, in which insulysin activity levels were decreased [approximately equal to]50%, brain A[beta] peptides were increased to levels intermediate between those in wild-type mice and homozygous insulysin gene-trap mice that had no detectable insulysin activity. These findings indicate that there is an inverse correlation between in vivo insulysin activity levels and brain A[beta] peptide levels and suggest that modulation of insulysin activity may alter the risk for Alzheimer's disease.

Published
2003

41. Expression of the acidic stretch of nardilysin as a functional binding domain

Author

Ma, Zhangliang, Csuhai, Eva, Chow, K. Martin, and Hersh, Louis B.

Subjects
Biochemistry -- Research, Amino acids -- Physiological aspects, Gene expression -- Physiological aspects, Glutathione -- Physiological aspects, Transferases -- Physiological aspects, Proteins -- Physiological aspects, Zinc -- Physiological aspects, Arginine -- Physiological aspects, Biological sciences, Chemistry
Abstract

Research has been conducted on the acidic domain in nardilysin. The mouse acidic domain and the human nardilysin have been expressed as fusion proteins with glutathione S-transferase and the results indicate that nardilysin acidic domain can function as an autonomous domain.

Published
2001

Catalog

Books, media, physical & digital resources
See catalog results