Zobrazeno 1 - 10
of 33
pro vyhledávání: '"William A. LaMarr"'
Autor:
Shunji Tomatsu, Tsutomu Shimada, Robert W. Mason, Adriana M. Montaño, Joan Kelly, William A. LaMarr, Francyne Kubaski, Roberto Giugliani, Aratrik Guha, Eriko Yasuda, William Mackenzie, Seiji Yamaguchi, Yasuyuki Suzuki, Tadao Orii
Publikováno v:
Metabolites, Vol 4, Iss 3, Pp 655-679 (2014)
Mucopolysaccharidoses (MPS) are a group of lysosomal storage disorders caused by deficiency of the lysosomal enzymes essential for catabolism of glycosaminoglycans (GAGs). Accumulation of undegraded GAGs results in dysfunction of multiple organs, res
Externí odkaz:
https://doaj.org/article/f1c6d7024dc24975b8e510fd50856ea4
Autor:
Peter T. Rye, William A. LaMarr
Publikováno v:
Analytical Biochemistry. 482:40-47
Glycolysis is a 10-step metabolic pathway involved in producing cellular energy. Many tumors exhibit accelerated glycolytic rates, and enzymes that participate in this pathway are focal points of cancer research. Here, a novel method for the measurem
Autor:
Morteza Razavi, William A. LaMarr, Matthew E. Pope, Christine A. Miller, N. Leigh Anderson, Lauren E. Frick, Terry W. Pearson
Publikováno v:
Journal of Proteome Research. 11:5642-5649
We investigated the utility of an SPE-MS/MS platform in combination with a modified SISCAPA workflow for chromatography-free MRM analysis of proteotypic peptides in digested human plasma. This combination of SISCAPA and SPE-MS/MS technology allows se
Publikováno v:
SLAS Discovery. 16:1217-1226
The sirtuin enzymes, a class of NAD(+)-dependent histone deacetylases, are a focal point of epigenetic research because of their roles in regulating gene expression and cellular differentiation by deacetylating histones and a host of transcription fa
Publikováno v:
SLAS Discovery. 16:1186-1195
Histone acetyltransferases (HATs) catalyze the transfer of an acetyl group from an acetyl-coenzyme A donor molecule to specific lysine residues within proteins. The acetylation state of proteins, particularly histones, is known to modulate their inte
Autor:
Yusheng Xiong, William A. LaMarr, Ming-juan Luo, Tom G. Holt, Kristian K. Jensen, Lorraine Malkowitz, Bernard K. Choi, Maxine Jonas, Can C. Ozbal, Neil S. Geoghagen, Jun Wang, Qi Luo, Xun Chen, Claude Dufresne
Publikováno v:
Label-Free Technologies for Drug Discovery
Autor:
Olga V. Nemirovskiy, Jaime L. Masferrer, Grace E. Munie, William A. LaMarr, Maureen K. Highkin, John W. Rains, Marek M. Nagiec, Matthew P. Yates
Publikováno v:
SLAS Discovery. 16:272-277
To facilitate discovery of compounds modulating sphingosine-1-phosphate (S1P) signaling, the authors used high-throughput mass spectrometry technology to measure S1P formation in human whole blood. Since blood contains endogenous sphingosine (SPH) an
Autor:
Asra Malikzay, Lynn Miesel, Dayna L. Daubaras, Rumin Zhang, Cynthia Kravec, Frederick J. Monsma, Charles A. Lunn, William A. LaMarr, Richard F. Hart, Can C. Ozbal, Todd A. Black, Erik F. Langsdorf
Publikováno v:
SLAS Discovery. 15:52-61
A high-throughput mass spectrometry assay to measure the catalytic activity of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase, LpxC, is described. This reaction is essential in the biosynthesis of lipopolysaccharide (LPS) of gram-nega
Autor:
Kristian K. Jensen, Qi Luo, Ming-juan Luo, Neil S. Geoghagen, Yusheng Xiong, Gergely M. Makara, Claude Dufresne, William A. LaMarr, Bernard K. Choi, Lorraine Malkowitz, Can C. Ozbal, Tom G. Holt
Publikováno v:
ASSAY and Drug Development Technologies. 7:495-506
Label-free mass spectrometric (MS) technologies are particularly useful for enzyme assay design for drug discovery screens. MS permits the selective detection of enzyme substrates or products in a wide range of biological matrices without need for de
Publikováno v:
Combinatorial Chemistry & High Throughput Screening. 12:752-759
In this review various technologies and approaches for the utilization of mass spectrometry in high throughput analyses are discussed. The use of quadrupole-based mass spectrometry in the screening of chemical libraries against enzymatic targets for