Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Philip K. Tan"'
Autor:
Philip K. Tan, Jeffrey N. Miner
Publikováno v:
ADMET and DMPK, Vol 5, Iss 2, Pp 59-74 (2017)
Gout is a common inflammatory arthritis that is caused by chronically-elevated serum uric acid (sUA) levels (hyperuricemia). In humans, sUA levels are predominantly controlled by a variety of transporters that mediate the elimination of uric acid thr
Externí odkaz:
https://doaj.org/article/3c67fb428ae6422286e4d7f630fdfeb3
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Abstract Gout is caused by elevated serum urate levels, which can be treated using inhibitors of the uric acid transporter, URAT1. Here, we characterize verinurad (RDEA3170), which is currently under evaluation for gout therapy. Verinurad specificall
Externí odkaz:
https://doaj.org/article/101d72a4c0c246b6a3c62d73d187ccad
Publikováno v:
Molecular Biology and Evolution
Uric acid is the highly insoluble end-product of purine metabolism in humans. Serum levels exceeding the solubility threshold can trigger formation of urate crystals resulting in gouty arthritis. Uric acid is primarily excreted through the kidneys wi
Publikováno v:
Scientific Reports
Gout is caused by elevated serum urate levels, which can be treated using inhibitors of the uric acid transporter, URAT1. We exploited affinity differences between the human and rat transporters to map inhibitor binding sites in URAT1. Human-rat tran
Autor:
David T. Hagerty, Payal Nanavati, Philip K. Tan, Li-Tain Yeh, Barry D. Quart, Jean-Luc Girardet, Kimberly Manhard, Sha Liu, Robert Terkeltaub, Jeffrey N. Miner, Cory Iverson, David Hyndman, Zancong Shen
Publikováno v:
Arthritis Research & Therapy
Arthritis research & therapy, vol 18, iss 1
Arthritis research & therapy, vol 18, iss 1
Background Excess body burden of uric acid promotes gout. Diminished renal clearance of uric acid causes hyperuricemia in most patients with gout, and the renal urate transporter (URAT)1 is important for regulation of serum uric acid (sUA) levels. Th
Autor:
William Keefe, Philip K. Tan, Kenneth K. Wong, Norman Nash, Fabrice Piu, Jean Wang, Esther C. Reding, Hans H. Schiffer, Timothy A. Sweetnam, Pey-Lih H. Littler, Mark R. Brann
Publikováno v:
Molecular Pharmacology. 72:1440-1446
A limited number of whole-cell assays allow monitoring of receptor tyrosine kinase (RTK) activity in a signaling pathway-specific manner. We present the general use of the bioluminescence resonance energy transfer (BRET) technology to quantitatively
Autor:
Anand Mehta, Gary Thomas, Clarissa L. Waites, Robert H. Edwards, Philip K. Tan, David E. Krantz
Publikováno v:
The Journal of cell biology, vol 152, iss 6
The Journal of Cell Biology
The Journal of Cell Biology
The release of biogenic amines from large dense core vesicles (LDCVs) depends on localization of the vesicular monoamine transporter VMAT2 to LDCVs. We now find that a cluster of acidic residues including two serines phosphorylated by casein kinase 2
Autor:
Philip K. Tan, Yongjian Liu, Rachel Wilson, Robert H. Edwards, Judith Klumperman, David E. Krantz, Clarissa L. Waites, Viola Oorschot
Publikováno v:
The Journal of Cell Biology
The Journal of cell biology, vol 149, iss 2
The Journal of cell biology, vol 149, iss 2
Vesicular transport proteins package classical neurotransmitters for regulated exocytotic release, and localize to at least two distinct types of secretory vesicles. In PC12 cells, the vesicular acetylcholine transporter (VAChT) localizes preferentia
Autor:
Philip K. Tan, Holly M. Engle, Heather R. Panek, Sandra K. Lemmon, Kim M. Marks, J. David Stepp, Lucy C. Robinson
Publikováno v:
The EMBO Journal. 16:4194-4204
In Saccharomyces cerevisiae, the redundant YCK1 and YCK2 genes (Yeast Casein Kinase 1) are required for viability. We describe here the molecular analysis of four mutations that eliminate the requirement for Yck activity. These mutations alter protei
Publikováno v:
The Journal of Cell Biology
The yeast membrane protein Kex2p uses a tyrosine-containing motif within the cytoplasmic domain for localization to a late Golgi compartment. Because Golgi membrane proteins mislocalized to the plasma membrane in yeast can undergo endocytosis, we exa