Results 41 to 50 of about 2,830 (142)

Endothelial Cells Mediated by STING Regulate Oligodendrogenesis and Myelination During Brain Development

Advanced Science
Oligodendrocyte precursor cells (OPCs) migrate extensively using blood vessels as physical scaffolds in the developing central nervous system. Although the association of OPCs with the vasculature is critical for migration, the regulatory mechanisms ...
Wenwen Wang, Yanyan Wang, Libo Su, Mengtian Zhang, Tianyu Zhang, Jinyue Zhao, Hongyan Ma, Dongming Zhang, Fen Ji, Ryan Dingli Jiao, Hong Li, Yuming Xu, Lei Chen, Jianwei Jiao   +13 more
doaj   +1 more source

Studies of CTNNBL1 and FDFT1 variants and measures of obesity: analyses of quantitative traits and case-control studies in 18,014 Danes

BMC Medical Genetics, 2009
Background A genome-wide scan in unrelated US Caucasians identified rs7001819 upstream of farnesyl-diphosphate farnesyltransferase 1 (FDFT1) and multiple variants within catenin (cadherin-associated protein), β-like 1 (CTNNBL1) to associate strongly with
Almind Katrine, Lauritzen Torsten, Sandbæk Annelli, Borch-Johnsen Knut, Mogensen Mette, Andreasen Camilla, Hansen Lars, Jørgensen Torben, Pedersen Oluf, Hansen Torben   +9 more
doaj   +1 more source

The CaaX specificities of Arabidopsis protein prenyltransferases explain era1 and ggb phenotypes [PDF]

, 2010
Background Protein prenylation is a common post-translational modification in metazoans, protozoans, fungi, and plants. This modification, which mediates protein-membrane and protein-protein interactions, is characterized by the covalent attachment of
Michelle Andrews, David H Huizinga, Dring N Crowell   +2 more
core   +2 more sources

Prenylated Proteins: Structural Diversity and Functions [PDF]

, 2022
The cell membranes consist of lipid bilayers that are semipermeable. The semipermeable nature enables the cell membranes to regulate the transport of materials entering and exiting the cell.
Kamanna, Kantharaju, Kamath, Aravind
core   +2 more sources

La prénylation des protéines chez les insectes : cible prometteuse pour le développement d'insecticides biorationnels ciblant les Lépidoptères ?

Biotechnologie, Agronomie, Société et Environnement, 2014
Protein prenylation in insects: a potential target for the development of bio-rational insecticides targeting the Lepidoptera?. Short-chain prenyltransferases (farnesyl diphosphate synthase [FPPS] and geranylgeranyl diphosphate synthase [GGPPS]) and ...
Barbar, A., Cusson, M.
doaj  

The Concise Guide to PHARMACOLOGY 2015/16:Enzymes [PDF]

, 2015
The Concise Guide to PHARMACOLOGY 2015/16 provides concise overviews of the key properties of over 1750 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org),
Aldrich, R, Alexander, SPH, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Benson, HE, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Davies, JA, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Fabbro, D, Faccenda, E, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kelly, E, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, Marrion, N, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Pawson, AJ, Perez-Reyes, E, Pertwee, RG, Peters, JA, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sharman, JL, Sladek, FM, Southan, C, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, Zajac, J-M   +151 more
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Identification of Genes Potentially Regulated by Human Polynucleotide Phosphorylase (hPNPaseold-35) Using Melanoma as a Model [PDF]

, 2013
Human Polynucleotide Phosphorylase (hPNPaseold-35 or PNPT1) is an evolutionarily conserved 3′→5′ exoribonuclease implicated in the regulation of numerous physiological processes including maintenance of mitochondrial homeostasis, mtRNA import and aging ...
Bacolod, Manny D., Das, Swadesh K., Dasgupta, Santanu, Emdad, Luni, Sokhi, Upneet K.   +4 more
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Estrogen Enhances FDFT1 Expression in Theca Cells of Chicken Hierarchical Ovarian Follicles by Increasing LSD1Ser54p Level Through GSK3β Phosphorylation at 216th Tyrosine

Biomolecules
The development of chicken ovarian follicles involves two key stages of primordial follicle recruitment and follicle selection that are tightly regulated by multiple reproductive hormones and cytokines.
Yanhong Zhang, Conghao Zhong, Xinmei Shu, Qingxin Liu, Yunliang Jiang   +4 more
doaj   +1 more source

Assessment of the rs2645424 C/T single nucleotide polymorphisms in the FDFT1 gene, hepatic expression, and serum concentration of the FDFT patients with nonalcoholic fatty liver disease [PDF]

, 2018
The present work was supported by a grant from the Scientific Research Projects Coordination Unit of Istanbul University (Project No: 12888).Despite being the most common chronic liver disease, the pathogenesis of nonalcoholic fatty liver disease (NAFLD)
Aydoğan, Hülya Yılmaz, Coşkunpınar, Ender M., Ekmekçi, Cumhur Gökhan, Gömleksiz, Özlem Kurnaz, Hastürk, Burcu, Oltulu, Yasemin Müşteri, Tiryakioğlu, Necip Ozan, Yaylım, İlhan, Çolak, Yaşar, Şenateş, Ebubekir   +9 more
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Elucidation of the Photorhabdus temperata Genome and Generation of a Transposon Mutant Library To Identify Motility Mutants Altered in Pathogenesis [PDF]

, 2015
The entomopathogenic nematode Heterorhabditis bacteriophora forms a specific mutualistic association with its bacterial partner Photorhabdus temperata.
Abebe-Akele, Feseha, Bullock, Hannah, Durakovic, Umjia, Gately, Jon, Hurst, Sheldon G., IV, Jackobeck, Ryan, Janicki, Erik, Michaels, Brandye, Rowedder, Holli, Tisa, Louis S.   +9 more
core   +2 more sources