Results 31 to 40 of about 20,263 (273)

A secretory kinase complex regulates extracellular protein phosphorylation. [PDF]

, 2015
Although numerous extracellular phosphoproteins have been identified, the protein kinases within the secretory pathway have only recently been discovered, and their regulation is virtually unexplored.
Cui, Jixin, Dixon, Jack E, Rahdar, Meghdad, Tagliabracci, Vincent S, Wen, Jianzhong, Xiao, Junyu   +5 more
core   +2 more sources

Comparative Ser/Thr/Tyr phosphoproteomics between two Mycobacterial species: The fast growing Mycobacterium smegmatis and the slow growing Mycobacterium bovis BCG.

Frontiers in Microbiology, 2015
Ser/Thr/Tyr protein phosphorylation plays a critical role in regulating mycobacterial growth and development. Understanding the mechanistic link between protein phosphorylation signaling network and mycobacterial growth rate requires a global view of the
Kehilwe Confidence Nakedi, Andrew JM Nel, Shaun eGarnett, Jonathan M Blackburn, Nelson Da Cruz Soares   +4 more
doaj   +1 more source

Investigating the effect of target of rapamycin kinase inhibition on the Chlamydomonas reinhardtii phosphoproteome: from known homologs to new targets [PDF]

, 2019
Recuperado de: https://www.biorxiv.org/content/10.1101/310102v1Target of rapamycin (TOR) kinase is a conserved regulator of cell growth whose activity is modulated in response to nutrients, energy and stress.
Couso Liáñez, Inmaculada Concepción, Crespo González, José Luis, Hicks, Leslie, McConnell, Evan W., Perrine, Zoee, Umen, James G., Werth, Emily G.   +6 more
core   +1 more source

Interrogating the hidden phosphoproteome [PDF]

PROTEOMICS, 2017
Postgenomic studies continue to highlight the potential clinical importance of protein phosphorylation signaling pathways in drug discovery. Unfortunately, the dynamic range and variable stoichiometry of protein phosphorylation continues to stymie efforts to achieve comprehensive characterization of the human phosphoproteome.
Un-Beom, Kang, William M, Alexander, Jarrod A, Marto   +2 more
openaire   +2 more sources

Ancestral roles of the Fam20C family of secreted protein kinases revealed in C. elegans. [PDF]

, 2019
Fam20C is a secreted protein kinase mutated in Raine syndrome, a human skeletal disorder. In vertebrates, bone and enamel proteins are major Fam20C substrates.
Adina Gerson-Gurwitz, Arribere, Arshad Desai, Bahl, Bando, Bies, Brown, Byerly, Cancino, Carolyn A. Worby, Carrascal, Cui, Dhanya Cheerambathur, Erin J. Cram, Fradin, Frøkjaer-Jensen, Gerald, Ghazarian, Gibson, Gorelik, Green, Ishikawa, Jack E. Dixon, Jeff Bouffard, Johnson, Kamath, Karen Oegema, Kian-Yong Lee, Kim, Kimble, Koike, Koob, Kovacevic, Köppen, Leiser, Leiser, Levin, Lindberg, Mann, Manning, Minko, Mody, Nakamura, Paschinger, Petrella, Pollak, Pollard, Pulvirenti, Raine, Reinhart, Renat Khaliullin, Rolls, Salvi, Sievers, Simpson, Sreelatha, Tagliabracci, Tagliabracci, Tagliabracci, Takeuchi, Tseng, Vogel, Wang, Ward, Wen, Wewer, Xiao, Yue, Zhang, Zhou, Zhou   +70 more
core   +3 more sources

Medicago PhosphoProtein Database: a repository for Medicago truncatula phosphoprotein data

Frontiers in Plant Science, 2012
The ability of legume crops to fix atmospheric nitrogen via a symbiotic association with soil rhizobia makes them an essential component of many agricultural systems.
Christopher M. Rose, Muthusubramanian eVenkateshwaran, Paul A. Grimsrud, Michael S. Westphall, Michael R. Sussman, Joshua J. Coon, Joshua J. Coon, Jean-Michel eAné   +7 more
doaj   +1 more source

Proteome and phosphoproteome analysis of 2,4-epibrassinolide-mediated cold stress response in cucumber seedlings

Frontiers in Plant Science, 2023
The 2, 4-epibrassinolide (EBR) significantly increased plants cold tolerance. However, mechanisms of EBR in regulating cold tolerance in phosphoproteome and proteome levels have not been reported. The mechanism of EBR regulating cold response in cucumber
Mengdi Zhou, Mengdi Zhou, Yansu Li, Yan Yan, Lihong Gao, Chaoxing He, Jun Wang, Quan Yuan, Li Miao, Shuzhen Li, Qinghua Di, Xianchang Yu, Mintao Sun   +12 more
doaj   +1 more source

SILAC-based phosphoproteomics reveals an inhibitory role of KSR1 in p53 transcriptional activity via modulation of DBC1 [PDF]

, 2013
BACKGROUND We have previously identified kinase suppressor of ras-1 (KSR1) as a potential regulatory gene in breast cancer. KSR1, originally described as a novel protein kinase, has a role in activation of mitogen-activated protein kinases.
A Filipovic, AA Adjei, AJ Levine, B Vogelstein, C-Y Koo, CH Shen, CL Brooks, D Zhang, DP Xirodimas, DR Rhodes, F De Amicis, F Vikhanskaya, G Giamas, G Giamas, H Mi, H Vaziri, H Zhang, H Zhang, HR Xing, J Cox, J Cox, J Hu, J Lozano, J Stebbing, J Yuan, JA Goettel, JE Kim, JR Wisniewski, K Kornfeld, L C Lit, L Zannini, M Therrien, M Therrien, M Zafrullah, MN Laurent, R Brough, R Fujita, R Kolesnick, RL Kortum, S Matsuoka, T Rajakulendran, TE Thingholm, V Nin, W Zhao, WM Abida, Y Tang, Y Xu, Y Zhang   +47 more
core   +2 more sources

Quantitative phosphoproteomics of cytotoxic T cells to reveal Protein Kinase D 2 regulated networks [PDF]

, 2014
The focus of the present study was to characterize the phosphoproteome of cytotoxic T cells and to explore the role of the serine threonine kinase PKD2 (Protein Kinase D2) in the phosphorylation networks of this key lymphocyte population.
Azzam, Balagopalan, Beadling, Caenepeel, Chiang, Cornish, Cox, Cox, Dequiedt, Doreen A. Cantrell, Döppler, Eggers, Eiseler, Eiseler, Flotho, Franz-Wachtel, Fugmann, Grønborg, Hao, Hardie, Hausser, Hay, Huang, Hunter, Hutti, Huttlin, Jens L. Hukelmann, Juergen Goebel, Kajiho, Kalia, Kitao, Komander, Larghi, Malek, Marklund, María N. Navarro, Matthews, Matthews, Matthews, Mayya, Navarro, Navarro, Ng, Nhek, Nishikawa, Olayioye, Parra, Parra, Peterburs, Pipkin, Rey, Rozengurt, Ruperez, Seaman, Sinclair, Soares, Spitaler, Spratley, Tamas, Urso, Vizcaíno, Wang, Wang, Waugh, Weninger, Wood, Zarrouk, Zhou, Ziegler   +68 more
core   +3 more sources

Integrative features of the yeast phosphoproteome and protein-protein interaction map. [PDF]

PLoS Computational Biology, 2011
Following recent advances in high-throughput mass spectrometry (MS)-based proteomics, the numbers of identified phosphoproteins and their phosphosites have greatly increased in a wide variety of organisms.
Nozomu Yachie, Rintaro Saito, Naoyuki Sugiyama, Masaru Tomita, Yasushi Ishihama   +4 more
doaj   +1 more source