Results 51 to 60 of about 209,848 (307)

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

FEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes, Guilherme M. Azevedo, Amanda P. Barcellos, Diana Bahia   +3 more
wiley   +1 more source

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

Crosstalk between the ribosome quality control‐associated E3 ubiquitin ligases LTN1 and RNF10

FEBS Letters, EarlyView.
Loss of the E3 ligase LTN1, the ubiquitin‐like modifier UFM1, or the deubiquitinating enzyme UFSP2 disrupts endoplasmic reticulum–ribosome quality control (ER‐RQC), a pathway that removes stalled ribosomes and faulty proteins. This disruption may trigger a compensatory response to ER‐RQC defects, including increased expression of the E3 ligase RNF10 ...
Yuxi Huang, Satoshi Hashimoto, Sota Ito, Chisato Kikuguchi, Miho Hoshi, Kiyoshi Yamaguchi, Yoichi Furukawa, Toru Suzuki, Toshifumi Inada   +8 more
wiley   +1 more source

Structure of substrate-bound SMG1-8-9 kinase complex reveals molecular basis for phosphorylation specificity

eLife, 2020
PI3K-related kinases (PIKKs) are large Serine/Threonine (Ser/Thr)-protein kinases central to the regulation of many fundamental cellular processes.
Lukas M Langer, Yair Gat, Fabien Bonneau, Elena Conti   +3 more
doaj   +1 more source

Kinase Targeted Anticancer Agents: A Perspective

NUST Journal of Natural Sciences, 2022
The phosphate group present in the ATP (adenosine triphosphate) is transferred to the hydroxy group-containing tyrosine, serine, or threonine residue by the protein kinases encoded in the human genome. Till now, a large number of these kinases have been
Shannelle Diana Habániková, Rubina Dad, Chandra S Azad   +2 more
doaj   +1 more source

Tv-RIO1 – an atypical protein kinase from the parasitic nematode Trichostrongylus vitrinus [PDF]

, 2008
Background: Protein kinases are key enzymes that regulate a wide range of cellular processes, including cell-cycle progression, transcription, DNA replication and metabolic functions. These enzymes catalyse the transfer of phosphates to serine, threonine
Gasser, Robin B., Hu, Min, LaRonde-LeBlanc, Nicole, Sternberg, Paul W.   +3 more
core   +6 more sources

Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation

FEBS Letters, EarlyView.
Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe, Tanmay Kumar Mohanty, Rashna Bhandari, Dorothea Fiedler   +3 more
wiley   +1 more source

Phosphorylation and regulation of group II metabotropic glutamate receptors (mGlu2/3) in neurons

Frontiers in Cell and Developmental Biology, 2022
Group II metabotropic glutamate (mGlu) receptors (mGlu2/3) are Gαi/o-coupled receptors and are primarily located on presynaptic axonal terminals in the central nervous system.
Li-Min Mao, Nirav Mathur, Tayyibah Mahmood, Sri Rajan, Xiang-Ping Chu, John Q. Wang, John Q. Wang   +6 more
doaj   +1 more source

Erythropoietin-induced serine 727 phosphorylation of STAT3 in erythroid cells is mediated by a MEK-, ERK-, and MSK1-dependent pathway [PDF]

, 2003
Objective. Erythropoietin (EPO) is a key regulator of erythropoiesis, playing a role in both the proliferation and differentiation of erythroid cells.
Bieber, Boer, Chung, Decker, Gabrilove, Gonzalez, Goodnough, Gotoh, Haq, Jain, Jain, Jonk, Kaptein, Kirito, Kirito, Kirito, Lim, Millot, Miyazaki, Mulcahy, Ng, Schuringa, Schuringa, Schuringa, Smithgall, Socolovsky, Teglund, Tilbrook, Turkson, Watowich, Wen, Wen, Woetmann, Yokogami, Youssoufian, Yu, Zhang   +36 more
core   +1 more source

Cell wall target fragment discovery using a low‐cost, minimal fragment library

FEBS Letters, EarlyView.
LoCoFrag100 is a fragment library made up of 100 different compounds. Similarity between the fragments is minimized and 10 different fragments are mixed into a single cocktail, which is soaked to protein crystals. These crystals are analysed by X‐ray crystallography, revealing the binding modes of the bound fragment ligands.
Kaizhou Yan, Mathew Stanley, Olawale Raimi, Andrew T. Ferenbach, Helge C Dorfmueller, Daan M. F. van Aalten   +5 more
wiley   +1 more source