Results 51 to 60 of about 11,155,248 (357)

An allosteric switch between the activation loop and a c-terminal palindromic phospho-motif controls c-Src function

Nature Communications, 2023
Autophosphorylation controls the transition between discrete functional and conformational states in protein kinases, yet the structural and molecular determinants underlying this fundamental process remain unclear.
Hipólito Nicolás Cuesta-Hernández, Julia Contreras, Pablo Soriano-Maldonado, Jana Sánchez-Wandelmer, Wayland Yeung, Ana Martín-Hurtado, Inés G. Muñoz, Natarajan Kannan, Marta Llimargas, Javier Muñoz, Iván Plaza-Menacho   +10 more
doaj   +1 more source

Structural and dynamic determinants for highly selective RET kinase inhibition reveal cryptic druggability

Journal of Advanced Research, 2023
Introduction: The structural and dynamic determinants that confer highly selective RET kinase inhibition are poorly understood. Objectives: To explore the druggability landscape of the RET active site in order to uncover structural and dynamic ...
Moustafa A. Shehata, Julia Contreras, Ana Martín-Hurtado, Aurane Froux, Hossam Taha Mohamed, Ahmed A. El-Sherif, Iván Plaza-Menacho   +6 more
doaj   +1 more source

Role of Protein Phosphorylation in the Regulation of Cell Cycle and DNA-Related Processes in Bacteria

Frontiers in Microbiology, 2016
In all living organisms, the phosphorylation of proteins modulates various aspects of their functionalities. In eukaryotes, protein phosphorylation plays a key role in cell signaling, gene expression, and differentiation.
Transito Garcia-Garcia, S. Poncet, A. Derouiche, Lei Shi, I. Mijakovic, M. Noirot-Gros   +5 more
semanticscholar   +1 more source

Genome-wide analysis to predict protein sequence variations that change phosphorylation sites or their corresponding kinases [PDF]

, 2008
We define phosphovariants as genetic variations that change phosphorylation sites or their interacting kinases. Considering the essential role of phosphorylation in protein functions, it is highly likely that phosphovariants change protein functions and ...
Pamela Song, Kyu-Won Kim, Jong Hun Kim, Kyung-Soo Oh, Gil-Mi Ryu   +4 more
core  

Phosphorylation by Akt within the ST loop of AMPK-α1 down-regulates its activation in tumour cells [PDF]

, 2014
The insulin/IGF-1 (insulin-like growth factor 1)-activated protein kinase Akt (also known as protein kinase B) phosphorylates Ser487 in the ‘ST loop’ (serine/threonine-rich loop) within the C-terminal domain of AMPK-a1 (AMP-activated protein kinase-a1 ...
Leslie, Nicholas R., Leslie, Nicholas R.; id_orcid, Ross, Fiona A., Hardie, D. Grahame, Tibarewal, Priyanka, Gowans, Graeme J., Hawley, Simon A.   +6 more
core   +1 more source

Rab14 regulates the transport of human papillomavirus to the trans‐Golgi network for infectious cell entry

FEBS Letters, EarlyView.
This study reveals that the small GTPase Rab14 is necessary for human papillomavirus (HPV) infection and plays an essential role in the transport of virions to the trans‐Golgi network (TGN). HPV in the early endosome (EE), which harbors GTP‐bound Rab14, is transported to the TGN through the switch of Rab14 from its GTP‐bound to GDP‐bound form.
Yoshiyuki Ishii, Iwao Kukimoto
wiley   +1 more source

Corrigendum: Rapid alteration of protein phosphorylation during postmortem: implication in the study of protein phosphorylation

Scientific Reports, 2016
Protein phosphorylation is an important post-translational modification of proteins. Postmortem tissues are widely being utilized in the biomedical studies, but the effects of postmortem on protein phosphorylation have not been received enough attention.
Yifan Wang, Yan-Chong Zhang, Wen Hu, Shutao Xie, C. Gong, K. Iqbal, Fei Liu   +6 more
semanticscholar   +1 more source

Phosphoinositide-dependent protein kinase-1 (PDK1)-independent activation of the protein kinase C substrate, protein kinase D [PDF]

, 2007
Phosphoinoisitide dependent kinase l (PDK1) is proposed to phosphorylate a key threonine residue within the catalytic domain of the protein kinase C (PKC) superfamily that controls the stability and catalytic competence of these kinases.
Kelly, April P., Cantrell, Doreen A., Wood, C. David, Matthews, Sharon A.   +3 more
core   +1 more source

Microbiome−host proteostasis crosstalk—An emerging perspective on mechanisms and interventions toward healthy longevity

FEBS Letters, EarlyView.
Proteostasis and the gut microbiota play a key role in shaping host physiology. Microbiota‐derived metabolites, vitamins, and RNA modulate host proteostasis. Findings from model systems, including C. elegans, indicate microbes can either stabilize or disrupt host proteostasis.
Abhishek Anil Dubey, Maria Ermolaeva
wiley   +1 more source

Phosphorylation of Sli15 by Ipl1 is important for proper CPC localization and chromosome stability in Saccharomyces cerevisiae [PDF]

, 2014
The chromosomal passenger complex (CPC) is a key regulator of eukaryotic cell division, consisting of the protein kinase Aurora B/Ipl1 in association with its activator (INCENP/Sli15) and two additional proteins (Survivin/Bir1 and Borealin/Nbl1). Here we
David A Robinson, Robinson, David A., Corbishley, Stephen, Stark, Michael J. R., Vasso Makrantoni, Michael J R Stark, Makrantoni Vasso, Najma Rachidi, Morrice Nicholas A., Robinson David A., Corbishley Stephen J., Makrantoni, Vasso, Stephen J Corbishley, Stark Michael J. R., Nicholas A Morrice, Rachidi, Najma, Morrice, Nicholas A., Rachidi Najma   +17 more
core   +1 more source