Results 11 to 20 of about 209,848 (307)

Identification of the protein kinases Pyk3 and Phg2 as regulators of the STATc-mediated response to hyperosmolarity [PDF]

open access: yes, 2014
Cellular adaptation to changes in environmental osmolarity is crucial for cell survival. In Dictyostelium, STATc is a key regulator of the transcriptional response to hyperosmotic stress. Its phosphorylation and consequent activation is controlled by two
A Kortholt   +37 more
core   +13 more sources

Molecular Basis for Ser/Thr Specificity in PKA Signaling

open access: yesCells, 2020
cAMP-dependent protein kinase (PKA) is the major receptor of the second messenger cAMP and a prototype for Ser/Thr-specific protein kinases. Although PKA strongly prefers serine over threonine substrates, little is known about the molecular basis of this
Matthias J. Knape   +7 more
doaj   +1 more source

Mycobacterium tuberculosis Serine/Threonine Protein Kinases [PDF]

open access: yesMicrobiology Spectrum, 2014
ABSTRACT The Mycobacterium tuberculosis genome encodes 11 serine/threonine protein kinases (STPKs). A similar number of two-component systems are also present, indicating that these two signal transduction mechanisms are both important in the adaptation of this bacterial pathogen to its environment. The
Sladjana, Prisic, Robert N, Husson
openaire   +2 more sources

A framework for classification of prokaryotic protein kinases. [PDF]

open access: yesPLoS ONE, 2010
BACKGROUND: Overwhelming majority of the Serine/Threonine protein kinases identified by gleaning archaeal and eubacterial genomes could not be classified into any of the well known Hanks and Hunter subfamilies of protein kinases.
Nidhi Tyagi   +2 more
doaj   +1 more source

Salt-inducible kinases (SIKs) regulate TGFβ-mediated transcriptional and apoptotic responses [PDF]

open access: yes, 2020
The signalling pathways initiated by members of the transforming growth factor-β (TGFβ) family of cytokines control many metazoan cellular processes, including proliferation and differentiation, epithelial-mesenchymal transition (EMT) and apoptosis. TGFβ
A Rojas-Fernandez   +63 more
core   +2 more sources

Tyrosine phosphorylation of the BRI1 receptor kinase occurs via a posttranslational modification and is activated by the juxtamembrane domain

open access: yesFrontiers in Plant Science, 2012
In metazoans, receptor kinases control many essential processes related to growth and development and response to the environment. The receptor kinases in plants and animals are structurally similar but evolutionarily distinct and thus while most animal ...
Man-Ho eOh   +3 more
doaj   +1 more source

Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments [PDF]

open access: yes, 2018
Reversible phosphorylation is a key mechanism that regulates many cellular processes in prokaryotes and eukaryotes. In prokaryotes, signal transduction includes two-component signaling systems, which involve a membrane sensor histidine kinase and a ...
Janczarek, Monika   +3 more
core   +1 more source

Proteínas quinases: características estruturais e inibidores químicos Kinase protein: structural features and chemical inhibitors

open access: yesQuímica Nova, 2009
Protein kinases are one of the largest protein families and they are responsible for regulation of a great number of signal transduction pathways in cells, through the phosphorylation of serine, threonine, or tyrosine residues.
Bárbara V. Silva   +3 more
doaj   +1 more source

Role of serine/threonine protein phosphatase PrpN in the life cycle of Bacillus anthracis.

open access: yesPLoS Pathogens, 2022
Reversible protein phosphorylation at serine/threonine residues is one of the most common protein modifications, widely observed in all kingdoms of life.
Aakriti Gangwal   +10 more
doaj   +1 more source

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

open access: yes, 2014
The insulin/IGF-1 (insulin-like growth factor 1)-activated protein kinase Akt (also known as protein kinase B) phosphorylates Ser(487) in the ‘ST loop’ (serine/threonine-rich loop) within the C-terminal domain of AMPK-α1 (AMP-activated protein kinase-α1),
Chen   +53 more
core   +4 more sources

Home - About - Disclaimer - Privacy