Results 1 to 10 of about 133,461 (307)

Correlated mutation analysis on the catalytic domains of serine/threonine protein kinases. [PDF]

open access: goldPLoS ONE, 2009
BACKGROUND:Protein kinases (PKs) have emerged as the largest family of signaling proteins in eukaryotic cells and are involved in every aspect of cellular regulation.
Feng Xu   +6 more
doaj   +6 more sources

The juxtamembrane domain of StkP is phosphorylated and influences cell division in Streptococcus pneumoniae [PDF]

open access: yesmBio
Eukaryotic-like membrane Ser/Thr protein kinases play a pivotal role in different aspects of bacterial physiology. In contrast to the diversity of their extracellular domains, their cytoplasmic catalytic domains are highly conserved.
Mélisse Hamidi   +9 more
doaj   +2 more sources

Bioinformatic search of plant microtubule-and cell cycle related serine-threonine protein kinases [PDF]

open access: goldBMC Genomics, 2010
A bioinformatic search was carried for plant homologues of human serine-threonine protein kinases involved in regulation of cell division and microtubule protein phosphorylation (SLK, PAK6, PAK7, MARK1, MAST2, TTBK1, TTBK2, AURKA, PLK1, PLK4 and PASK). A
Nyporko Alexey   +6 more
doaj   +2 more sources

The regulatory impact of serine/threonine-specific protein phosphorylation among cyanobacteria [PDF]

open access: yesFrontiers in Plant Science
Cyanobacteria are the only prokaryotes capable of performing oxygenic photosynthesis. To thrive under environmental fluctuations, photosynthesis and metabolic activities needs to be adjusted. Previous studies showed that the acclimation of primary carbon
Thomas Barske, Martin Hagemann
doaj   +2 more sources

Revealing phosphorylation regulatory networks during embryogenesis of honey bee worker and drone (Apis mellifera)

open access: yesFrontiers in Cell and Developmental Biology, 2022
Protein phosphorylation is known to regulate a comprehensive scenario of critical cellular processes. However, phosphorylation-mediated regulatory networks in honey bee embryogenesis are mainly unknown.
Beibei Ma, Chuan Ma, Jianke Li, Yu Fang
doaj   +1 more source

Association between intrinsic disorder and serine/threonine phosphorylation in Mycobacterium tuberculosis [PDF]

open access: yesPeerJ, 2015
Serine/threonine phosphorylation is an important mechanism that is involved in the regulation of protein function. In eukaryotes, phosphorylation occurs predominantly in intrinsically disordered regions of proteins.
Gajinder Pal Singh
doaj   +2 more sources

PeSTK db a comprehensive data repository of Probiotic Serine Threonine kinases

open access: yesScientific Data, 2022
Measurement(s) Serine threonine protein sequences of probiotic microbes Technology Type(s) Softwares uploading and downloading of sequences from various public sources Factor Type(s) Serine threonine kinases of Probiotic microbes Sample Characteristic ...
Dhanashree Lokesh   +2 more
doaj   +1 more source

Protein Tyrosine and Serine/Threonine Phosphorylation in Oral Bacterial Dysbiosis and Bacteria-Host Interaction

open access: yesFrontiers in Cellular and Infection Microbiology, 2022
The human oral cavity harbors approximately 1,000 microbial species, and dysbiosis of the microflora and imbalanced microbiota-host interactions drive many oral diseases, such as dental caries and periodontal disease.
Liang Ren   +3 more
doaj   +1 more source

Phosphorylation of the chromatin binding domain of KSHV LANA. [PDF]

open access: yesPLoS Pathogens, 2012
The Kaposi sarcoma associated herpesvirus (KSHV) latency associated nuclear antigen (LANA) is expressed in all KSHV associated malignancies and is essential for maintenance of KSHV genomes in infected cells.
Crystal Woodard   +12 more
doaj   +1 more source

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

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