Results 21 to 30 of about 212,467 (329)

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

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

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

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

Phosphoregulators:protein kinases and protein phosphatases of mouse [PDF]

open access: yes, 2003
With the completion of the human and mouse genome sequences, the task now turns to identifying their encoded transcripts and assigning gene function. In this study, we have undertaken a computational approach to identify and classify all of the protein ...
  +7 more
core   +2 more sources

A Serine/Threonine Protein Kinase fromMycobacterium tuberculosis [PDF]

open access: yesEuropean Journal of Biochemistry, 1997
Genomic DNA sequencing in the vicinity of thepstA‐1gene fromMycobacterium tuberculosisallowed us to clone, sequence and identify a gene encoding a 70‐kDa protein. The size of the protein was confirmed byin vitrocoupled transcription/translation. Its N‐terminal domain shows extensive sequence similarity with the catalytic domain of eukaryotic serine ...
Peirs, Priska   +4 more
openaire   +3 more sources

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

Computational identification of signalling pathways in Plasmodium falciparum [PDF]

open access: yes, 2011
Malaria is one of the world’s most common and serious diseases causing death of about 3 million people each year. Its most severe occurrence is caused by the protozoan Plasmodium falciparum.
Adebiyi, E. F.   +4 more
core   +2 more sources

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