Results 31 to 40 of about 41,275 (256)

Roles of Histidine Kinases and Histidine Phosphatases in Cancer

open access: yesChinese Journal of Lung Cancer, 2021
Phosphorylation is the most common and important post-translational modification of proteins, which plays an important role in the regulation of cell proliferation, differentiation, development and metabolism, and is closely related to the tumorigenesis ...
Yafang DONG   +3 more
doaj   +1 more source

A loss-of-function screen for phosphatases that regulate neurite outgrowth identifies PTPN12 as a negative regulator of TrkB tyrosine phosphorylation. [PDF]

open access: yesPLoS ONE, 2013
Alterations in function of the neurotrophin BDNF are associated with neurodegeneration, cognitive decline, and psychiatric disorders. BDNF promotes axonal outgrowth and branching, regulates dendritic tree morphology and is important for axonal ...
Malene Ambjørn   +8 more
doaj   +1 more source

α,α-Difluoro-β-ketophosphonates on a tetraazamacrocyclic platform: Synthesis and inhibitory activity against protein tyrosine phosphatases

open access: yesДоповiдi Нацiональної академiї наук України
The present study offers a new approach for designing inhibitors of protein tyrosine phosphatases. We have synthesized the cyclam derivatives with α,α-difluoro-β-ketophosphonate fragments covalently attached to tetraazamacrocyclic scaffold, which is ...
D. I. Khavrienko   +8 more
doaj   +1 more source

Interaction of kinase-interaction-motif protein tyrosine phosphatases with the mitogen-activated protein kinase ERK2. [PDF]

open access: yesPLoS ONE, 2014
The mitogen-activation protein kinase ERK2 is tightly regulated by multiple phosphatases, including those of the kinase interaction motif (KIM) PTP family (STEP, PTPSL and HePTP).
Dana M Francis   +4 more
doaj   +1 more source

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

open access: yesFEBS 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   +3 more
wiley   +1 more source

Regulatory Functions of Protein Tyrosine Phosphatase Receptor Type O in Immune Cells

open access: yesFrontiers in Immunology, 2021
The members of the protein tyrosine phosphatase (PTP) family are key regulators in multiple signal transduction pathways and therefore they play important roles in many cellular processes, including immune response.
Feiling Xie   +7 more
doaj   +1 more source

Organizing the interface—Plasma membrane architecture and receptor dynamics in virus‐cell interactions

open access: yesFEBS Letters, EarlyView.
Plasma membranes contain dynamic nanoscale domains that organize lipids and receptors. Because viruses operate at similar scales, this architecture shapes early infection steps, including attachment, receptor engagement, and entry. Using influenza A virus and HIV‐1 as examples, we highlight how receptor nanoclusters, multivalent glycan interactions ...
Jan Schlegel, Christian Sieben
wiley   +1 more source

Hereditable variants of classical protein tyrosine phosphatase genes: Will they prove innocent or guilty?

open access: yesFrontiers in Cell and Developmental Biology, 2023
Protein tyrosine phosphatases, together with protein tyrosine kinases, control many molecular signaling steps that control life at cellular and organismal levels. Impairing alterations in the genes encoding the involved proteins is expected to profoundly
Wiljan J. A. J. Hendriks   +3 more
doaj   +1 more source

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates

open access: yesFEBS Letters, EarlyView.
Inositol pyrophosphates are energy‐rich signaling molecules that perform critical functions in cells. Three different families of phosphatases hydrolyze the β phosphate of the inositol pyrophosphate molecules: two have narrow specificities and one is promiscuous.
Ronda J. Rolfes
wiley   +1 more source

ABL kinase‐dependent phosphorylation of SH proteins promotes their direct interaction with CRK family SH2 domains

open access: yesFEBS Letters, EarlyView.
CT10 regulator of kinase (CRK) and CRK‐Like (CRKL) are signaling adaptors driving cell adhesion, motility, differentiation, and proliferation. SH2‐domain containing (SH) proteins are enriched in YXXP motifs which when phosphorylated create preferred binding sites for CRK family SH2 domains.
Phoebe M. Cousens   +8 more
wiley   +1 more source

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