Results 111 to 120 of about 205,532 (202)

Abnormalities affecting tyrosine kinase signalling in atypical myeloproliferative disorders [PDF]

open access: yes, 2009
The myeloproliferative disorders (MPDs) are a group of haematopoietic stem cell diseases, characterised by proliferation of one or more cells of the myeloid lineage.
Hidalgo-Curtis, Claire
core   +1 more source

T cell development and T cell responses in mice with mutations affecting tyrosines 292 or 315 of the ZAP-70 protein tyrosine kinase [PDF]

open access: yes, 2001
After stimulation of the T cell receptor (TCR), the tyrosine residues 292 and 315 in interdomain B of the protein tyrosine kinase ZAP-70 become phosphorylated and plausibly function as docking sites for Cbl and Vav1, respectively. The two latter proteins
Magnan, A   +38 more
core   +1 more source

The cleavage mode of the Cre recombinase [PDF]

open access: yes, 2000
grantor: University of TorontoThe Cre protein, encoded by the bacteriophage P1, and the Flp protein, encoded by the 2 [mu]M plasmid found in budding yeast, belong to the Integrase family of site-specific recombinases.
Shaikh, A. C.
core   +1 more source

Tyrosine-Based Dual-Functional Interface for Trapping and On-Site Photo-Induced Covalent Immobilization of Proteins

open access: yes, 2022
Tyrosine, a simple and well-available natural amino acid, is featured by the small size of the compound that contains multiple reactive groups. This study developed an efficient bioconjugation strategy using tyrosine-based dual-functional interfaces ...
Xu Xiang   +13 more
core   +1 more source

The Peutz-Jeghers kinase LKB1 suppresses polyp growth from intestinal cells of a proglucagon-expressing lineage in mice

open access: yesDisease Models & Mechanisms, 2014
Liver kinase B1 (LKB1; also known as STK11) is a serine/threonine kinase and tumour suppressor that is mutated in Peutz-Jeghers syndrome (PJS), a premalignant syndrome associated with the development of gastrointestinal polyps.
Sagen Zac-Varghese   +8 more
doaj   +1 more source

Angiotensin II impairs endothelial function via tyrosine phosphorylation of the endothelial nitric oxide synthase [PDF]

open access: yes, 2009
Proline-rich tyrosine kinase 2 (PYK2) can be activated by angiotensin II (Ang II) and reactive oxygen species. We report that in endothelial cells, Ang II enhances the tyrosine phosphorylation of endothelial NO synthase (eNOS) in an AT1-, H2O2-, and PYK2-
Loot, Annemarieke E.   +7 more
core   +1 more source

A NaV1.8FlpO mouse enabling selective intersectional targeting of low threshold C fiber mechanoreceptors and nociceptors

open access: yesFrontiers in Molecular Neuroscience
Genetic targeting of select populations of cells in the mouse nervous system is often hampered by a lack of selectivity, as candidate genes for such targeting are commonly expressed by multiple cell populations, also in the same region.
John C. Y. Chen   +5 more
doaj   +1 more source

Ptpn11 Deletion in CD4+ Cells Does Not Affect T Cell Development and Functions but Causes Cartilage Tumors in a T Cell-Independent Manner

open access: yesFrontiers in Immunology, 2017
The ubiquitously expressed tyrosine phosphatase Src homology region 2 domain-containing phosphatase-2 (SHP-2, encoded by Ptpn11) is required for constitutive cellular processes including proliferation, differentiation, and the regulation of immune ...
S. M. Shahjahan Miah   +7 more
doaj   +1 more source

AMPK-α1 or AMPK-α2 Deletion in Smooth Muscles Does Not Affect the Hypoxic Ventilatory Response or Systemic Arterial Blood Pressure Regulation During Hypoxia

open access: yesFrontiers in Physiology, 2018
The hypoxic ventilatory response (HVR) is markedly attenuated by AMPK-α1 deletion conditional on the expression of Cre-recombinase in tyrosine hydroxylase (TH) expressing cells, precipitating marked increases in apnea frequency and duration.
Sandy MacMillan, A. Mark Evans
doaj   +1 more source

Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases [PDF]

open access: yes, 2009
Background: The c-Cbl-associated protein (CAP), also known as ponsin, localizes to focal adhesions and stress fibers and is involved in signaling events.
Tomasovic, Ana   +11 more
core   +1 more source

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