Results 21 to 30 of about 2,399,730 (304)

Adipose tissue protein phosphatase inhibitor‐2 [PDF]

open access: yesEuropean Journal of Biochemistry, 1988
Rat fat cells contain three species of spontaneously active inhibitor proteins of protein phosphatase 1, as resolved by SDS‐PAGE, with apparent molecular masses of 40 kDa, 33 kDa and 28 kDa respectively. The 33‐kDa, thermostable inhibitor was highly purified from bovine adipose tissue and shown to be very similar to inhibitor‐2 of skeletal muscle.
openaire   +2 more sources

The protein phosphatases involved in cellular regulation. Identification of the inhibitor-2 phosphatases in rabbit skeletal muscle [PDF]

open access: yesEuropean Journal of Biochemistry, 1984
Inhibitor-2, purified by an improved procedure, was used to identify protein phosphatases capable of catalysing its dephosphorylation. The results showed that, under our experimental conditions, protein phosphatases-1, 2A and 2B were the only significant protein phosphatases in rabbit skeletal muscle extracts acting on this substrate.
N K, Tonks, P, Cohen
openaire   +2 more sources

SH2 domain‐containing protein tyrosine phosphatase‐2 is enriched in eyelid specimens of rosacea

open access: yesSkin Health and Disease, 2023
Background Rosacea is a cutaneous disease that may secondarily affect the ocular surface. Due to the vision threatening, cosmetic, psychological, and work productivity impact, the identification of cellular targets that govern rosacea would enhance our ...
Apoorv Chebolu   +4 more
doaj   +1 more source

Modeling (not so) rare developmental disorders associated with mutations in the protein-tyrosine phosphatase SHP2

open access: yesFrontiers in Cell and Developmental Biology, 2022
Src homology region 2 (SH2)-containing protein tyrosine phosphatase 2 (SHP2) is a highly conserved protein tyrosine phosphatase (PTP), which is encoded by PTPN11 and is indispensable during embryonic development.
Maja Solman   +3 more
doaj   +1 more source

T cell-specific constitutive active SHP2 enhances T cell memory formation and reduces T cell activation

open access: yesFrontiers in Immunology, 2022
Upon antigen recognition by the T cell receptor (TCR), a complex signaling network orchestrated by protein-tyrosine kinases (PTKs) and protein-tyrosine phosphatases (PTPs) regulates the transmission of the extracellular signal to the nucleus. The role of
Clemens Cammann   +17 more
doaj   +1 more source

The protein tyrosine phosphatase Shp-2 regulates RhoA activity [PDF]

open access: yesCurrent Biology, 2000
Remodeling of filamentous actin into distinct arrangements is precisely controlled by members of the Rho family of small GTPases [1]. A well characterized member of this family is RhoA, whose activation results in reorganization of the cytoskeleton into thick actin stress fibers terminating in integrin-rich focal adhesions [2].
Schoenwaelder, Simone M.   +5 more
openaire   +2 more sources

Identification of a protein phosphatase-1/phospholamban complex that is regulated by cAMP-dependent phosphorylation.

open access: yesPLoS ONE, 2013
In human and experimental heart failure, the activity of the type 1 phosphatase is significantly increased, associated with dephosphorylation of phospholamban, inhibition of the sarco(endo)plasmic reticulum Ca(2+) transport ATPase (SERCA2a) and depressed
Elizabeth Vafiadaki   +3 more
doaj   +1 more source

Purification and characterization of a protein inhibitor from rat liver that inhibits type 1 protein phosphatase when 3-hydroxy-3-methylglutaryl CoA reductase is the substrate.

open access: yesJournal of Lipid Research, 1990
A protein inhibitor of HMG-CoA reductase phosphatase activity from rat liver was purified to homogeneity. The protein was purified 4,000-fold with an overall yield of 4%. The purified protein had a molecular mass of 31 kDa.
D Serra, G Asins, FG Hegardt
doaj   +1 more source

Targeting protein phosphatases in cancer immunotherapy and autoimmune disorders

open access: yesNature reviews. Drug discovery, 2023
Protein phosphatases act as key regulators of multiple important cellular processes and are attractive therapeutic targets for various diseases. Although extensive effort has been dedicated to phosphatase-targeted drug discovery, early expeditions for ...
Stephanie M Stanford, N. Bottini
semanticscholar   +1 more source

Activity of protein phosphatases against initiation factor-2 and elongation factor-2 [PDF]

open access: yesBiochemical Journal, 1990
The protein phosphatases active against phosphorylase a, elongation factor-2 (EF-2) and the alpha-subunit of initiation factor-2 (eIF-2) [eIF-2(alpha P)] were studied in extracts of rabbit reticulocytes. Swiss-mouse 3T3 fibroblasts and rat hepatocytes, by use of the specific phosphatase inhibitors okadaic acid and inhibitor proteins-1 and -2.
N T, Redpath, C G, Proud
openaire   +2 more sources

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