Results 251 to 260 of about 44,229 (291)

Interplay of Ser273 Phosphorylation and K268 and K293 Acetylation in PPARγ: Implications for PPARγ Activation

Proteins: Structure, Function, and Bioinformatics, EarlyView.
ABSTRACT Post‐translational modifications (PTMs) play a critical role in regulating the transcriptional activity of PPARγ, a nuclear receptor central to glucose and lipid homeostasis. Among these, lysine acetylation at K268 and K293 and phosphorylation at S273 are particularly relevant to insulin sensitivity.
Caique Camargo Malospirito, Marieli Mariano Gonçalves Dias, Gabriel Ernesto Jara, Thayná Mendonça Avelino, Giovanna Blazutti Elias, Paulo Sergio Lopes de Oliveira, Ana Carolina Migliorini Figueira   +6 more
wiley   +1 more source

Structural Insights Into the Function of Leishmania major Adenylosuccinate Lyase

Proteins: Structure, Function, and Bioinformatics, EarlyView.
ABSTRACT One of several intriguing aspects of kinetoplastid biochemistry is the complete dependence on host purines and purine recycling due to the lack of a de novo purine biosynthesis pathway. Adenylosuccinate lyase (ASL, EC 4.3.2.2) is a key enzyme in the purine synthesis pathway responsible for the conversion of adenylosuccinate into adenosine ...
Ivan R. e Silva, Monique Mantovani, Maria E. S. D. Lino, Aline O. Albuquerque, João H. M. da Silva, Ronaldo A. P. Nagem, Adriana L. Rojas, Geraldo R. Sartori, Eduardo Horjales, David Campbell, Otavio H. Thiemann   +10 more
wiley   +1 more source

Dehydrocostus Lactone Suppresses Hepatocellular Carcinoma by Inhibiting Protein Tyrosine Kinase‐7 Mediated β‐Catenin Signaling

Phytotherapy Research, EarlyView.
Schematic summary of the experimentally supported mechanism of DHL in hepatocellular carcinoma. Dehydrocostus lactone (DHL), a sesquiterpene lactone derived from Aucklandia lappa, directly engages protein tyrosine kinase 7 (PTK7), as supported by molecular docking, CETSA, and DARTS assays.
Xiwen Fan, Junhui Li, Yu Qiao, Yuwen Zhong, Xuecheng Ge, Yaoshuai Zhang, Zishu Wang, Feng Qian, Weixin Ren   +8 more
wiley   +1 more source

AKAP2 is required for assembly of cytoskeletal signaling complexes that promote growth and metastasis of triple-negative breast cancer. [PDF]

J Biol Chem
Rosenthal KJ, Felix-Sanchez P, Forbush K, Rhoads N, Kang M, Vicente JJ, Smith FD, Wordeman L, Ong SE, Cheung KJ, Scott JD.   +10 more
europepmc   +1 more source

Canonical and Alternative Pathways (Insulin and Exercise) of GLUT4 Synthesis, Signaling, Intracellular Clustering, and Recruitment to the Plasma Membrane. [PDF]

Int J Mol Sci
Ramos-Jiménez A, Rubio-Valles M, Guereca-Arvizuo J, Juárez-Oropeza MA, Ramos-Hernández JA, Chávez-Guevara IA, González-Rodríguez E, Moreno-Brito V, Hernández Torres RP.   +8 more
europepmc   +1 more source

Research progress on the interaction mechanisms and functions between exosomes and the cytoskeleton. [PDF]

Front Cell Dev Biol
Yang S, Zhang X, Chen B, Kou H, Lai L, Liu H, Xu Y, Sun Y.   +7 more
europepmc   +1 more source

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A-kinase anchoring protein targeting of protein kinase A in the heart

Journal of Molecular and Cellular Cardiology, 2004
There is increasing evidence that subcellular targeting of signaling molecules is an important means of regulating the protein kinase A (PKA) pathway. Subcellular organization of the signaling molecules in the PKA pathway insures that a signal initiated at the receptor level is transferred efficiently to a PKA substrate eliciting some cellular response.
Mary A Russell, Meredith Bond
exaly   +3 more sources

A-kinase anchoring proteins: protein kinase A and beyond

Current Opinion in Cell Biology, 2000
Compartmentalization of kinases and phosphatases is a key determinant in the specificity of second messenger mediated signaling events. Localization of the cAMP-dependent protein kinase (PKA) and other signaling enzymes is mediated by interaction with A-kinase anchoring proteins (AKAPs).
A S, Edwards, J D, Scott
openaire   +2 more sources

The biological functions of A-kinase anchor proteins.

Journal of molecular biology, 2001
cAMP-dependent protein kinase is targeted to discrete subcellular locations by a family of specific anchor proteins (A-kinase anchor proteins, AKAPs). Localization recruits protein kinase A (PKA) holoenzyme close to its substrate/effector proteins, directing and amplifying the biological effects of cAMP signaling.AKAPs include two conserved structural ...
FELICIELLO, ANTONIO, GOTTESMAN M. E., AVVEDIMENTO, VITTORIO ENRICO   +2 more
openaire   +3 more sources

Kinase-anchoring proteins in ciliary signal transduction

Biochemical Journal, 2021
Historically, the diffusion of chemical signals through the cell was thought to occur within a cytoplasmic soup bounded by the plasma membrane. This theory was predicated on the notion that all regulatory enzymes are soluble and moved with a Brownian motion. Although enzyme compartmentalization was initially rebuffed by biochemists as a ‘last refuge of
Janani Gopalan, Linda Wordeman, John D. Scott   +2 more
openaire   +2 more sources