Biosynthesis of polyketides by trans-AT polyketide synthases
EJN Helfrich, J Piel - Natural product reports, 2016 - pubs.rsc.org
Covering 2000 to June 2015 This review discusses the biosynthesis of natural products that
are generated by trans-AT polyketide synthases, a family of catalytically versatile enzymes …
are generated by trans-AT polyketide synthases, a family of catalytically versatile enzymes …
Functional diversity of protein phosphatase-1, a cellular economizer and reset button
H Ceulemans, M Bollen - Physiological reviews, 2004 - journals.physiology.org
Ceulemans, Hugo, and Mathieu Bollen. Functional Diversity of Protein Phosphatase-1, a
Cellular Economizer and Reset Button. Physiol Rev 84: 1–39, 2004; 10.1152/physrev …
Cellular Economizer and Reset Button. Physiol Rev 84: 1–39, 2004; 10.1152/physrev …
A machine learning-based chemoproteomic approach to identify drug targets and binding sites in complex proteomes
I Piazza, N Beaton, R Bruderer, T Knobloch… - Nature …, 2020 - nature.com
Chemoproteomics is a key technology to characterize the mode of action of drugs, as it
directly identifies the protein targets of bioactive compounds and aids in the development of …
directly identifies the protein targets of bioactive compounds and aids in the development of …
Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
Abstract Protein phosphatase 2A (PP2A) is a principal Ser/Thr phosphatase, the
deregulation of which is associated with multiple human cancers, Alzheimer's disease and …
deregulation of which is associated with multiple human cancers, Alzheimer's disease and …
Structural basis for protein phosphatase 1 regulation and specificity
The ubiquitous serine/threonine protein phosphatase 1 (PP1) regulates diverse, essential
cellular processes such as cell cycle progression, protein synthesis, muscle contraction …
cellular processes such as cell cycle progression, protein synthesis, muscle contraction …
Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
Y Xing, Y Xu, Y Chen, PD Jeffrey, Y Chao, Z Lin, Z Li… - Cell, 2006 - cell.com
The serine/threonine phosphatase protein phosphatase 2A (PP2A) plays an essential role in
many aspects of cellular functions and has been shown to be an important tumor …
many aspects of cellular functions and has been shown to be an important tumor …
Structural basis of protein phosphatase 1 regulation
M Terrak, F Kerff, K Langsetmo, T Tao, R Dominguez - Nature, 2004 - nature.com
The coordinated and reciprocal action of serine/threonine (Ser/Thr) protein kinases and
phosphatases produces transient phosphorylation, a fundamental regulatory mechanism for …
phosphatases produces transient phosphorylation, a fundamental regulatory mechanism for …
Substrate and phosphorylation site selection by phosphoprotein phosphatases
H Nguyen, AN Kettenbach - Trends in Biochemical Sciences, 2023 - cell.com
Dynamic protein phosphorylation and dephosphorylation are essential regulatory
mechanisms that ensure proper cellular signaling and biological functions. Deregulation of …
mechanisms that ensure proper cellular signaling and biological functions. Deregulation of …
Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites
MJ Ragusa, B Dancheck, DA Critton… - Nature structural & …, 2010 - nature.com
The serine/threonine protein phosphatase 1 (PP1) dephosphorylates hundreds of key
biological targets. PP1 associates with≥ 200 regulatory proteins to form highly specific …
biological targets. PP1 associates with≥ 200 regulatory proteins to form highly specific …
Molecular basis for TPR domain‐mediated regulation of protein phosphatase 5
J Yang, SM Roe, MJ Cliff, MA Williams… - The EMBO …, 2005 - embopress.org
Protein phosphatase 5 (Ppp5) is a serine/threonine protein phosphatase comprising a
regulatory tetratricopeptide repeat (TPR) domain N‐terminal to its phosphatase domain …
regulatory tetratricopeptide repeat (TPR) domain N‐terminal to its phosphatase domain …