Member of the European Molecular Biology Organization (EMBO)
His primary areas of study are Cell biology, Biochemistry, Protein structure, Genetics and GTPase. His DNA damage research extends to the thematically linked field of Cell biology. His study in Binding selectivity and Phosphorylation falls under the purview of Biochemistry.
His Protein structure research integrates issues from Peptide library, Peptide sequence, Enzyme inhibitor and Binding site. The GTPase study combines topics in areas such as Small G Protein, GTP' and G protein. His Plasma protein binding study incorporates themes from Phosphoserine and PLK1.
Stephen J. Smerdon mainly focuses on Biochemistry, Cell biology, Molecular biology, Phosphorylation and Stereochemistry. When carried out as part of a general Biochemistry research project, his work on Plasma protein binding, Protein kinase A and Phosphoserine is frequently linked to work in Mycobacterium tuberculosis, therefore connecting diverse disciplines of study. Stephen J. Smerdon has researched Phosphoserine in several fields, including Polo-like kinase and Binding selectivity.
His biological study spans a wide range of topics, including G2-M DNA damage checkpoint, Chromatin, DNA damage and DNA repair. His research integrates issues of R2TP complex, Protein subunit and Kinase in his study of Phosphorylation. His research in Stereochemistry intersects with topics in Myoglobin, Metmyoglobin, Crystallography, 14-3-3 protein and Hemeprotein.
The scientist’s investigation covers issues in Cell biology, Biochemistry, Molecular biology, DNA repair and Phosphorylation. He has included themes like Nuclear export signal, Ubiquitin and DNA damage in his Cell biology study. His Allosteric regulation, Phosphopeptide and Poly-ADP-Ribose Binding Proteins study, which is part of a larger body of work in Biochemistry, is frequently linked to ATP phosphoribosyltransferase and XRCC1, bridging the gap between disciplines.
Stephen J. Smerdon studied Molecular biology and RNA that intersect with Transcription and Nucleolus. His DNA repair research is multidisciplinary, relying on both Chromatin, Casein kinase 1 and DNA-binding protein. His Phosphorylation study combines topics from a wide range of disciplines, such as Hippo signaling pathway, Signal transduction, Kinase and Mitosis.
Stephen J. Smerdon mainly investigates Cell biology, Molecular biology, Kinase, Phosphorylation and Plasma protein binding. Many of his studies on Cell biology involve topics that are commonly interrelated, such as IκB kinase. In his study, which falls under the umbrella issue of Molecular biology, Nucleolus and DNA damage is strongly linked to RNA.
The subject of his Kinase research is within the realm of Biochemistry. His work carried out in the field of Phosphorylation brings together such families of science as Binding domain, Scaffold protein, Signal transduction and Mitosis. His studies in Plasma protein binding integrate themes in fields like Ribonucleoprotein, RNA polymerase III and Messenger RNA, RNA-binding protein.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
The structural basis for 14-3-3:phosphopeptide binding specificity.
Michael B Yaffe;Katrin Rittinger;Stefano Volinia;Paul R Caron.
MDC1 Directly Binds Phosphorylated Histone H2AX to Regulate Cellular Responses to DNA Double-Strand Breaks
Manuel Stucki;Julie A. Clapperton;Duaa Mohammad;Michael B. Yaffe.
The ankyrin repeat: a diversity of interactions on a common structural framework.
Steven G Sedgwick;Stephen J Smerdon.
Trends in Biochemical Sciences (1999)
The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain.
Andrew E.H. Elia;Peter Rellos;Lesley F. Haire;Jerry W. Chao.
Structural Analysis of 14-3-3 Phosphopeptide Complexes Identifies a Dual Role for the Nuclear Export Signal of 14-3-3 in Ligand Binding
Katrin Rittinger;Joe Budman;Jian Xu;Stefano Volinia.
Molecular Cell (1999)
Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways
Bing Xiao;Stephen J. Smerdon;David H. Jones;Guy G. Dodson;Guy G. Dodson.
Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue
Katrin Rittinger;Philip A. Walker;John F. Eccleston;Stephen J. Smerdon.
The Molecular Basis of FHA Domain:Phosphopeptide Binding Specificity and Implications for Phospho-Dependent Signaling Mechanisms
Daniel Durocher;Ian A. Taylor;Dilara Sarbassova;Lesley F. Haire.
Molecular Cell (2000)
The mechanism of autooxidation of myoglobin.
R E Brantley;S J Smerdon;A J Wilkinson;E W Singleton.
Journal of Biological Chemistry (1993)
Molecular Basis of Phosphorylation-Induced Activation of the NADPH Oxidase
Yvonne Groemping;Karine Lapouge;Stephen J. Smerdon;Katrin Rittinger.
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