Martin E.M. Noble

What is he best known for?

The fields of study he is best known for:

• Gene
• Enzyme
• Amino acid

His primary areas of study are Biochemistry, Kinase, Protein structure, Cyclin-dependent kinase 2 and Protein kinase A. His study brings together the fields of Biophysics and Biochemistry. His study in Protein structure is interdisciplinary in nature, drawing from both Phosphorylase kinase, Stereochemistry, Conserved sequence and Binding site.

His biological study spans a wide range of topics, including Hydrolase, Triacylglycerol lipase, Lipase, Enzyme and Alanine. His work investigates the relationship between Binding site and topics such as Cyclin binding that intersect with problems in Adenine binding and Active site. His Cyclin-dependent kinase 2 research focuses on subjects like Cyclin-dependent kinase, which are linked to Cyclin.

His most cited work include:

• Active and Inactive Protein Kinases: Structural Basis for Regulation (1177 citations)
• Protein kinase inhibitors: insights into drug design from structure. (1021 citations)
• Presenting your structures: the CCP4mg molecular-graphics software. (842 citations)

What are the main themes of his work throughout his whole career to date?

His primary areas of investigation include Biochemistry, Stereochemistry, Cell biology, Cyclin-dependent kinase and Cyclin-dependent kinase 2. His studies examine the connections between Biochemistry and genetics, as well as such issues in Biophysics, with regards to Plasma protein binding. The various areas that Martin E.M. Noble examines in his Stereochemistry study include Transferase, Crystallography, Catalytic triad, Active site and Structure–activity relationship.

His work in Cell biology tackles topics such as Cyclin D which are related to areas like Cyclin A2. Within one scientific family, he focuses on topics pertaining to Binding site under Cyclin-dependent kinase, and may sometimes address concerns connected to Adenosine triphosphate. His Protein structure study incorporates themes from Glycogen phosphorylase and Peptide sequence.

He most often published in these fields:

• Biochemistry (31.11%)
• Stereochemistry (22.67%)
• Cell biology (21.33%)

What were the highlights of his more recent work (between 2017-2021)?

• Computational chemistry (8.89%)
• Cell biology (21.33%)
• Cancer research (4.00%)

In recent papers he was focusing on the following fields of study:

Computational chemistry, Cell biology, Cancer research, Cyclin-dependent kinase 1 and Kinase are his primary areas of study. His Cell biology research integrates issues from Cyclin-dependent kinase, Regulation of gene expression, Ubiquitin ligase, Protein kinase domain and Cyclin. His research investigates the connection between Cyclin-dependent kinase and topics such as SKP2 that intersect with issues in Binding site.

His work deals with themes such as Mdm2, Cyclin-dependent kinase 2 and Protein–protein interaction, which intersect with Cancer research. His Kinase research is under the purview of Biochemistry. Martin E.M. Noble has researched Biochemistry in several fields, including Angiogenesis and Motility.

Between 2017 and 2021, his most popular works were:

• CCP4i2: the new graphical user interface to the CCP4 program suite. (141 citations)
• Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease. (73 citations)
• Announcing mandatory submission of PDBx/mmCIF format files for crystallographic depositions to the Protein Data Bank (PDB). (20 citations)

In his most recent research, the most cited papers focused on:

• Gene
• Enzyme
• Amino acid

His primary areas of study are Kinase, Crystallography, Cysteine, Computational biology and Binding site. His Kinase study falls within the topics of Cell biology and Biochemistry. His research ties Motility and Biochemistry together.

His research in Crystallography focuses on subjects like Electrophile, which are connected to Viral protease. His Cysteine research incorporates elements of Stereochemistry, MDMX and Peptide. His work in Binding site is not limited to one particular discipline; it also encompasses Protein structure.