What is she best known for?
The fields of study she is best known for:
Her main research concerns Biochemistry, Cyclin-dependent kinase, Kinase, Cyclin-dependent kinase 2 and Cyclin-dependent kinase 1.
In the subject of general Biochemistry, her work in Cyclin-dependent kinase complex, Glycoprotein, Phosphorylation and Histone H3 is often linked to P-glycoprotein, thereby combining diverse domains of study.
The Cyclin-dependent kinase study which covers Cyclin that intersects with Cyclin-dependent kinase 5.
Her Kinase study improves the overall literature in Cell biology.
Her Cyclin-dependent kinase 2 research incorporates themes from Protein structure and Stereochemistry.
Her Cyclin-dependent kinase 1 research incorporates elements of Molecular biology and Cell growth.
Her most cited work include:
- The biochemistry of P-glycoprotein-mediated multidrug resistance. (1811 citations)
- Protein kinase inhibitors: insights into drug design from structure. (1021 citations)
- Indirubin, the active constituent of a Chinese antileukaemia medicine, inhibits cyclin-dependent kinases. (642 citations)
What are the main themes of her work throughout her whole career to date?
Jane A. Endicott spends much of her time researching Cyclin-dependent kinase, Cell biology, Cyclin-dependent kinase 2, Biochemistry and Kinase.
Jane A. Endicott combines subjects such as Cyclin-dependent kinase 1, Binding site and Cyclin with her study of Cyclin-dependent kinase.
The study incorporates disciplines such as Cancer research and Purine in addition to Cyclin-dependent kinase 1.
Her work deals with themes such as Protein structure, Cell cycle, Ubiquitin and Cyclin D, which intersect with Cell biology.
She interconnects Stereochemistry and Mitogen-activated protein kinase kinase in the investigation of issues within Cyclin-dependent kinase 2.
Her studies examine the connections between Kinase and genetics, as well as such issues in Computational biology, with regards to Drug discovery.
She most often published in these fields:
- Cyclin-dependent kinase (37.01%)
- Cell biology (36.36%)
- Cyclin-dependent kinase 2 (30.52%)
What were the highlights of her more recent work (between 2013-2021)?
- Cell biology (36.36%)
- Cyclin-dependent kinase (37.01%)
- Cyclin-dependent kinase 1 (15.58%)
In recent papers she was focusing on the following fields of study:
Jane A. Endicott mainly investigates Cell biology, Cyclin-dependent kinase, Cyclin-dependent kinase 1, Cyclin-dependent kinase 2 and Kinase.
The concepts of her Cell biology study are interwoven with issues in Genetics, Structural motif, Mutant and Nuclear transport.
Her Cyclin-dependent kinase study combines topics from a wide range of disciplines, such as Binding site and Cyclin.
Her Cyclin study incorporates themes from Computational biology and Protein kinase A.
Her Cyclin-dependent kinase 2 research includes themes of Cancer research and Stereochemistry.
Her Kinase study is concerned with Biochemistry in general.
Between 2013 and 2021, her most popular works were:
- CDK1 structures reveal conserved and unique features of the essential cell cycle CDK. (83 citations)
- CDK1 structures reveal conserved and unique features of the essential cell cycle CDK. (83 citations)
- Structural insights into the functional diversity of the CDK–cyclin family (49 citations)
In her most recent research, the most cited papers focused on:
Jane A. Endicott mainly focuses on Cyclin-dependent kinase, Cell biology, Binding site, Cell cycle and Cyclin-dependent kinase 1.
Her study in Kinase extends to Cyclin-dependent kinase with its themes.
Her Kinase research includes elements of Apoptosis, Transcription and Cyclin.
Her studies deal with areas such as Nuclear transport, Cell nucleus, Importin, Nuclear protein and Ankyrin repeat as well as Cell biology.
Her Binding site research integrates issues from Adenosine triphosphate, Druggability, Pharmacophore, Stereochemistry and Structure–activity relationship.
Her Cyclin-dependent kinase 1 research focuses on Cyclin-dependent kinase 2 and how it relates to Conformational energy, Non-competitive inhibition and Transferase.
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