What is he best known for?
The fields of study he is best known for:
Jens Peter Andersen spends much of his time researching ATPase, Biochemistry, Biophysics, Endoplasmic reticulum and Mutant.
His ATPase research is multidisciplinary, relying on both Dephosphorylation, Ion binding, Lipid bilayer and Phosphorylation.
His Biophysics research includes themes of P-type ATPase and Na+/K+-ATPase.
He has researched P-type ATPase in several fields, including Sodium and Calcium pump.
His Na+/K+-ATPase study combines topics from a wide range of disciplines, such as Electrochemical gradient and Membrane transport.
His work carried out in the field of Mutant brings together such families of science as ATP hydrolysis, Molecular biology, Thapsigargin and Calcium ATPase.
His most cited work include:
- Crystal structure of the sodium–potassium pump (750 citations)
- Crystal structure of the sodium–potassium pump (750 citations)
- Structural basis for E1-E2 conformational transitions in Na,K-pump and Ca-pump proteins. (300 citations)
What are the main themes of his work throughout his whole career to date?
His primary areas of study are ATPase, Biochemistry, Endoplasmic reticulum, Biophysics and Mutant.
The concepts of his ATPase study are interwoven with issues in Dephosphorylation, Wild type, Stereochemistry, Transmembrane domain and Phosphorylation.
Jens Peter Andersen works mostly in the field of Stereochemistry, limiting it down to concerns involving Na+/K+-ATPase and, occasionally, Electrochemical gradient, Cation binding and Ouabain.
His Endoplasmic reticulum study combines topics in areas such as Calcium, Calcium ATPase, Binding site and Enzyme.
His Biophysics study which covers Protein structure that intersects with Plasma protein binding.
His Mutant study also includes
- Molecular biology, which have a strong connection to Thapsigargin,
- SERCA which is related to area like Cytosol.
He most often published in these fields:
- ATPase (59.89%)
- Biochemistry (48.02%)
- Endoplasmic reticulum (42.94%)
What were the highlights of his more recent work (between 2011-2021)?
- Biophysics (37.85%)
- ATPase (59.89%)
- Biochemistry (48.02%)
In recent papers he was focusing on the following fields of study:
Jens Peter Andersen mainly focuses on Biophysics, ATPase, Biochemistry, Transmembrane domain and Na+/K+-ATPase.
His studies in Biophysics integrate themes in fields like P-type ATPase, SERCA, Calcium ATPase and Mutant.
The ATPase study combines topics in areas such as Dephosphorylation, Ion binding, Phosphatidylserine, Flippase and Phosphorylation.
His work in Biochemistry tackles topics such as Cation binding which are related to areas like Aminophospholipid transport.
His Transmembrane domain research is multidisciplinary, incorporating elements of Protein structure and Reticulum.
The various areas that he examines in his Na+/K+-ATPase study include Molecular biology, Stereochemistry, Intracellular and Binding site.
Between 2011 and 2021, his most popular works were:
- P4-ATPases as Phospholipid Flippases-Structure, Function, and Enigmas. (124 citations)
- Critical roles of isoleucine-364 and adjacent residues in a hydrophobic gate control of phospholipid transport by the mammalian P4-ATPase ATP8A2 (72 citations)
- Critical role of a transmembrane lysine in aminophospholipid transport by mammalian photoreceptor P4-ATPase ATP8A2. (66 citations)
In his most recent research, the most cited papers focused on:
Jens Peter Andersen focuses on Biochemistry, ATPase, Transmembrane domain, Biophysics and Protein structure.
His study in ATPase is interdisciplinary in nature, drawing from both Dephosphorylation, Ion binding, Phosphatidylethanolamine and Phosphorylation.
His Transmembrane domain research integrates issues from P-type ATPase, Phospholipid, Flippase and SERCA.
His Biophysics study frequently links to related topics such as Phosphatidylserine.
His research integrates issues of Calcium ATPase and Enzyme kinetics in his study of Ion transporter.
The study incorporates disciplines such as Mutation and Na+/K+-ATPase in addition to COS cells.
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