What is he best known for?
The fields of study he is best known for:
The scientist’s investigation covers issues in Biochemistry, Tau protein, Kinase, Phosphorylation and Cell biology.
His study in Mitogen-activated protein kinase kinase and Cyclin-dependent kinase 2 is carried out as part of his Biochemistry studies.
His research in Tau protein intersects with topics in Microtubule-associated protein, Biophysics, Point mutation and Kinase activity.
His Biophysics study incorporates themes from Alzheimer's disease, Protein structure and Recombinant DNA.
His studies deal with areas such as Peptide sequence and Microtubule as well as Protein structure.
The concepts of his Kinase study are interwoven with issues in Epitope, Cyclin-dependent kinase and Molecular biology.
His most cited work include:
- Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure. (697 citations)
- Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding (626 citations)
- Indirubins Inhibit Glycogen Synthase Kinase-3β and CDK5/P25, Two Protein Kinases Involved in Abnormal Tau Phosphorylation in Alzheimer's Disease A PROPERTY COMMON TO MOST CYCLIN-DEPENDENT KINASE INHIBITORS? (600 citations)
What are the main themes of his work throughout his whole career to date?
Jacek Biernat mainly focuses on Tau protein, Biophysics, Biochemistry, Phosphorylation and Cell biology.
The various areas that Jacek Biernat examines in his Tau protein study include Protein structure, Microtubule-associated protein, Microtubule and Hyperphosphorylation.
The study incorporates disciplines such as Crystallography, Fibril and Peptide sequence in addition to Protein structure.
Jacek Biernat works mostly in the field of Biophysics, limiting it down to topics relating to Plasma protein binding and, in certain cases, Binding site, as a part of the same area of interest.
The Phosphorylation study combines topics in areas such as Epitope, Molecular biology and Kinase.
His work on Protein phosphorylation as part of general Cell biology study is frequently linked to Genetically modified mouse, bridging the gap between disciplines.
He most often published in these fields:
- Tau protein (61.29%)
- Biophysics (36.77%)
- Biochemistry (36.13%)
What were the highlights of his more recent work (between 2014-2021)?
- Tau protein (61.29%)
- Biophysics (36.77%)
- Phosphorylation (34.84%)
In recent papers he was focusing on the following fields of study:
Tau protein, Biophysics, Phosphorylation, Microtubule and Tubulin are his primary areas of study.
His biological study spans a wide range of topics, including Biochemistry, Protein aggregation, Cell biology and Hyperphosphorylation.
His research in Biophysics intersects with topics in Protein structure, Plasma protein binding and Green fluorescent protein.
His Phosphorylation research integrates issues from Tau phosphorylation, Central nervous system, Disease and Microtubule assembly.
His Microtubule research incorporates themes from Folding and Cytoskeleton.
His research integrates issues of Molecular biology, Tyrosine, Salt bridge and Peptide in his study of Tubulin.
Between 2014 and 2021, his most popular works were:
- Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau (234 citations)
- Tau stabilizes microtubules by binding at the interface between tubulin heterodimers (230 citations)
- Folding of the Tau Protein on Microtubules. (78 citations)
In his most recent research, the most cited papers focused on:
His scientific interests lie mostly in Tau protein, Microtubule, Biophysics, Phosphorylation and Biochemistry.
His Tau protein study results in a more complete grasp of Alzheimer's disease.
His study in Biochemistry is interdisciplinary in nature, drawing from both Amyloid fibril and Microtubule polymerization.
His Plasma protein binding research includes elements of Protein aggregation, Alternative splicing and Amyloid.
His work deals with themes such as Actin cytoskeleton, Filamentous actin, Cytoskeleton, Nuclear magnetic resonance spectroscopy and Actin, which intersect with Microtubule-associated protein.
His Tubulin research is multidisciplinary, incorporating perspectives in Salt bridge, Protein structure, Conformational ensembles, Intrinsically disordered proteins and Binding site.
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