What is he best known for?
The fields of study he is best known for:
His primary areas of investigation include Chaperone, Cell biology, Biochemistry, Protein folding and Heat shock protein.
His research combines Binding site and Chaperone.
His studies deal with areas such as Heat shock factor, Protein subunit and Co-chaperone as well as Cell biology.
His work investigates the relationship between Protein folding and topics such as Hsp70 that intersect with problems in Chaperone activity.
His study of Hsp90 is a part of Heat shock protein.
His Allosteric regulation study deals with Biophysics intersecting with Amino acid.
His most cited work include:
- Hsp70 chaperones: Cellular functions and molecular mechanism (1958 citations)
- Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones (448 citations)
- Multistep mechanism of substrate binding determines chaperone activity of Hsp70 (319 citations)
What are the main themes of his work throughout his whole career to date?
The scientist’s investigation covers issues in Chaperone, Biochemistry, Cell biology, Protein folding and Hsp70.
His research integrates issues of Heat shock protein, Hsp90, Co-chaperone, Allosteric regulation and Binding site in his study of Chaperone.
As a part of the same scientific family, he mostly works in the field of Biochemistry, focusing on Biophysics and, on occasion, Peptide sequence, DNA and HSF1.
His studies in Cell biology integrate themes in fields like Heat shock factor and Heat shock.
His Protein folding research incorporates themes from Nucleotide exchange factor, Mutant, Nucleotide, Escherichia coli and Native state.
His work focuses on many connections between Hsp70 and other disciplines, such as Yeast, that overlap with his field of interest in Cytosol.
He most often published in these fields:
- Chaperone (43.37%)
- Biochemistry (37.95%)
- Cell biology (35.54%)
What were the highlights of his more recent work (between 2017-2021)?
- Cell biology (35.54%)
- Protein folding (36.14%)
- Chaperone (43.37%)
In recent papers he was focusing on the following fields of study:
Matthias P. Mayer mainly investigates Cell biology, Protein folding, Chaperone, Hsp70 and Hsp90.
His Cell biology research incorporates elements of Psychological repression, Dimer and Heat shock.
The Chaperone study combines topics in areas such as Heat shock protein, Proteome and Protein degradation.
The various areas that Matthias P. Mayer examines in his Hsp70 study include Proteostasis, Nucleotide and Allosteric regulation, Enzyme.
In his study, which falls under the umbrella issue of Allosteric regulation, Protein Homeostasis is strongly linked to ATP hydrolysis.
His Hsp90 research is multidisciplinary, relying on both Tyrosine, Denaturation, Native state, Protein–protein interaction and In vivo.
Between 2017 and 2021, his most popular works were:
- The Hsp70 chaperone network (172 citations)
- Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones (84 citations)
- Hsp90 Breaks the Deadlock of the Hsp70 Chaperone System. (62 citations)
In his most recent research, the most cited papers focused on:
His primary areas of study are Chaperone, Protein folding, Hsp70, Hsp90 and Cell biology.
His Chaperone study integrates concerns from other disciplines, such as Heat shock protein, Protein domain, Nucleotide, Proteostasis and Computational biology.
His studies examine the connections between Heat shock protein and genetics, as well as such issues in Protein aggregation, with regards to Heat shock, Signal transduction, Intracellular and Cytosol.
His Nucleotide study combines topics in areas such as ATP hydrolysis, Yeast, Allosteric regulation and Protein Homeostasis.
He regularly ties together related areas like Biophysics in his Protein folding studies.
His Cell biology research includes themes of Budding yeast and Peptide substrate.
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