What is he best known for?
The fields of study he is best known for:
Johannes Buchner mostly deals with Chaperone, Biochemistry, Protein folding, Hsp90 and Cell biology.
His Chaperone research is multidisciplinary, incorporating perspectives in Heat shock protein, Hsp70, Co-chaperone, Saccharomyces cerevisiae and Hsp33.
His Heat shock protein study incorporates themes from Protein family, Protein aggregation and Cytosol.
His study ties his expertise on Biophysics together with the subject of Biochemistry.
His Protein folding study combines topics from a wide range of disciplines, such as Endoplasmic reticulum, GroEL, Adenosine triphosphate and Förster resonance energy transfer.
His Hsp90 research is multidisciplinary, relying on both ATP hydrolysis, ATPase, Protein degradation, Tetratricopeptide and Binding site.
His most cited work include:
- Small heat shock proteins are molecular chaperones (1229 citations)
- The Heat Shock Response: Life on the Verge of Death (1044 citations)
- Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation (690 citations)
What are the main themes of his work throughout his whole career to date?
Johannes Buchner mainly investigates Biochemistry, Chaperone, Hsp90, Protein folding and Cell biology.
His Biochemistry study frequently involves adjacent topics like Biophysics.
The study incorporates disciplines such as Heat shock protein, Co-chaperone, Hsp33, Endoplasmic reticulum and Protein structure in addition to Chaperone.
His work carried out in the field of Hsp90 brings together such families of science as ATP hydrolysis, Nucleotide, Cytosol, Förster resonance energy transfer and Binding site.
In his study, which falls under the umbrella issue of Protein folding, Protein secondary structure is strongly linked to Native state.
He combines subjects such as Proteome and In vitro with his study of Cell biology.
He most often published in these fields:
- Biochemistry (46.57%)
- Chaperone (41.79%)
- Hsp90 (32.54%)
What were the highlights of his more recent work (between 2014-2021)?
- Hsp90 (32.54%)
- Cell biology (27.76%)
- Biophysics (27.76%)
In recent papers he was focusing on the following fields of study:
His scientific interests lie mostly in Hsp90, Cell biology, Biophysics, Chaperone and Protein folding.
His Hsp90 study is associated with Heat shock protein.
His work in Cell biology addresses subjects such as Biochemistry, which are connected to disciplines such as Förster resonance energy transfer.
His Biophysics study integrates concerns from other disciplines, such as Immunoglobulin light chain, Protein aggregation and Binding site.
His research investigates the link between Chaperone and topics such as Protein structure that cross with problems in Mutation.
His Protein folding research integrates issues from Folding, Nucleotide exchange factor, Endoplasmic reticulum and Force spectroscopy.
Between 2014 and 2021, his most popular works were:
- The HSP90 chaperone machinery (499 citations)
- The Growing World of Small Heat Shock Proteins: From Structure to Functions (94 citations)
- ThT 101: a primer on the use of thioflavin T to investigate amyloid formation (93 citations)
In his most recent research, the most cited papers focused on:
Johannes Buchner focuses on Cell biology, Biochemistry, Hsp90, Chaperone and Heat shock protein.
His study looks at the relationship between Cell biology and topics such as Yeast, which overlap with Protein turnover, Heat shock, Transcriptome, Gene expression and Protein Homeostasis.
Biochemistry is closely attributed to Antigen-Antibody Complex in his work.
His work deals with themes such as Crystallography, Computational biology and Peptide, which intersect with Chaperone.
The concepts of his Heat shock protein study are interwoven with issues in Regulator, Amino acid, Proteostasis and In vitro.
His studies examine the connections between Proteostasis and genetics, as well as such issues in DNA repair, with regards to Protein folding.
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