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Johannes Buchner (1960-)

Molekularbiologe

Name	Johannes Buchner
Zeit	1960- (Lebensdaten)
Ort	Ihrlerstein (Geburtsort) München (Wirkungsort) Deutschland
Geschlecht	männlich
Akademischer Grad bzw. Titel	Prof. Dr.
Beruf	Molekularbiologe (charakteristischer Beruf)
Beziehung	Deutsche Akademie der Naturforscher Leopoldina (Mitglied, Matrikelnr. 07074) (2006-)
Weitere Angaben	deutscher Molekularbiologe ; Professor an der TU München (Lehrstuhl für Biotechnologie) ; erforscht die Strukturbildung von Proteinen und die zellulären Mechanismen der Proteinfaltung mit den daran beteiligten Chaperonen (besonders HSP90, Kleine Hitzeschockproteine sHsps) ; seit 2012 im Herausgebergremium des Journal of Molecular Biology ; ab 2013 war er Vizepräsident und ab 2015 Präsident der Deutschen Gesellschaft für Biochemie und Molekularbiologie ; 2014 wurde er Mitglied der European Molecular Biology Organisation (EMBO) ; 2006 wurde er Mitglied der Leopoldina ; 2010 wurde er Mitglied der Bayerischen Akademie der Wissenschaften ; erhielt 2015 die Schleiden-Medaille
Quelle	Internet
Datensatztyp	Person
GND-Nummer	111549970X
Datensatz-ID	111549970X
Beteiligt an alle anzeigen Evolution of the conformational dynamics of the molecular chaperone Hsp90 Comparative analysis of the conformational dynamics of human and yeast Hsp90 Elektronenmikroskopische Untersuchungen von kleinen Hitzeschockproteinen : Strukturbiologische Charakterisierung von Sip1 und Hsp17 aus C.elegans Multimeric ACE2-IgM fusions as broadly active antivirals that potently neutralize SARS-CoV-2 variants Molecular mechanisms of antibody light chain amyloidogenicity Structure and Function of the Invariant Light Chain Studies on eucaryotic small heat shock proteins Biogenesis of secretory immunoglobulin M requires intermediate non‐native disulfide bonds and engagement of the protein disulfide isomerase ERp44 Imbalances in the eye lens proteome are linked to cataract formation Hsp90‐mediated regulation of DYRK3 couples stress granule disassembly and growth via mTORC1 signaling Chicken-derived antibodies for therapeutic, diagnostic and bioprocessing applications Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae Characterization of the essential Hsp90 co-chaperone Sgt1 in S. cerevisiae Global and protein-specific analysis of the heat shock response in S. cerevisiae Investigation of the Hsp90 co-chaperone machinery in eukaryotes Mechanistic Analysis of the Hsp70/ Hsp90 Co-chaperone Sti1 Molecular Insights into Antibody Light Chain Pathogenicity Regulation of small heat shock proteins Structural and biophysical characterization of FKBP51/52 and their binding partners A switch point in the molecular chaperone Hsp90 responding to client interaction Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate Conformational analysis of proteins of biopharmaceutical interest Mechanistic Analysis of Conformational Dynamics of the Molecular Chaperone Hsp90 The Hsp90 machinery facilitates the transport of diphtheria toxin into human cells Analysis of different antibody domain mutations affecting the VH/VL interface, CH1 folding and CH2 stability Characterization of different Hsp90-client and chaperone-substrate interactions Influence of the Hsp90 co-chaperones on client protein activation The regulation of Hsp90 by its essential co-chaperone Cns1 The Small Heat Shock Proteins and the Heat Stress Response of Baker’s Yeast Der große Wurf : Faltungen in der Gegenwartskunst ; [anlässlich der Ausstellung "Der Große Wurf. Faltungen in der Gegenwartskunst", Kunstmuseen Krefeld/Museum Haus Lange und Kaiser-Wilhelm-Museum, Krefeld, 2. März - 25. Mai 2008] = Falling right into place

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Katalog der Deutschen Nationalbibliothek

Johannes Buchner (1960-)

Evolution of the conformational dynamics of the molecular chaperone Hsp90

Comparative analysis of the conformational dynamics of human and yeast Hsp90

Elektronenmikroskopische Untersuchungen von kleinen Hitzeschockproteinen : Strukturbiologische Charakterisierung von Sip1 und Hsp17 aus C.elegans

Multimeric ACE2-IgM fusions as broadly active antivirals that potently neutralize SARS-CoV-2 variants

Molecular mechanisms of antibody light chain amyloidogenicity

Structure and Function of the Invariant Light Chain

Studies on eucaryotic small heat shock proteins

Biogenesis of secretory immunoglobulin M requires intermediate non‐native disulfide bonds and engagement of the protein disulfide isomerase ERp44

Imbalances in the eye lens proteome are linked to cataract formation

Hsp90‐mediated regulation of DYRK3 couples stress granule disassembly and growth via mTORC1 signaling

Chicken-derived antibodies for therapeutic, diagnostic and bioprocessing applications

Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae

Characterization of the essential Hsp90 co-chaperone Sgt1 in S. cerevisiae

Global and protein-specific analysis of the heat shock response in S. cerevisiae

Investigation of the Hsp90 co-chaperone machinery in eukaryotes

Mechanistic Analysis of the Hsp70/ Hsp90 Co-chaperone Sti1

Molecular Insights into Antibody Light Chain Pathogenicity

Regulation of small heat shock proteins

Structural and biophysical characterization of FKBP51/52 and their binding partners

A switch point in the molecular chaperone Hsp90 responding to client interaction

Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate

Conformational analysis of proteins of biopharmaceutical interest

Mechanistic Analysis of Conformational Dynamics of the Molecular Chaperone Hsp90

The Hsp90 machinery facilitates the transport of diphtheria toxin into human cells

Analysis of different antibody domain mutations affecting the VH/VL interface, CH1 folding and CH2 stability

Characterization of different Hsp90-client and chaperone-substrate interactions

Influence of the Hsp90 co-chaperones on client protein activation

The regulation of Hsp90 by its essential co-chaperone Cns1

The Small Heat Shock Proteins and the Heat Stress Response of Baker’s Yeast

Der große Wurf : Faltungen in der Gegenwartskunst ; [anlässlich der Ausstellung "Der Große Wurf. Faltungen in der Gegenwartskunst", Kunstmuseen Krefeld/Museum Haus Lange und Kaiser-Wilhelm-Museum, Krefeld, 2. März - 25. Mai 2008] = Falling right into place