K. Richter

发表

The heat shock response: life on the verge of death.

J. Buchner, M. Haslbeck, K. Richter, 2010, Molecular cell.

hsp90: Twist and Fold

Johannes Buchner, Klaus Richter, J. Buchner, 2006, Cell.

The Charged Linker Region Is an Important Regulator of Hsp90 Function*

J. Buchner, O. Hainzl, K. Richter, 2009, The Journal of Biological Chemistry.

N-terminal Residues Regulate the Catalytic Efficiency of the Hsp90 ATPase Cycle*

J. Reinstein, J. Buchner, K. Richter, 2002, The Journal of Biological Chemistry.

Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB

H. Dietz, F. Praetorius, C. Ihling, 2018, Nature Communications.

Cns1 Is an Activator of the Ssa1 ATPase Activity*

J. Buchner, O. Hainzl, K. Richter, 2004, Journal of Biological Chemistry.

E. Grill, A. Korte, A. Christmann, 2010, The Plant journal : for cell and molecular biology.

Hsp90-downregulation influences the heat-shock response, innate immune response and onset of oocyte development in nematodes

K. Richter, K. Marcus, Julia M. Eckl, 2017, PloS one.

Natural-Product-Inspired Aminoepoxybenzoquinones Kill Members of the Gram-Negative Pathogen Salmonella by Attenuating Cellular Stress Response.

F. Mandl, T. Fuchs, S. Schneider, 2016, Angewandte Chemie.

Asymmetric activation of the hsp90 dimer by its cochaperone aha1.

J. Buchner, H. Kessler, M. Retzlaff, 2010, Molecular cell.

Sti1 Is a Non-competitive Inhibitor of the Hsp90 ATPase

J. Reinstein, J. Buchner, O. Hainzl, 2003, The Journal of Biological Chemistry.

Unique proline-rich domain regulates the chaperone function of AIPL1.

J. Buchner, F. Schmid, Thomas Kriehuber, 2013, Biochemistry.

Functions of the Hsp90 chaperone system: lifting client proteins to new heights.

K. Richter, Julia M. Eckl, 2013, International journal of biochemistry and molecular biology.

The architecture of functional modules in the Hsp90 co‐chaperone Sti1/Hop

J. Buchner, H. Kessler, Stephan Lagleder, 2012, The EMBO journal.

Hsp90·Cdc37 Complexes with Protein Kinases Form Cooperatively with Multiple Distinct Interaction Sites*

M. Sattler, Matthias J. Scherr, K. Richter, 2015, The Journal of Biological Chemistry.

Hsp90: Chaperoning signal transduction

J. Buchner, K. Richter, 2001, Journal of cellular physiology.

Cdc37 (Cell Division Cycle 37) Restricts Hsp90 (Heat Shock Protein 90) Motility by Interaction with N-terminal and Middle Domain Binding Sites*

J. Reinstein, D. Rutz, K. Richter, 2013, The Journal of Biological Chemistry.

Hop/Sti1 phosphorylation inhibits its co-chaperone function

J. Buchner, T. Madl, K. Richter, 2014, EMBO reports.

The cellular world according to Hsp90

L. Hendershot, B. Freeman, K. Richter, 2007, Nature Structural &Molecular Biology.

Allosteric Regulation Points Control the Conformational Dynamics of the Molecular Chaperone Hsp90.

G. Colombo, E. Moroni, J. Buchner, 2016, Journal of molecular biology.

Glucocorticoid receptor complexes form cooperatively with the Hsp90 co-chaperones Pp5 and FKBPs

K. Richter, K. Marcus, K. Barkovits, 2020, Scientific Reports.

Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation

R. Huber, W. Bode, S. Kawabata, 2003, Nature.

Fibrinogen Substrate Recognition by Staphylocoagulase·(Pro)thrombin Complexes*

W. Bode, P. Panizzi, K. Richter, 2006, Journal of Biological Chemistry.

head-bent resistant Hsc70 variants show reduced Hsp40 affinity and altered protein folding activity

K. Richter, Siyuan Sima, Katharina Papsdorf, 2019, Scientific Reports.

Binding of the HSF-1 DNA-binding domain to multimeric C. elegans consensus HSEs is guided by cooperative interactions

K. Richter, Siyuan Sima, Lukas Schmauder, 2022, Scientific Reports.

Selective Activation of Human Caseinolytic Protease P (ClpP).

S. Schneider, S. Sieber, K. Richter, 2018, Angewandte Chemie.

The Prion Curing Agent Guanidinium Chloride Specifically Inhibits ATP Hydrolysis by Hsp104*

J. Buchner, A. Imhof, S. Walter, 2004, Journal of Biological Chemistry.

Multiple regulatory intrinsically disordered motifs control FOXO4 transcription factor binding and function.

Emil Spreitzer, T. Madl, B. Burgering, 2020, Cell reports.

The Dimer Interface of the Membrane Type 1 Matrix Metalloproteinase Hemopexin Domain

D. Svergun, W. Bode, D. Franke, 2010, The Journal of Biological Chemistry.

Analysis of the Regulation of the Molecular Chaperone Hsp26 by Temperature-induced Dissociation

J. Buchner, T. Stromer, M. Haslbeck, 2004, Journal of Biological Chemistry.

The activation mechanism of Hsp26 does not require dissociation of the oligomer.

M. Wühr, J. Buchner, Titus M. Franzmann, 2005, Journal of molecular biology.

Reversible Inhibitors Arrest ClpP in a Defined Conformational State that Can Be Revoked by ClpX Association.

S. Sieber, H. Waldmann, M. Groll, 2015, Angewandte Chemie.

The Arabidopsis ESCRT protein–protein interaction network

S. Schellmann, K. Richter, M. Shahriari, 2011, Plant Molecular Biology.

AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control

S. Sieber, T. Madl, Christoph Göbl, 2015, Nature Communications.

Energetics by NMR: Site-specific binding in a positively cooperative system

D. Cistola, K. Richter, D. Covey, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Mixed Hsp90–cochaperone complexes are important for the progression of the reaction cycle

J. Buchner, K. Richter, Jing Li, 2011, Nature Structural &Molecular Biology.

Hsp90 in non-mammalian metazoan model systems.

K. Richter, C. Kaiser, Veronika Haslbeck, 2012, Biochimica et biophysica acta.

The Hsp90 Family of Molecular Chaperones

J. Buchner, K. Richter, Birgit Meinlschmidt, 2008 .

daf-41/p23: A Small Protein Heating Up Lifespan Regulation

K. Richter, 2015, PLoS genetics.

Protein folding, misfolding and quality control: the role of molecular chaperones.

K. Richter, Katharina Papsdorf, 2014, Essays in biochemistry.

The Balanced Regulation of Hsc70 by DNJ-13 and UNC-23 Is Required for Muscle Functionality*

K. Richter, Katharina Papsdorf, Julia Sacherl, 2014, The Journal of Biological Chemistry.

The Lid Domain of Caenorhabditis elegans Hsc70 Influences ATP Turnover, Cofactor Binding and Protein Folding Activity

K. Richter, C. Kaiser, Katharina Papsdorf, 2012, PloS one.

Glucocorticoid resistance conferring mutation in the C-terminus of GR alters the receptor conformational dynamics

K. Richter, Anna Kaziales, Florian Rührnößl, 2021, Scientific Reports.

hsp-90 and unc-45 depletion induce characteristic transcriptional signatures in coexpression cliques of C. elegans

K. Richter, Lukas Schmauder, 2021, Scientific Reports.

A methylated lysine is a switch point for conformational communication in the chaperone Hsp90

Ville R. I. Kaila, J. Buchner, Jannis Lawatscheck, 2020, Nature Communications.

Importance of cycle timing for the function of the molecular chaperone Hsp90

J. Buchner, T. Madl, M. Sattler, 2016, Nature Structural &Molecular Biology.

Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules

D. Lamb, J. Buchner, H. Kessler, 2015, Nature Communications.

Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle

J. Reinstein, J. Buchner, K. Richter, 2013, Nature Structural &Molecular Biology.

Conformational switching of the molecular chaperone Hsp90 via regulated phosphorylation.

J. Buchner, H. Daub, S. Wandinger, 2012, Molecular cell.

Downregulation of the Hsp90 System Causes Defects in Muscle Cells of Caenorhabditis Elegans

K. Richter, C. Kaiser, Veronika Haslbeck, 2011, PloS one.

The non-canonical Hop protein from Caenorhabditis elegans exerts essential functions and forms binary complexes with either Hsc70 or Hsp90.

K. Richter, Florian Brandt, Andreas M. Gaiser, 2009, Journal of molecular biology.

Conserved Conformational Changes in the ATPase Cycle of Human Hsp90*

J. Reinstein, L. Skalniak, J. Buchner, 2008, Journal of Biological Chemistry.

Selective activators of protein phosphatase 5 target the auto-inhibitory mechanism

G. Popowicz, G. Gemmecker, M. Sattler, 2015, Bioscience reports.

A central role of Arabidopsis thaliana ovate family proteins in networking and subcellular localization of 3-aa loop extension homeodomain proteins.

Klaus Richter, F. Salamini, J. Uhrig, 2005, Proceedings of the National Academy of Sciences of the United States of America.

A network of genes connects polyglutamine toxicity to ploidy control in yeast

K. Richter, Stefan Jordan, C. Kaiser, 2013, Nature Communications.

Nucleotide-Free sB-Raf is Preferentially Bound by Hsp90 and Cdc37 In Vitro.

K. Richter, Marina Daake, Julia M. Eckl, 2016, Journal of molecular biology.

Lipid Droplets Protect Aging Mitochondria and Thus Promote Lifespan in Yeast Cells

M. Rinnerthaler, K. Richter, Florian Geltinger, 2021, Frontiers in Cell and Developmental Biology.

Coordinated ATP Hydrolysis by the Hsp90 Dimer*

J. Buchner, O. Hainzl, K. Richter, 2001, The Journal of Biological Chemistry.

The alternatively folded state of the antibody C(H)3 domain.

J. Buchner, K. Richter, M. J. Thies, 2001, Journal of molecular biology.

SV-AUC as a stability-indicating method for the characterization of mRNA-LNPs

G. Winter, T. Menzen, A. Hawe, 2022, European Journal of Pharmaceutics and Biopharmaceutics.

A Multilaboratory Comparison of Calibration Accuracy and the Performance of External References in Analytical Ultracentrifugation

P. V. von Hippel, P. Prevelige, R. Fairman, 2015, PloS one.

Formation of She2p tetramers is required for mRNA binding, mRNP assembly, and localization.

E. Kremmer, J. Buchner, A. Heuck, 2009, RNA.

C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle.

J. Reinstein, T. Veit, J. Buchner, 2000, Journal of molecular biology.

An improved mRFP1 adds red to bimolecular fluorescence complementation

Guido Jach, Klaus Richter, J. Uhrig, 2006, Nature Methods.

Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90

Martin Hessling, Johannes Buchner, Klaus Richter, 2009, Nature Structural &Molecular Biology.

The rod-shaped conformation of Starmaker.

A. Ożyhar, K. Richter, A. Michnik, 2009, Biochimica et biophysica acta.

Spermidine synthase is prominently expressed in the striatal patch compartment and in putative interneurones of the matrix compartment

M. Krauss, G. Laube, G. Ahnert-Hilger, 2006, Journal of neurochemistry.

Nematode Sgt1-homologue D1054.3 binds open and closed conformations of Hsp90 via distinct binding sites.

D. Rutz, K. Richter, Adrian Drazic, 2014, Biochemistry.

Subunit Interactions and Cooperativity in the Microtubule-severing AAA ATPase Spastin*

T. Eckert, G. Woehlke, K. Richter, 2012, The Journal of Biological Chemistry.

Axin cancer mutants form nanoaggregates to rewire the Wnt signaling network

A. Heck, I. Jordens, R. Boelens, 2016, Nature Structural &Molecular Biology.

Polyglutamine toxicity in yeast induces metabolic alterations and mitochondrial defects

W. Eisenreich, K. Richter, Adrian Drazic, 2015, BMC Genomics.

The Hsp90 Chaperone Machinery*

J. Buchner, S. Wandinger, K. Richter, 2008, Journal of Biological Chemistry.

Cpr6 and Cpr7, Two Closely Related Hsp90-associated Immunophilins from Saccharomyces cerevisiae, Differ in Their Functional Properties*

Johannes Buchner, Klaus Richter, J. Buchner, 2000, The Journal of Biological Chemistry.

Regulation of the Hsp90 system.

K. Richter, Siyuan Sima, 2018, Biochimica et biophysica acta. Molecular cell research.

Chaperone-interacting TPR proteins in Caenorhabditis elegans.

K. Richter, M. Hessling, C. Kaiser, 2013, Journal of molecular biology.

Cdc37-Hsp90 Complexes Are Responsive to Nucleotide-induced Conformational Changes and Binding of Further Cofactors*

K. Richter, A. Kretzschmar, Andreas M. Gaiser, 2010, The Journal of Biological Chemistry.

Intrinsic Inhibition of the Hsp90 ATPase Activity*

J. Reinstein, J. Buchner, H. Kessler, 2006, Journal of Biological Chemistry.

The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle.

Johannes Buchner, Klaus Richter, J. Buchner, 2004, Journal of molecular biology.

PFN2 and NAA80 cooperate to efficiently acetylate the N-terminus of actin

T. Arnesen, K. Richter, Rasmus Ree, 2020, The Journal of Biological Chemistry.

PFN2 and NAA80 cooperate to efficiently acetylate the N-terminus of actin

T. Arnesen, K. Richter, Rasmus Ree, 2020, bioRxiv.

NMR Chemical Shift Perturbation Study of the N‐Terminal Domain of Hsp90 upon Binding of ADP, AMP‐PNP, Geldanamycin, and Radicicol

A. Dehner, J. Buchner, H. Kessler, 2003, Chembiochem : a European journal of chemical biology.

A methylated lysine is a switch point for conformational communication in the chaperone Hsp90

Ville R. I. Kaila, J. Buchner, Jannis Lawatscheck, 2020, Nature Communications.

Structure-based mutagenesis of phycobiliprotein smURFP for optoacoustic imaging.

V. Ntziachristos, A. Stiel, A. Chmyrov, 2019, ACS chemical biology.

Cellular and subcellular rat brain spermidine synthase expression patterns suggest region‐specific roles for polyamines, including cerebellar pre‐synaptic function

M. Krauss, G. Laube, K. Richter, 2007, Journal of neurochemistry.

Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53

J. Buchner, H. Kessler, M. Retzlaff, 2011, Nature Structural &Molecular Biology.

HSP-90/kinase complexes are stabilized by the large PPIase FKB-6

N. Morgner, K. Richter, K. Marcus, 2021, Scientific Reports.

The activity of protein phosphatase 5 towards native clients is modulated by the middle- and C-terminal domains of Hsp90

T. Madl, D. Rutz, Thomas Kriehuber, 2015, Scientific Reports.

The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function

M. Rief, J. Buchner, T. Hugel, 2014, Proceedings of the National Academy of Sciences.

A Grp on the Hsp90 mechanism.

J. Reinstein, J. Buchner, K. Richter, 2007, Molecular cell.

Protein-Protein-Wechselwirkungen

P. Uetz, D. Klostermeier, U. Curth, 2021, Bioanalytik.

Monomeric myosin V uses two binding regions for the assembly of stable translocation complexes

J. Buchner, A. Heuck, R. Jansen, 2007, Proceedings of the National Academy of Sciences.

Nematode CDC-37 and DNJ-13 form complexes and can interact with HSP-90

Alexander Bepperling, K. Richter, K. Marcus, 2021, Scientific Reports.

Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB

F. Praetorius, C. Ihling, A. Sinz, 2018, Nature Communications.

Artificial accelerators of the molecular chaperone Hsp90 facilitate rate-limiting conformational transitions.

J. Buchner, M. Sattler, G. Fischer, 2014, Angewandte Chemie.

Polyglutamine toxicity in yeast induces metabolic alterations and mitochondrial defects

W. Eisenreich, K. Richter, Adrian Drazic, 2015, BMC Genomics.

head-bent resistant Hsc70 variants show reduced Hsp40 affinity and altered protein folding activity

K. Richter, Siyuan Sima, Katharina Papsdorf, 2019, Scientific Reports.

Genome-wide analysis of yeast expression data based on a priori generated co-regulation cliques

K. Richter, Siyuan Sima, Lukas Schmauder, 2019, Microbial cell.

Modulated scanning fluorimetry can quickly assess thermal protein unfolding reversibility in microvolume samples.

G. Winter, T. Menzen, K. Richter, 2020, Molecular pharmaceutics.

Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53

J. Buchner, H. Kessler, M. Retzlaff, 2011, Nature Structural &Molecular Biology.

Closing in on the Hsp90 chaperone-client relationship.

J. Buchner, K. Richter, 2011, Structure.