H. Schönfeld

发表

The heat-sensitive Escherichia coli grpE280 phenotype: impaired interaction of GrpE(G122D) with DnaK.

P. Christen, S. Züger, J. Grimshaw, 2005, Journal of molecular biology.

Three-State Equilibrium of Escherichia coli Trigger Factor

H. Patzelt, B. Bukau, G. Kramer, 2002, Biological chemistry.

Sequential action of two hsp 70 complexes during protein import into mitochondria a polypeptide chain oscillates randomly by diffusion within

A. Azem, W. Oppliger, S. Rospert, 2013 .

Investigation of the molecular chaperone DnaJ by analytical ultracentrifugation

M. Zulauf, D. Schmidt, H. Schönfeld, 1995 .

Use of prior vaccinations for the development of new vaccines.

A. Trzeciak, H. Matile, H. Etlinger, 1990, Science.

Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.

B. Bukau, A. Buchberger, T. Hesterkamp, 1996, Journal of molecular biology.

Reversible Thermal Transition in GrpE, the Nucleotide Exchange Factor of the DnaK Heat-Shock System*

P. Christen, I. Jelesarov, J. Grimshaw, 2001, The Journal of Biological Chemistry.

Refolding of Substrates Bound to Small Hsps Relies on a Disaggregation Reaction Mediated Most Efficiently by ClpB/DnaK*

B. Bukau, E. Vierling, A. Mogk, 2003, Journal of Biological Chemistry.

d-Peptide Ligands for the Co-chaperone DnaJ*

P. Christen, H. Schönfeld, B. Feifel, 1998, The Journal of Biological Chemistry.

Control of the DnaK Chaperone Cycle by Substoichiometric Concentrations of the Co-chaperones DnaJ and GrpE*

P. Christen, H. Schönfeld, E. Pierpaoli, 1998, The Journal of Biological Chemistry.

Altered differentiation of limb bud cells by transforming growth factors-beta isolated from bone matrix and from platelets.

H. Schönfeld, A. Kistler, B. Pöschl, 1991, Bone and mineral.

Cyclophilin-promoted folding of mouse dihydrofolate reductase does not include the slow conversion of the late-folding intermediate to the active enzyme.

P. Caspers, O. von Ahsen, N. Pfanner, 2000, Journal of molecular biology.

Preoperative isolation of a reversible protein-protein crosslink generated in 50 S subunits of Escherichia coli ribosomes and identification of its components.

K. Foulaki, H. Schönfeld, 1987, Analytical biochemistry.

Glycerol affects the quantification of aspartate and glutamate in acid-hydrolyzed proteins

M. Fountoulakis, H. Schönfeld, G. Oesterhelt, 1998, Amino Acids.

The intermediate filament protein vimentin binds specifically to a recombinant integrin alpha2/beta1 cytoplasmic tail complex and co-localizes with native alpha2/beta1 in endothelial cell focal adhesions.

N. Kieffer, S. Kreis, B. Steiner, 2005, Experimental cell research.

Glutamine Synthetase Isolated from Human Brain: Octameric Structure and Homology of Partial Primary Structure with Human Liver Glutamine Synthetase

H. Langen, F. Müller, G. Burbaeva, 2002, Biochemistry (Moscow).

Molecular chaperones and their interactions investigated by analytical ultracentrifugation and other methodologies.

J. Behlke, H. Schönfeld, 1998, Methods in enzymology.

Structure and function of the dihydropteroate synthase from Staphylococcus aureus.

M. Page, A. D'arcy, I. Hampele, 1997, Journal of molecular biology.

Sequential action of two hsp70 complexes during protein import into mitochondria

A. Azem, W. Oppliger, S. Rospert, 1997, The EMBO journal.

Genetic Analysis and Functional Characterization of the Streptococcus pneumoniae vic Operon

M. Page, C. Thompson, R. Lange, 2002, Infection and Immunity.

Myeloid-derived growth factor (C19orf10) mediates cardiac repair following myocardial infarction

A. Ganser, H. Niessen, J. Bauersachs, 2015, Nature Medicine.

The intermediate filament protein vimentin binds specifically to a recombinant integrin α2/β1 cytoplasmic tail complex and co-localizes with native α2/β1 in endothelial cell focal adhesions

N. Kieffer, S. Kreis, B. Steiner, 2005 .

Substrate Specificity of the SecB Chaperone*

J. Schneider-Mergener, S. Rüdiger, B. Bukau, 1999, The Journal of Biological Chemistry.

EMC10 (Endoplasmic Reticulum Membrane Protein Complex Subunit 10) Is a Bone Marrow–Derived Angiogenic Growth Factor Promoting Tissue Repair After Myocardial Infarction

J. Gogos, M. Gaestel, M. Klintschar, 2017, Circulation.

The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system.

P. Christen, A. Baici, H. Schönfeld, 1997, Journal of molecular biology.

Cooperative unfolding of apolipoprotein A-1 induced by chemical denaturation.

J. Seelig, H. Heerklotz, X. Li-Blatter, 2018, Biophysical chemistry.

Thermal protein unfolding by differential scanning calorimetry and circular dichroism spectroscopy Two-state model versus sequential unfolding

J. Seelig, H. Schönfeld, 2016, Quarterly Reviews of Biophysics.

Thermodynamics of protein self-association and unfolding. The case of apolipoprotein A-I.

J. Seelig, A. Ziegler, H. Schönfeld, 2012, Biochemistry.

The HspR regulon of Streptomyces coelicolor: a role for the DnaK chaperone as a transcriptional co‐repressor†

G. Bucca, Colin P. Smith, H. Schönfeld, 2000, Molecular microbiology.

A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32.

H. Bujard, G. Multhaup, S. Rüdiger, 1996, The EMBO journal.

Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria.

J. Schneider-Mergener, K. Nakahigashi, S. Rüdiger, 1996, Journal of molecular biology.

Self-Association of Apo A-1 Studied with Dynamic and Static Light Scattering.

J. Seelig, D. Roessner, H. Schönfeld, 2016, Journal of Physical Chemistry B.

Thermal unfolding of apolipoprotein A-1. Evaluation of methods and models.

T. Schulthess, J. Seelig, H. Schönfeld, 2015, Biochemistry.

Potassium ions and the molecular-chaperone activity of DnaK.

P. Christen, H. Schönfeld, E. Sandmeier, 1996, European journal of biochemistry.

d-Peptides as Inhibitors of the DnaK/DnaJ/GrpE Chaperone System*

P. Christen, H. Schönfeld, B. Feifel, 2003, Journal of Biological Chemistry.

The DnaK Chaperone System of Escherichia coli: Quaternary Structures and Interactions of the DnaK and GrpE Components (*)

B. Bukau, D. Schmidt, H. Schönfeld, 1995, The Journal of Biological Chemistry.

Increased solubility of trimethoprim-resistant type S1 DHFR from Staphylococcus aureus in Escherichia coli cells overproducing the chaperonins GroEL and GroES.

G. Dale, H. Langen, M. Stieger, 1994, Protein engineering.

Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions.

J. Behlke, O. Ristau, H. Schönfeld, 1997, Biochemistry.

Quasi-elastic light scattering and analytical ultracentrifugation are indispensable tools for the purification and characterization of recombinant proteins.

F. Müller, H. Schönfeld, B. Pöschl, 1998, Biochemical Society transactions.

Myeloid-derived growth factor (C19orf10) mediates cardiac repair following myocardial infarction

A. Ganser, J. Bauersachs, K. Wollert, 2015, Nature Medicine.

Crystallization and preliminary crystallographic analysis of a TNF-beta-55 kDa TNF receptor complex.

F. Winkler, D. Banner, R. Gentz, 1993, Journal of molecular biology.

Control of the DnaK Chaperone Cycle by Substoichiometric Concentrations of the Co-chaperones DnaJ and GrpE*

P. Christen, H. Schönfeld, E. Sandmeier, 1998, The Journal of Biological Chemistry.

Thermodynamics of protein self-association and unfolding. The case of apolipoprotein A-I.

H. Schönfeld, André Ziegler, Joachim Seelig, 2012, Biochemistry.