Franz X. Schmid

Overview

Best Publications

• Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins.

  Gunter Fischer;Brigitte Wittmann-Liebold;Kurt Lang;Thomas Kiefhaber

  1991
  Citations

• GroE facilitates refolding of citrate synthase by suppressing aggregation.

  Johannes Buchner;Marion Schmidt;Miriam Fuchs;Rainer Jaenicke

  675
  Citations

• Catalysis of protein folding by prolyl isomerase.

  Kurt Lang;Franz X. Schmid;Gunter Fischer

  663
  Citations

• The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell.

  Gunter Fischer;Franz X. Schmid

  495
  Citations

• Two exposed amino acid residues confer thermostability on a cold shock protein.

  Dieter Perl;Uwe Mueller;Udo Heinemann;Franz X. Schmid

  434
  Citations

• Prolyl Isomerase: Enzymatic Catalysis of Slow Protein-Folding Reactions

  Franz X. Schmid

  429
  Citations

• Extremely rapid protein folding in the absence of intermediates.

  Thomas Schindler;Michael Herrler;Mohamed A. Marahiel;Franz X. Schmid

  404
  Citations

• A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor.

  G. Stoller;K. P. Rücknagel;K. H. Nierhaus;F. X. Schmid

  387
  Citations

• Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins.

  Dieter Perl;Christine Welker;Thomas Schindler;Katja Schröder

  385
  Citations

• Prolyl isomerases: role in protein folding.

  Franz X. Schmid;Lorenz M. Mayr;Matthias Mücke;Erhard Ralf Schönbrunner

  366
  Citations

• The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis

  Axel Mogk;Georg Homuth;Christian Scholz;Lana Kim

  350
  Citations

• The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity

  Susanne Behrens;Susanne Behrens;Raimund Maier;Hans de Cock;Franz X. Schmid

  343
  Citations

• Acid catalysis of the formation of the slow-folding species of RNase A: evidence that the reaction is proline isomerization.

  Franz X. Schmid;Robert L. Baldwin

  320
  Citations

• Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding.

  Christian Scholz;Gerlind Stoller;Toralf Zarnt;Gunter Fischer

  296
  Citations

• Selecting proteins with improved stability by a phage-based method

  Volker Sieber;Andreas Plückthun;Franz X. Schmid

  275
  Citations

• Catalysis of protein folding by cyclophilins from different species.

  Erhard Ralf Schönbrunner;Sabine Mayer;Maximilian Tropschug;Gunter Fischer

  238
  Citations

• The Effects of Ionic Strength on Protein Stability: The Cold Shock Protein Family

  Brian N. Dominy;Dieter Perl;Franz X. Schmid;Charles L. Brooks

  227
  Citations

• Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization.

  Thomas Kiefhaber;Rainer Quaas;Ulrich Hahn;Franz X. Schmid

  223
  Citations

• Mechanism of folding of ribonuclease A. Slow refolding is a sequential reaction via structural intermediates.

  Franz X. Schmid

  219
  Citations

• Role of proline isomerization in folding of ribonuclease A at low temperatures.

  Kem H. Cook;Franz X. Schmid;Robert L. Baldwin

  218
  Citations