Michael R. Maurizi

Overview

Best Publications

• Posttranslational quality control: folding, refolding, and degrading proteins.

  Sue Wickner;Michael R. Maurizi;Susan Gottesman

  1575
  Citations

• Protein quality control: triage by chaperones and proteases.

  S Gottesman;S Wickner;M R Maurizi

  692
  Citations

• A molecular chaperone, ClpA, functions like DnaK and DnaJ

  Sue Wickner;Susan Gottesman;Dorota Skowyra;Joel Hoskins

  514
  Citations

• Homology in Structural Organization BetweenE. coliClpAP Protease and the Eukaryotic 26 S Proteasome

  Martin Kessel;Michael R. Maurizi;Bernard Kim;Eva Kocsis

  434
  Citations

• The RssB response regulator directly targets ςS for degradation by ClpXP

  YanNing Zhou;Susan Gottesman;Joel R. Hoskins;Michael R. Maurizi

  413
  Citations

• ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities.

  S Gottesman;W.P. Clark;V de Crecy-Lagard;M.R. Maurizi

  402
  Citations

• Clp P represents a unique family of serine proteases.

  M R Maurizi;W P Clark;S H Kim;S Gottesman

  395
  Citations

• Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli.

  M R Maurizi;W P Clark;Y Katayama;S Rudikoff

  370
  Citations

• The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component.

  Y Katayama;S Gottesman;J Pumphrey;S Rudikoff

  351
  Citations

• Enzymatic and Structural Similarities between the Escherichia coli ATP-dependent Proteases, ClpXP and ClpAP*

  Regis Grimaud;Martin Kessel;Fabienne Beuron;Alasdair C. Steven

  316
  Citations

• Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease.

  Fusheng Guo;Michael R. Maurizi;Lothar Esser;Di Xia

  292
  Citations

• Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP.

  Satyendra K. Singh;Regis Grimaud;Joel R. Hoskins;Sue Wickner

  289
  Citations

• ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions

  Laurence Van Melderen;Minh Hoa Dao Thi;Paolo Lecchi;Susan Gottesman

  270
  Citations

• The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site.

  Istvan Botos;Edward E. Melnikov;Scott Cherry;Joseph E. Tropea

  267
  Citations

• A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease

  Nan Wang;Susan Gottesman;Mark C. Willingham;Michael M. Gottesman

  256
  Citations

• Regulatory Subunits of Energy-Dependent Proteases

  Susan Gottesman;Michael R Maurizi;Sue Wickner

  245
  Citations

• Processive degradation of proteins by the ATP-dependent Clp protease from Escherichia coli. Requirement for the multiple array of active sites in ClpP but not ATP hydrolysis.

  M.W. Thompson;S.K. Singh;M.R. Maurizi

  244
  Citations

• ATP-dependent protease La (lon) from Escherichia coli

  A L Goldberg;R P Moerschell;C H Chung;M R Maurizi

  243
  Citations

• Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates.

  M W Thompson;M R Maurizi

  225
  Citations

• The ATP-dependent Clp protease of Escherichia coli : sequence of clpA and identification of a Clp-specific substrate

  S Gottesman;W P Clark;M R Maurizi

  215
  Citations