M. Maurizi

发表

Active-site ligand binding and subunit interactions in glutamine synthetase from Escherichia coli.

M. Maurizi, A. Ginsburg, 1985, Current topics in cellular regulation.

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

S. Gottesman, M. Maurizi, S. Wickner, 1999, Science.

At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease.

F P Booy, A C Steven, E Kocsis, 1998, Journal of structural biology.

Alternating translocation of protein substrates from both ends of ClpXP protease

A. Steven, J. Ortega, M. Maurizi, 2002, The EMBO journal.

Enzymatic and Structural Similarities between theEscherichia coli ATP-dependent Proteases, ClpXP and ClpAP*

A. Steven, M. Kessel, M. Maurizi, 1998, The Journal of Biological Chemistry.

Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP.

M. Kessel, M. Maurizi, A. Ginsburg, 1998, Biochemistry.

ClpA and ClpX ATPases bind simultaneously to opposite ends of ClpP peptidase to form active hybrid complexes.

Alasdair C Steven, A. Steven, J. Ortega, 2004, Journal of structural biology.

A Single ClpS Monomer Is Sufficient to Direct the Activity of the ClpA Hexamer*

Sarada Viswanathan, M. Maurizi, S. Singh, 2010, The Journal of Biological Chemistry.

Endopeptidase Clp: ATP-dependent Clp protease from Escherichia coli.

S. Kim, M. Maurizi, S. Singh, 1994, Methods in enzymology.

Selective, energy-dependent proteolysis in Escherichia coli.

S. Gottesman, M. Kessel, M. Maurizi, 1995, Cold Spring Harbor symposia on quantitative biology.

ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease.

M. Maurizi, S. Singh, F. Guo, 1999, Biochemistry.

Concurrent Chaperone and Protease Activities of ClpAP and the Requirement for the N-terminal ClpA ATP Binding Site for Chaperone Activity*

J. Hoskins, M. Maurizi, M. Pak, 1999, The Journal of Biological Chemistry.

Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP.

A. Steven, J. Ortega, T. Ishikawa, 2000, Molecular cell.

Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP.

J. Hoskins, M. Maurizi, S. Wickner, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Translocation pathway of protein substrates in ClpAP protease

A. Steven, M. Kessel, T. Ishikawa, 2001, Proceedings of the National Academy of Sciences of the United States of America.

The N-terminal substrate-binding domain of ClpA unfoldase is highly mobile and extends axially from the distal surface of ClpAP protease.

A. Steven, T. Ishikawa, M. Maurizi, 2004, Journal of structural biology.

4-O-Carboxymethyl Ascochlorin Causes ER Stress and Induced Autophagy in Human Hepatocellular Carcinoma Cells*

Young-Chae Chang, M. Maurizi, J. Kang, 2012, The Journal of Biological Chemistry.

PROTEIN STRUCTURE REPORT Crystal structure of the N-terminal domain of E. coli

A. Wlodawer, A. Gustchina, Mi Li, 2005 .

Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP.

R. Ghirlando, J. Ortega, A. Guarné, 2010, Chemistry & biology.

Mitochondrial ClpP activity is required for cisplatin resistance in human cells.

M. Maurizi, Yang Zhang, 2016, Biochimica et biophysica acta.

Here's the hook: similar substrate binding sites in the chaperone domains of Clp and Lon.

M. Maurizi, S. Wickner, 1999, Proceedings of the National Academy of Sciences of the United States of America.

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

S. Gottesman, J. Hoskins, D. Skowyra, 1994, Proceedings of the National Academy of Sciences of the United States of America.

A multiple-component, ATP-dependent protease from Escherichia coli.

S. Gottesman, M. Maurizi, Y. Katayama-Fujimura, 1987, The Journal of biological chemistry.

Regulatory Subunits of Energy-Dependent Proteases

S. Gottesman, M. Maurizi, S. Wickner, 1997, Cell.

ATP-promoted interaction between Clp A and Clp P in activation of Clp protease from Escherichia coli.

M. Maurizi, 1991, Biochemical Society transactions.

The role of the ClpA chaperone in proteolysis by ClpAP.

J. Hoskins, M. Maurizi, M. Pak, 1998, Proceedings of the National Academy of Sciences of the United States of America.

The C1pP Component of Clp Protease Is the a32-Dependent Heat Shock Protein F21.5

S. Gottesman, S. Rudikoff, J. Pumphrey, 2022 .

Nucleotide‐dependent oligomerization of C1pB from Escherichia coli

M. Kessel, M. Zółkiewski, M. Maurizi, 1999, Protein science : a publication of the Protein Society.

PinA Inhibits ATP Hydrolysis and Energy-dependent Protein Degradation by Lon Protease*

L. Van Melderen, M. Maurizi, L. Simon, 1998, The Journal of Biological Chemistry.

Isolation and Characterization of the Phage T4 PinA Protein, an Inhibitor of the ATP-dependent Lon Protease ofEscherichia coli *

M. Maurizi, L. Simon, J. Hilliard, 1998, The Journal of Biological Chemistry.

Turnover of mitochondrial steroidogenic acute regulatory (StAR) protein by Lon protease: the unexpected effect of proteasome inhibitors.

Z. Granot, A. Oppenheim, O. Kobiler, 2007, Molecular endocrinology.

Degradation in vitro of bacteriophage lambda N protein by Lon protease from Escherichia coli.

M. Maurizi, 1987, The Journal of biological chemistry.

Mutational analysis demonstrates different functional roles for the two ATP-binding sites in ClpAP protease from Escherichia coli.

Sudheer Kumar Singh, M. Maurizi, S. Singh, 1994, The Journal of biological chemistry.

Local and global mobility in the ClpA AAA+ chaperone detected by cryo-electron microscopy: functional connotations.

A. Steven, T. Ishikawa, M. Maurizi, 2010, Structure.

AAA proteins: in search of a common molecular basis

M. Maurizi, Chou-Chi H. Li, C. Li, 2001, EMBO reports.

Proteolysis in bacterial sporulation.

M. Maurizi, R. Switzer, 1980, Current topics in cellular regulation.

International meeting on cellular functions of AAA proteins

M. Maurizi, Chou-Chi H. Li, Chou-chi Li, 2001 .

Degradation of L-glutamate dehydrogenase from Escherichia coli: allosteric regulation of enzyme stability.

M. Maurizi, F. Rasulova, 2002, Archives of biochemistry and biophysics.

Clp Endopeptidase Homologs in Plants and Animals

M. Maurizi, A. Clarke, Z. Adam, 2013 .

Functional Proteolytic Complexes of the Human Mitochondrial ATP-dependent Protease, hClpXP*

A. Steven, J. Ortega, M. Maurizi, 2002, The Journal of Biological Chemistry.

[81] Aspartate transcarbamylase from Bacillus subtilis☆

M. Maurizi, R. Switzer, J. Brabson, 1985 .

Selective Inactivation and Degradation of Enzymes in Sporulating Bacteria

M. Maurizi, R. Switzer, K. Flom, 1979 .

ATP-dependent Clp protease ATP-binding subunit clpA/ATP-dependent Clp protease adaptor protein clpS

L. Esser, M. Maurizi, D. Xia, 2005 .

Mg2+ is bound to glutamine synthetase extracted from bovine or ovine brain in the presence of L-methionine-S-sulfoximine phosphate.

M. Maurizi, A. Ginsburg, H. Pinkofsky, 1986, Archives of biochemistry and biophysics.

Reactivation of glutamine synthetase from Escherichia coli after auto-inactivation with L-methionine-S-sulfoximine, ATP, and Mn2+.

M. Maurizi, A. Ginsburg, 1982, The Journal of biological chemistry.

Slicing a protease: Structural features of the ATP‐dependent Lon proteases gleaned from investigations of isolated domains

A. Wlodawer, A. Gustchina, M. Maurizi, 2006, Protein science : a publication of the Protein Society.

Clp P represents a unique family of serine proteases.

S. Gottesman, S. Kim, M. Maurizi, 1990, The Journal of biological chemistry.

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

A. Goldberg, C. Chung, M. Maurizi, 1994, Methods in enzymology.

Proteases and protein degradation inEscherichia coli

M. Maurizi, M. R. Maurizi, 2005, Experientia.

Effects of relaxin on the endometrial stroma. Studies in mice.

M. Maurizi, M. Bigazzi, G. Bani, 1995, Biology of reproduction.

Turnover of Endogenous SsrA-tagged Proteins Mediated by ATP-dependent Proteases in Escherichia coli*

M. Maurizi, Mark Lies, Michael R Maurizi, 2008, Journal of Biological Chemistry.

The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate.

S. Gottesman, M. Maurizi, S Gottesman, 1990, The Journal of biological chemistry.

Crystal structure of the AAA + a domain of E . coli Lon protease at 1 . 9 A resolution

A. Wlodawer, A. Gustchina, M. Maurizi, 2003 .

Crystal Structure of the Heterodimeric Complex of the Adaptor, ClpS, with the N-domain of the AAA+ Chaperone, ClpA*

L. Esser, M. Maurizi, D. Xia, 2002, The Journal of Biological Chemistry.

Human Mitochondrial ClpP Is a Stable Heptamer That Assembles into a Tetradecamer in the Presence of ClpX*

J. Ortega, M. Maurizi, A. Ginsburg, 2005, Journal of Biological Chemistry.

Original article: relaxin reduces the number of circulating platelets and depresses platelet release from megakaryocytes: studies in rats.

D. Bani, M. Maurizi, M. Bigazzi, 1995, Platelets.

The Catalytic Domain of Escherichia coli Lon Protease Has a Unique Fold and a Ser-Lys Dyad in the Active Site*

A. Wlodawer, Z. Dauter, A. Gustchina, 2004, Journal of Biological Chemistry.

The purification of the Chlamydomonas reinhardtii chloroplast ClpP complex: additional subunits and structural features

W. Majeran, G. Friso, K. V. van Wijk, 2012, Plant Molecular Biology.

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

S. Gottesman, S. Rudikoff, J. Pumphrey, 1990, The Journal of biological chemistry.

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

S. Gottesman, S. Rudikoff, J. Pumphrey, 1988, The Journal of biological chemistry.

Regulation by proteolysis: energy-dependent proteases and their targets

S. Gottesman, M. Maurizi, Susan GOTIESMANl, 1992, Microbiological reviews.

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

M. Willingham, M. Gottesman, S. Gottesman, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Insertional mutagenesis of the lon gene in Escherichia coli: lon is dispensable

S. Gottesman, M. Maurizi, P. Trisler, 1985, Journal of bacteriology.

Regulation by Proteolysis: Energy-Dependent Proteases

M. Maurizi, Susan GOTIESMANl, 2003 .

Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone.

L. Esser, M. Maurizi, D. Xia, 2004, Journal of structural biology.

Subunit‐specific degradation of the UmuD/D′ heterodimer by the ClpXP protease: the role of trans recognition in UmuD′ stability

R. Woodgate, M. Maurizi, F. Rasulova, 2000, The EMBO journal.

RcsA, an unstable positive regulator of capsular polysaccharide synthesis

S. Gottesman, M. Maurizi, V. Stout, 1991, Journal of bacteriology.

Aspartate Transcarbamylase Synthesis Ceases Prior to Inactivation of the Enzyme in Bacillus subtilis

M. Maurizi, R. Switzer, 1978, Journal of bacteriology.

Crystal Structure of ClpA, an Hsp100 Chaperone and Regulator of ClpAP Protease*

L. Esser, M. Maurizi, D. Xia, 2002, The Journal of Biological Chemistry.

Protein quality control: triage by chaperones and proteases.

S. Gottesman, M. Maurizi, S. Wickner, 1997, Genes & development.

The RssB response regulator directly targets sigma(S) for degradation by ClpXP.

S. Gottesman, J. Hoskins, M. Maurizi, 2001, Genes & development.

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

J. Hoskins, M. Maurizi, S. Wickner, 2000, Proceedings of the National Academy of Sciences of the United States of America.

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

S. Gottesman, V. de Crécy-Lagard, V. Crécy-Lagard, 1993, The Journal of biological chemistry.

ATP-dependent Degradation of CcdA by Lon Protease

S. Gottesman, M. Couturier, L. Van Melderen, 1996, The Journal of Biological Chemistry.

Synthesis, processing, and localization of human Lon protease.

M. Gottesman, M. Maurizi, L. Emmert-Buck, 1994, The Journal of biological chemistry.

Crystal structure at 1.9A of E. coli ClpP with a peptide covalently bound at the active site.

M. Maurizi, Michael R Maurizi, A. Szyk, 2006, Journal of structural biology.

Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP.

M. Maurizi, S. Kang, T. Mueser, 2004, Journal of structural biology.

Role of the Heat Shock Protein DnaJ in the Lon-dependent Degradation of Naturally Unstable Proteins*

S. Gottesman, M. Maurizi, Y. Jubete, 1996, The Journal of Biological Chemistry.

Structure and Functional Properties of the Active Form of the Proteolytic Complex, ClpP1P2, from Mycobacterium tuberculosis*

A. Goldberg, A. Wlodawer, T. Akopian, 2016, The Journal of Biological Chemistry.

Structure and Functional Properties of the Active Form of the Proteolytic Complex , ClpP 1 P 2 , from Mycobacterium tuberculosis *

A. Goldberg, A. Wlodawer, T. Akopian, 2016 .

Chapter 794 – Endopeptidase Clp

M. Maurizi, 2013 .

Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber

Y. Kim, M. Maurizi, S. Cha, 2010, The EMBO journal.

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. Maurizi, S. Singh, M. W. Thompson, 1994, The Journal of biological chemistry.

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

M. Maurizi, M R Maurizi, M W Thompson, 1994, The Journal of biological chemistry.

Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome.

B L Trus, A C Steven, E Kocsis, 1995, Journal of molecular biology.

ClpX Shifts into High Gear to Unfold Stable Proteins

Michael R. Maurizi, G. Stan, M. Maurizi, 2013, Cell.

Biochemical Properties and Biological Functions of Atp-Dependent Proteases In Bacterial Cells

M. Maurizi, 1998 .

The Molecular Chaperone, ClpA, Has a Single High Affinity Peptide Binding Site per Hexamer*

G. Piszczek, M. Maurizi, A. Ginsburg, 2005, Journal of Biological Chemistry.

Binding of the ClpA Unfoldase Opens the Axial Gate of ClpP Peptidase*

A. Steven, M. Maurizi, G. Effantin, 2010, The Journal of Biological Chemistry.

Protein binding and disruption by Clp/Hsp100 chaperones.

M. Maurizi, D. Xia, 2004, Structure.

Love it or cleave it: Tough choices in protein quality control

M. Maurizi, 2002, Nature Structural Biology.

Six‐fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP‐dependent activator, ClpY

A C Steven, E Kocsis, M Kessel, 1996, FEBS letters.

The N-degradome of Escherichia coli

L. Jenkins, M. Maurizi, Matthew A. Humbard, 2013, The Journal of Biological Chemistry.

Functional Domains of the ClpA and ClpX Molecular Chaperones Identified by Limited Proteolysis and Deletion Analysis*

A. Steven, M. Maurizi, Tomokazu Ishikawa, 2001, The Journal of Biological Chemistry.

Surviving Starvation

S. Gottesman, M. Maurizi, 2001, Science.

The N-degradome ofEscherichia coli LIMITEDPROTEOLYSISINVIVOGENERATESALARGEPOOLOFPROTEINSBEARING N-DEGRONS *

L. Jenkins, M. Maurizi, Matthew A. Humbard, 2013 .

Distances between active site probes in glutamine synthetase from Escherichia coli: fluorescence energy transfer in free and in stacked dodecamers.

M. Maurizi, A. Ginsburg, P. Kasprzyk, 1986, Biochemistry.

The purification of the Chlamydomonas reinhardtii chloroplast ClpP complex: additional subunits and structural features

W. Majeran, G. Friso, A. Steven, 2012, Plant Molecular Biology.

Importance of heptameric ring integrity for activity of Escherichia coli ClpP.

M. Maurizi, E. Kempner, M. W. Thompson, 1998, European journal of biochemistry.

Stability and Characterization of the ATP-dependent Clp Protease from Escherichia coli

M. Maurizi, 1992 .

ATP-dependent proteases: Docking of components in a bacterial complex

Michael R. Maurizi, Alasdair C. Steven, David Belnap, 2000, Nature.

Adenosine 5'-triphosphate analogues as structural probes for Escherichia coli glutamine synthetase.

M. Maurizi, A. Ginsburg, 1986, Biochemistry.

Active site ligand stabilization of quaternary structures of glutamine synthetase from Escherichia coli.

M. Maurizi, A. Ginsburg, 1982, The Journal of biological chemistry.

Structure of the N-terminal fragment of Escherichia coli Lon protease.

A. Wlodawer, Z. Dauter, A. Gustchina, 2010, Acta crystallographica. Section D, Biological crystallography.

Immunochemical studies of the inactivation of aspartate transcarbamylase by stationary phase Bacillus subtilis cells. Evidence for selective, energy-dependent degradation.

M. Maurizi, R. Switzer, J. Brabson, 1978, The Journal of biological chemistry.

4-O-Carboxymethyl Ascochlorin Causes ER Stress and Induced Autophagy in Human Hepatocellular Carcinoma Cells*

Young-Chae Chang, M. Maurizi, J. Kang, 2012, The Journal of Biological Chemistry.