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Cellular and ultra structural evidence for cytoskeletal localization of prolyl endopeptidase-like protein in neurons

Neuroscience, 2013-07, Vol.242, p.128-139

2013

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The PREPL A protein, a new member of the prolyl oligopeptidase family, lacking catalytic activity

Cellular and molecular life sciences : CMLS, 2005-10, Vol.62 (19-20), p.2376-2381

2005

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Substrate- and pH-dependent contribution of oxyanion binding site to the catalysis of prolyl oligopeptidase, a paradigm of the serine oligopeptidase family

Protein science, 2000-02, Vol.9 (2), p.353-360

2000

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Thiolate-Imidazolium Ion Pair Is Not an Obligatory Catalytic Entity of Cysteine Peptidases: The Active Site of Picornain 3C

Biochemistry (Easton), 2001-09, Vol.40 (35), p.10601-10606

2001

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Structure and Catalysis of Acylaminoacyl Peptidase: CLOSED AND OPEN SUBUNITS OF A DIMER OLIGOPEPTIDASE

The Journal of biological chemistry, 2011-01, Vol.286 (3), p.1987-1998

2011

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Unclosed β-Propellers Display Stable Structures: Implications for Substrate Access to the Active Site of Prolyl Oligopeptidase

Journal of molecular biology, 2005-02, Vol.346 (3), p.907-917

2005

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Catalysis of serine oligopeptidases is controlled by a gating filter mechanism

EMBO reports, 2000-09, Vol.1 (3), p.277-281

2000

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Flexibility of prolyl oligopeptidase: Molecular dynamics and molecular framework analysis of the potential substrate pathways

Proteins, structure, function, and bioinformatics, 2005-08, Vol.60 (3), p.504-512

2005

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Concerted Structural Changes in the Peptidase and the Propeller Domains of Prolyl Oligopeptidase are Required for Substrate Binding

Journal of molecular biology, 2004-07, Vol.340 (3), p.627-637

2004

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Trp42 rotamers report reduced flexibility when the inhibitor acetyl-pepstatin is bound to HIV-1 protease

Protein science, 2000-11, Vol.9 (11), p.2232-2245

2000

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Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue

The Journal of biological chemistry, 2001-01, Vol.276 (2), p.1262

2001

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Kosmotropic Salt Activation and Substrate Specificity of Poliovirus Protease 3C

Biochemistry (Easton), 2006-10, Vol.45 (39), p.12083-12089

2006

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Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site specific mutagenesis at the oxyanion binding site

The Journal of biological chemistry, 2002-11, Vol.277 (45), p.42613-42622

2002

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Electrostatic Environment at the Active Site of Prolyl Oligopeptidase Is Highly Influential during Substrate Binding

The Journal of biological chemistry, 2003-12, Vol.278 (49), p.48786-48793

2003

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The Noncatalytic β-Propeller Domain of Prolyl Oligopeptidase Enhances the Catalytic Capability of the Peptidase Domain

The Journal of biological chemistry, 2000-05, Vol.275 (20), p.15000-15005

2000

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Substrate-dependent Competency of the Catalytic Triad of Prolyl Oligopeptidase

The Journal of biological chemistry, 2002-11, Vol.277 (47), p.44597-44605

2002

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Role of the Oxyanion Binding Site and Subsites S1 and S2 in the Catalysis of Oligopeptidase B, a Novel Target for Antimicrobial Chemotherapy

Biochemistry (Easton), 2002-03, Vol.41 (12), p.4096-4106

2002

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Rate-determining steps in HIV-1 protease catalysis. The hydrolysis of the most specific substrate

The Journal of biological chemistry, 1996-12, Vol.271 (50), p.32180-32184

1996

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His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate

FEBS letters, 2004-07, Vol.571 (1), p.17-20

2004

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Conformational Stability and Catalytic Activity of HIV-1 Protease Are Both Enhanced at High Salt Concentration (∗)

The Journal of biological chemistry, 1996-03, Vol.271 (10), p.5458-5463

1996

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Substrate-Dependent Mechanisms in the Catalysis of Human Immunodeficiency Virus Protease

Biochemistry (Easton), 1994-08, Vol.33 (31), p.9351-9357

1994

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Tryptophan rotamers that report the conformational dynamics of proteins

Pure and applied chemistry, 2001-01, Vol.73 (3), p.415-419

2001

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Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase

Acta crystallographica. Section F, Structural biology and crystallization communications, 2005-10, Vol.61 (10), p.942-944

2005

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Structure–function studies on prolyl oligopeptidase

Acta crystallographica. Section A, Foundations of crystallography, 2004-08, Vol.60 (a1), p.s173-s173

2004

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Determination of the structure of serine-type protease acylaminoacyl peptidase (AAP)

Acta crystallographica. Section A, Foundations of crystallography, 2004-08, Vol.60 (a1), p.s176-s176

2004

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Cellular and ultra structural evidence for cytoskeletal localization of prolyl endopeptidase-like protein in neurons

The PREPL A protein, a new member of the prolyl oligopeptidase family, lacking catalytic activity

Substrate- and pH-dependent contribution of oxyanion binding site to the catalysis of prolyl oligopeptidase, a paradigm of the serine oligopeptidase family

Thiolate-Imidazolium Ion Pair Is Not an Obligatory Catalytic Entity of Cysteine Peptidases: The Active Site of Picornain 3C

Structure and Catalysis of Acylaminoacyl Peptidase: CLOSED AND OPEN SUBUNITS OF A DIMER OLIGOPEPTIDASE

Unclosed β-Propellers Display Stable Structures: Implications for Substrate Access to the Active Site of Prolyl Oligopeptidase

Catalysis of serine oligopeptidases is controlled by a gating filter mechanism

Flexibility of prolyl oligopeptidase: Molecular dynamics and molecular framework analysis of the potential substrate pathways

Concerted Structural Changes in the Peptidase and the Propeller Domains of Prolyl Oligopeptidase are Required for Substrate Binding

Trp42 rotamers report reduced flexibility when the inhibitor acetyl-pepstatin is bound to HIV-1 protease

Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue

Kosmotropic Salt Activation and Substrate Specificity of Poliovirus Protease 3C

Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site specific mutagenesis at the oxyanion binding site

Electrostatic Environment at the Active Site of Prolyl Oligopeptidase Is Highly Influential during Substrate Binding

The Noncatalytic β-Propeller Domain of Prolyl Oligopeptidase Enhances the Catalytic Capability of the Peptidase Domain

Substrate-dependent Competency of the Catalytic Triad of Prolyl Oligopeptidase

Role of the Oxyanion Binding Site and Subsites S1 and S2 in the Catalysis of Oligopeptidase B, a Novel Target for Antimicrobial Chemotherapy

Rate-determining steps in HIV-1 protease catalysis. The hydrolysis of the most specific substrate

His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate

Conformational Stability and Catalytic Activity of HIV-1 Protease Are Both Enhanced at High Salt Concentration (∗)

Substrate-Dependent Mechanisms in the Catalysis of Human Immunodeficiency Virus Protease

Tryptophan rotamers that report the conformational dynamics of proteins

Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase

Structure–function studies on prolyl oligopeptidase

Determination of the structure of serine-type protease acylaminoacyl peptidase (AAP)

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