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The catalytic triad of serine peptidases

Cellular and molecular life sciences : CMLS, 2005-10, Vol.62 (19-20), p.2161-2172

Polgár, L

2005

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The prolyl oligopeptidase family

Cellular and molecular life sciences : CMLS, 2002-02, Vol.59 (2), p.349-362

Polgár, L

2002

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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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Effect of Rubber Polarity on Cluster Formation in Rubbers Cross-Linked with Diels–Alder Chemistry

Macromolecules, 2017-11, Vol.50 (22), p.8955-8964

2017

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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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Platelet impedance adhesiometry: A novel technique for the measurement of platelet adhesion and spreading

International journal of laboratory hematology, 2018-06, Vol.40 (3), p.372-381

2018

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Prolyl Oligopeptidase: An Unusual β-Propeller Domain Regulates Proteolysis

Cell, 1998-07, Vol.94 (2), p.161-170

1998

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Cross-linking of rubber in the presence of multi-functional cross-linking aids via thermoreversible Diels-Alder chemistry

European polymer journal, 2016-09, Vol.82, p.208-219

2016

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Diapause induction in aphid parasitoids

Entomologia experimentalis et applicata, 2000-10, Vol.97 (1), p.21-27

2000

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Sustainable EPM rubber compounds

Polymer-plastics technology and engineering, 2020-08, Vol.59 (12), p.1379-1385

2020

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An easy synthetic way to exfoliate and stabilize MWCNTs in a thermoplastic pyrrole-containing matrix assisted by hydrogen bonds

RSC advances, 2016-01, Vol.6 (89), p.85829-85837

2016

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Thermally reversible rubber-toughened thermoset networks via Diels–Alder chemistry

European polymer journal, 2016-01, Vol.74, p.229-240

2016

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Synthesis and Linear Viscoelasticity of Polystyrene Stars with a Polyketone Core

Macromolecules, 2015-09, Vol.48 (18), p.6662-6671

2015

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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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Use of Diels–Alder Chemistry for Thermoreversible Cross-Linking of Rubbers: The Next Step toward Recycling of Rubber Products?

Macromolecules, 2015-10, Vol.48 (19), p.7096-7105

2015

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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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Per os efficacy of Ajuga extracts against sucking insects

Pest management science, 2004-11, Vol.60 (11), p.1099-1104

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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Oligopeptidase B: A New Type of Serine Peptidase with a Unique Substrate-Dependent Temperature Sensitivity

Biochemistry (Easton), 1999-11, Vol.38 (47), p.15548-15555

Polgar, L

1999

Volltextzugriff (PDF)

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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Practical application of thermoreversibly Cross-linked rubber products

IOP conference series. Materials Science and Engineering, 2017-07, Vol.223 (1), p.12004

2017

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A potential processing enzyme in prokaryotes: Oligopeptidase B, a new type of serine peptidase

Proteins, structure, function, and bioinformatics, 1997-07, Vol.28 (3), p.375-379

Polgar, L

1997

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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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Low Barrier Hydrogen Bond Is Absent in the Catalytic Triads in the Ground State but Is Present in a Transition-state Complex in the Prolyl Oligopeptidase Family of Serine Proteases

The Journal of biological chemistry, 1997-10, Vol.272 (41), p.25547-25554

1997

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The catalytic triad of serine peptidases

The prolyl oligopeptidase family

Catalysis of serine oligopeptidases is controlled by a gating filter mechanism

Effect of Rubber Polarity on Cluster Formation in Rubbers Cross-Linked with Diels–Alder Chemistry

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

Platelet impedance adhesiometry: A novel technique for the measurement of platelet adhesion and spreading

Prolyl Oligopeptidase: An Unusual β-Propeller Domain Regulates Proteolysis

Cross-linking of rubber in the presence of multi-functional cross-linking aids via thermoreversible Diels-Alder chemistry

Diapause induction in aphid parasitoids

Sustainable EPM rubber compounds

An easy synthetic way to exfoliate and stabilize MWCNTs in a thermoplastic pyrrole-containing matrix assisted by hydrogen bonds

Thermally reversible rubber-toughened thermoset networks via Diels–Alder chemistry

Synthesis and Linear Viscoelasticity of Polystyrene Stars with a Polyketone Core

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

Use of Diels–Alder Chemistry for Thermoreversible Cross-Linking of Rubbers: The Next Step toward Recycling of Rubber Products?

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

Per os efficacy of Ajuga extracts against sucking insects

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

Oligopeptidase B: A New Type of Serine Peptidase with a Unique Substrate-Dependent Temperature Sensitivity

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

Practical application of thermoreversibly Cross-linked rubber products

A potential processing enzyme in prokaryotes: Oligopeptidase B, a new type of serine peptidase

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

Low Barrier Hydrogen Bond Is Absent in the Catalytic Triads in the Ground State but Is Present in a Transition-state Complex in the Prolyl Oligopeptidase Family of Serine Proteases

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