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Structural Diversity in Calmodulin - Peptide Interactions

Current protein & peptide science, 2019-01, Vol.20 (11), p.1102

2019

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Aromatic stacking between nucleobase and enzyme promotes phosphate ester hydrolysis in dUTPase

Nucleic acids research, 2010-11, Vol.38 (20), p.7179

2010

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MASP-1, a Promiscuous Complement Protease: Structure of Its Catalytic Region Reveals the Basis of Its Broad Specificity

The Journal of immunology (1950), 2009-07, Vol.183 (2), p.1207-1214

2009

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Achieving Functionality Through Modular Build-up: Structure and Size Selection of Serine Oligopeptidases

Current protein & peptide science, 2019-01, Vol.20 (11), p.1089

2019

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Novel Polycondensed Partly Saturated β-Carbolines Including Ferrocene Derivatives: Synthesis, DFT-Supported Structural Analysis, Mechanism of Some Diastereoselective Transformations and a Preliminary Study of Their in vitro Antiproliferative Effects

Molecules (Basel, Switzerland), 2020-03, Vol.25 (7), p.1599

2020

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Comparison of ligand binding and conformational stability of human calmodulin with its homolog from the malaria parasite Plasmodium falciparum

FASEB bioAdvances, 2020-08, Vol.2 (8), p.489-505

2020

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C1 Inhibitor Serpin Domain Structure Reveals the Likely Mechanism of Heparin Potentiation and Conformational Disease

The Journal of biological chemistry, 2007-07, Vol.282 (29), p.21100-21109

2007

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Structures of calmodulin–melittin complexes show multiple binding modes lacking classical anchoring interactions

The Journal of biological chemistry, 2023-04, Vol.299 (4), p.104596-104596, Article 104596

2023

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Structural Evidence for Non-canonical Binding of Ca2+ to a Canonical EF-hand of a Conventional Myosin

The Journal of biological chemistry, 2005-12, Vol.280 (50), p.41458-41464

2005

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Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation

The Journal of biological chemistry, 2022-06, Vol.298 (6), p.101985-101985, Article 101985

2022

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Monospecific Inhibitors Show That Both Mannan-binding Lectin-associated Serine Protease-1 (MASP-1) and -2 Are Essential for Lectin Pathway Activation and Reveal Structural Plasticity of MASP-2

The Journal of biological chemistry, 2012-06, Vol.287 (24), p.20290-20300

2012

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Quantitative Characterization of the Activation Steps of Mannan-binding Lectin (MBL)-associated Serine Proteases (MASPs) Points to the Central Role of MASP-1 in the Initiation of the Complement Lectin Pathway

The Journal of biological chemistry, 2013-03, Vol.288 (13), p.8922-8934

2013

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Directed Evolution-Driven Increase of Structural Plasticity Is a Prerequisite for Binding the Complement Lectin Pathway Blocking MASP-Inhibitor Peptides

ACS chemical biology, 2022-04, Vol.17 (4), p.969-986

2022

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Origin of problems related to Staudinger reduction in carbopeptoid syntheses

Amino acids, 2016-11, Vol.48 (11), p.2619-2633

2016

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Structure and enzymatic mechanism of a moonlighting dUTPase

Acta crystallographica. Section D, Biological crystallography., 2013-12, Vol.69 (12), p.2298-2308

2013

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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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A true autoactivating enzyme. Structural insight into mannose-binding lectin-associated serine protease-2 activations

The Journal of biological chemistry, 2005-09, Vol.280 (39), p.33435

2005

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A self-compartmentalizing hexamer serine protease from Pyrococcus horikoshii: substrate selection achieved through multimerization

The Journal of biological chemistry, 2013-06, Vol.288 (24), p.17884-17894

2013

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Enzyme:Substrate Hydrogen Bond Shortening during the Acylation Phase of Serine Protease Catalysis

Biochemistry (Easton), 2006-02, Vol.45 (7), p.2114-2121

2006

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Direct contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPases

FEBS letters, 2010-07, Vol.584 (14), p.3047-3054

2010

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Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins

Nucleic acids research, 2007-01, Vol.35 (2), p.495

2007

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Prolyl Oligopeptidase Inhibition by N-Acyl-pro-pyrrolidine-type Molecules

Journal of medicinal chemistry, 2008-12, Vol.51 (23), p.7514-7522

2008

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Structure and mechanism of calmodulin binding to a signaling sphingolipid reveal new aspects of lipid-protein interactions

The FASEB journal, 2010-10, Vol.24 (10), p.3829-3839

2010

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Catalytically distinct states captured in a crystal lattice: the substrate-bound and scavenger states of acylaminoacyl peptidase and their implications for functionality

Acta crystallographica. Section D, Biological crystallography., 2015-03, Vol.71 (3), p.461-472

2015

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Crystallization and preliminary crystallographic analysis of dUTPase from the phi 11 helper phage of Staphylococcus aureus

Acta crystallographica. Section F, Structural biology and crystallization communications, 2011-11, Vol.67 (11), p.1411-1413

2011

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Structural Diversity in Calmodulin - Peptide Interactions

Aromatic stacking between nucleobase and enzyme promotes phosphate ester hydrolysis in dUTPase

MASP-1, a Promiscuous Complement Protease: Structure of Its Catalytic Region Reveals the Basis of Its Broad Specificity

Achieving Functionality Through Modular Build-up: Structure and Size Selection of Serine Oligopeptidases

Novel Polycondensed Partly Saturated β-Carbolines Including Ferrocene Derivatives: Synthesis, DFT-Supported Structural Analysis, Mechanism of Some Diastereoselective Transformations and a Preliminary Study of Their in vitro Antiproliferative Effects

Comparison of ligand binding and conformational stability of human calmodulin with its homolog from the malaria parasite Plasmodium falciparum

C1 Inhibitor Serpin Domain Structure Reveals the Likely Mechanism of Heparin Potentiation and Conformational Disease

Structures of calmodulin–melittin complexes show multiple binding modes lacking classical anchoring interactions

Structural Evidence for Non-canonical Binding of Ca2+ to a Canonical EF-hand of a Conventional Myosin

Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation

Monospecific Inhibitors Show That Both Mannan-binding Lectin-associated Serine Protease-1 (MASP-1) and -2 Are Essential for Lectin Pathway Activation and Reveal Structural Plasticity of MASP-2

Quantitative Characterization of the Activation Steps of Mannan-binding Lectin (MBL)-associated Serine Proteases (MASPs) Points to the Central Role of MASP-1 in the Initiation of the Complement Lectin Pathway

Directed Evolution-Driven Increase of Structural Plasticity Is a Prerequisite for Binding the Complement Lectin Pathway Blocking MASP-Inhibitor Peptides

Origin of problems related to Staudinger reduction in carbopeptoid syntheses

Structure and enzymatic mechanism of a moonlighting dUTPase

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

A true autoactivating enzyme. Structural insight into mannose-binding lectin-associated serine protease-2 activations

A self-compartmentalizing hexamer serine protease from Pyrococcus horikoshii: substrate selection achieved through multimerization

Enzyme:Substrate Hydrogen Bond Shortening during the Acylation Phase of Serine Protease Catalysis

Direct contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPases

Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins

Prolyl Oligopeptidase Inhibition by N-Acyl-pro-pyrrolidine-type Molecules

Structure and mechanism of calmodulin binding to a signaling sphingolipid reveal new aspects of lipid-protein interactions

Catalytically distinct states captured in a crystal lattice: the substrate-bound and scavenger states of acylaminoacyl peptidase and their implications for functionality

Crystallization and preliminary crystallographic analysis of dUTPase from the phi 11 helper phage of Staphylococcus aureus

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