Purification, crystallization and preliminary X-ray analysis of human mannose-binding lectin-associated serine protease-1 (MASP-1) catalytic region.

No abstract is available for this paper.

• Publication year

  2008

• Venue

  Acta Crystallographica. Section F : Structural Biology and Crystallization Communications

• Publication date

  2008-09-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1107/S174430910802294XPMID 18765903PMCID PMC2531277
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Kinetics and kinematics for translational motions in microgravity during parabolic flight.

  2009cited by this paper
• Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: structure of the active catalytic region of C1r.

  2008cited by this paper
• C1 Inhibitor Serpin Domain Structure Reveals the Likely Mechanism of Heparin Potentiation and Conformational Disease*

  2007cited by this paper
• Serine proteases of the classical and lectin pathways: similarities and differences.

  2007cited by this paper
• Complement activating soluble pattern recognition molecules with collagen-like regions, mannan-binding lectin, ficolins and associated proteins.

  2007cited by this paper
• Cooperation between MASP-1 and MASP-2 in the generation of C3 convertase through the MBL pathway.

  2006cited by this paper
• A True Autoactivating Enzyme

  2005cited by this paper
• Mannan-binding-lectin-associated serine proteases, characteristics and disease associations

  2005cited by this paper
• The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions.

  2004cited by this paper
• Natural Substrates and Inhibitors of Mannan-Binding Lectin-Associated Serine Protease-1 and -2: A Study on Recombinant Catalytic Fragments 1

  2003cited by this paper
• Protein deamidation

  2002cited by this paper
• The biological functions of MBL-associated serine proteases (MASPs).

  2002cited by this paper
• Stoichiometry of Complexes between Mannose-binding Protein and Its Associated Serine Proteases

  2001influential reference
• Crystal structure of the catalytic domain of human complement C1s: a serine protease with a handle

  2000cited by this paper
• Distinct Pathways of Mannan-Binding Lectin (MBL)- and C1-Complex Autoactivation Revealed by Reconstitution of MBL with Recombinant MBL-Associated Serine Protease-21

  2000cited by this paper
• A second serine protease associated with mannan-binding lectin that activates complement

  1997influential reference
• Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants

  1993cited by this paper
• Activation of the classical complement pathway by mannose-binding protein in association with a novel C1s-like serine protease

  1992cited by this paper
• Binding of the pentamer/hexamer forms of mannan-binding protein to zymosan activates the proenzyme C1r2C1s2 complex, of the classical pathway of complement, without involvement of C1q.

  1990cited by this paper
• Solvent content of protein crystals.

  1968influential reference
• Disk Electrophoresis of Basic Proteins and Peptides on Polyacrylamide Gels

  1962cited by this paper

• Guianensin, a Blackfly Salivary Protein, Inhibits the Lectin Pathway of Complement

  2025cites this paper
• Detrimental interactions of hypoxia and complement MASP-1 in endothelial cells as a model for atherosclerosis-related diseases

  2024cites this paper
• Quantification of the zymogenicity and the substrate-induced activity enhancement of complement factor D

  2023cites this paper
• Directed Evolution-Driven Increase of Structural Plasticity Is a Prerequisite for Binding the Complement Lectin Pathway Blocking MASP-Inhibitor Peptides

  2022cites this paper
• Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation

  2022cites this paper
• Proprotein Convertase Is the Highest-Level Activator of the Alternative Complement Pathway in the Blood

  2021cites this paper
• Human primary endothelial label-free biochip assay reveals unpredicted functions of plasma serine proteases

  2020cites this paper
• MASP-1 Increases Endothelial Permeability

  2019cites this paper
• Cutting Edge: A New Player in the Alternative Complement Pathway, MASP-1 Is Essential for LPS-Induced, but Not for Zymosan-Induced, Alternative Pathway Activation

  2018cites this paper
• Extensive Basal Level Activation of Complement Mannose-Binding Lectin-Associated Serine Protease-3: Kinetic Modeling of Lectin Pathway Activation Provides Possible Mechanism

  2017cites this paper
• Transcriptome analysis of inflammation-related gene expression in endothelial cells activated by complement MASP-1

  2017cites this paper
• Alapvető kapcsolat a komplementrendszer lektin és alternatív útvonalai között: A humán pro-D-faktor aktiválódásának mechanizmusa

  2017cites this paper
• Complement MASP-1 enhances adhesion between endothelial cells and neutrophils by up-regulating E-selectin expression.

  2016cites this paper
• MASP-1 and MASP-2 Do Not Activate Pro–Factor D in Resting Human Blood, whereas MASP-3 Is a Potential Activator: Kinetic Analysis Involving Specific MASP-1 and MASP-2 Inhibitors

  2016cites this paper
• Serum MASP-1 in complex with MBL activates endothelial cells.

  2014cites this paper
• MASP-1 Induces a Unique Cytokine Pattern in Endothelial Cells: A Novel Link between Complement System and Neutrophil Granulocytes

  2014cites this paper
• 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*

  2013cites this paper
• The control of the complement lectin pathway activation revisited: both C1-inhibitor and antithrombin are likely physiological inhibitors, while α2-macroglobulin is not.

  2013cites this paper
• Cleavage of Kininogen and Subsequent Bradykinin Release by the Complement Component: Mannose-Binding Lectin-Associated Serine Protease (MASP)-1

  2011cites this paper
• Biological variations of MASP-3 and MAp44, two splice products of the MASP1 gene involved in regulation of the complement system.

  2010cites this paper
• Complement Protease MASP-1 Activates Human Endothelial Cells: PAR4 Activation Is a Link between Complement and Endothelial Function1

  2009cites this paper
• Reveals the Basis of Its Broad Specificity Protease : Structure of Its Catalytic Region MASP-1 , a Promiscuous Complement

  2009influential citation
• Function a Link between Complement and Endothelial IsHuman Endothelial Cells : PAR 4 Activation Complement Protease MASP-1 Activates Závodszky and Péter

  2009cites this paper
• Early complement proteases: C1r, C1s and MASPs. A structural insight into activation and functions.

  2009cites this paper
• MASP-1, a Promiscuous Complement Protease: Structure of Its Catalytic Region Reveals the Basis of Its Broad Specificity1

  2009influential citation
• C1, MBL-MASPs and C1-inhibitor: novel approaches for targeting complement-mediated inflammation.

  2008cites this paper
• Forschung mit Photonen

  2006cites this paper