Massively parallel enzyme kinetics reveals the substrate recognition landscape of the metalloprotease ADAMTS13

No abstract is available for this paper.

• Publication year

  2015

• Venue

  Proceedings of the National Academy of Sciences of the United States of America

• Publication date

  2015-07-13

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1073/pnas.1511328112PMID 26170332PMCID PMC4522773
• 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.

• THROMBOSIS AND HEMOSTASIS The role of the ADAMTS 13 cysteine-rich domain in VWF binding and proteolysis

  2015cited by this paper
• The role of the ADAMTS13 cysteine-rich domain in VWF binding and proteolysis.

  2015cited by this paper
• Probing ADAMTS13 Substrate Specificity using Phage Display

  2015cited by this paper
• Basis for substrate recognition and distinction by matrix metalloproteinases

  2014cited by this paper
• The UCSC Genome Browser database: 2015 update

  2014cited by this paper
• Discrepancies between ADAMTS13 activity assays in patients with thrombotic microangiopathies

  2013cited by this paper
• Assessment of computational methods for predicting the effects of missense mutations in human cancers

  2013cited by this paper
• von Willebrand Factor: Form for Function

  2013cited by this paper
• Mechanisms by which von Willebrand Disease Mutations Destabilize the A2 Domain*

  2013cited by this paper
• Deep sequencing of phage display libraries to support antibody discovery.

  2013cited by this paper
• PhIP-Seq characterization of autoantibodies from patients with multiple sclerosis, type 1 diabetes and rheumatoid arthritis.

  2013cited by this paper
• Epistasis as the primary factor in molecular evolution

  2012cited by this paper
• BayesHammer: Bayesian clustering for error correction in single-cell sequencing

  2012cited by this paper
• Phage display screening without repetitious selection rounds.

  2012cited by this paper
• Identification of epitopes on ADAMTS13 recognized by a panel of monoclonal antibodies with functional or non-functional effects on catalytic activity.

  2012cited by this paper
• The Extended Cleavage Specificity of Human Thrombin

  2012cited by this paper
• The expanding scope of DNA sequencing

  2012cited by this paper
• Estimating the Rate of Irreversibility in Protein Evolution

  2012cited by this paper
• Autoantigen discovery with a synthetic human peptidome

  2011cited by this paper
• Mechanism of von Willebrand factor scissile bond cleavage by a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13 (ADAMTS13)

  2011cited by this paper
• Enrich: software for analysis of protein function by enrichment and depletion of variants

  2011cited by this paper
• Unraveling the scissile bond: how ADAMTS13 recognizes and cleaves von Willebrand factor.

  2011cited by this paper
• Emerging principles in protease-based drug discovery

  2010cited by this paper
• High Resolution Mapping of Protein Sequence–Function Relationships

  2010cited by this paper
• ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids

  2010cited by this paper
• Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Willebrand factor

  2009cited by this paper
• Mechanoenzymatic Cleavage of the Ultralarge Vascular Protein von Willebrand Factor

  2009cited by this paper
• HD1, a thrombin- and prothrombin-binding DNA aptamer, inhibits thrombin generation by attenuating prothrombin activation and thrombin feedback reactions

  2009cited by this paper
• Crystal structures of the noncatalytic domains of ADAMTS13 reveal multiple discontinuous exosites for von Willebrand factor

  2009cited by this paper
• Mechanoenzymatic Cleavage of the Ultralarge Vascular Protein von Willebrand Factor

  2009cited by this paper
• High throughput substrate phage display for protease profiling.

  2009cited by this paper
• Extensive contacts between ADAMTS13 exosites and von Willebrand factor domain A2 contribute to substrate specificity.

  2008cited by this paper
• Identification of an ADAMTS-4 Cleavage Motif Using Phage Display Leads to the Development of Fluorogenic Peptide Substrates and Reveals Matrilin-3 as a Novel Substrate*

  2007cited by this paper
• ADAMTS13 Substrate Recognition of von Willebrand Factor A2 Domain*

  2006cited by this paper
• Exosite interactions contribute to tension-induced cleavage of von Willebrand factor by the antithrombotic ADAMTS13 metalloprotease

  2006cited by this paper
• Functional evolution of ADAMTS genes: Evidence from analyses of phylogeny and gene organization

  2005cited by this paper
• The spacer domain of ADAMTS13 contains a major binding site for antibodies in patients with thrombotic thrombocytopenic purpura

  2005cited by this paper
• Increased susceptibility of von Willebrand factor to proteolysis by ADAMTS13: should the multimer profile be normal or type 2A?

  2004cited by this paper
• ConSeq: the identification of functionally and structurally important residues in protein sequences

  2004cited by this paper
• VWF73, a region from D1596 to R1668 of von Willebrand factor, provides a minimal substrate for ADAMTS-13.

  2004cited by this paper
• A Unique Substrate Binding Mode Discriminates Membrane Type-1 Matrix Metalloproteinase from Other Matrix Metalloproteinases*

  2002cited by this paper
• Peptide Substrate Specificities and Protein Cleavage Sites of Human Endometase/Matrilysin-2/Matrix Metalloproteinase-26*

  2002cited by this paper
• Dobzhansky–Muller incompatibilities in protein evolution

  2002cited by this paper
• A Unique Substrate Recognition Profile for Matrix Metalloproteinase-2*

  2002cited by this paper
• Determination of protease cleavage site motifs using mixture-based oriented peptide libraries

  2001cited by this paper
• An Extensive Interaction Interface between Thrombin and Factor V Is Required for Factor V Activation*

  2001cited by this paper
• Mutations in a member of the ADAMTS gene family cause thrombotic thrombocytopenic purpura

  2001cited by this paper
• Structure of von Willebrand Factor-cleaving Protease (ADAMTS13), a Metalloprotease Involved in Thrombotic Thrombocytopenic Purpura*

  2001cited by this paper
• Partial purification and characterization of a protease from human plasma cleaving von Willebrand factor to fragments produced by in vivo proteolysis.

  1996cited by this paper
• Antibody-selectable filamentous fd phage vectors: affinity purification of target genes.

  1988cited by this paper
• On the size of the active site in proteases. I. Papain.

  1967cited by this paper
• Bmc Evolutionary Biology the Evolution of the Vertebrate Metzincins; Insights from Ciona Intestinalis and Danio Rerio

  year unknowncited by this paper

• Development of a protease-resistant ADAMTS13 to improve stability against proteolytic degradation

  2025cites this paper
• Thermodynamics and selection of the plasminogen activator inhibitor-1 latency transition

  2025cites this paper
• Measuring kcat/KM values for over 200,000 enzymatic substrates with mRNA display

  2025cites this paper
• Venous Thromboembolic Disease Genetics: From variants to function.

  2024cites this paper
• Interpretable neural architecture search and transfer learning for understanding CRISPR/Cas9 off-target enzymatic reactions

  2023cites this paper
• Metalloprotease domain latency protects ADAMTS13 against broad- spectrum inhibitors of metalloproteases while maintaining activity towards VWF.

  2023cites this paper
• Interpretable neural architecture search and transfer learning for understanding CRISPR–Cas9 off-target enzymatic reactions

  2023cites this paper
• Interpretable neural architecture search and transfer learning for understanding sequence dependent enzymatic reactions

  2023cites this paper
• Mechanisms of ADAMTS13 regulation

  2022cites this paper
• Deep mutational scanning and massively parallel kinetics of plasminogen activator inhibitor-1 functional stability

  2022cites this paper
• Molecular interplay of ADAMTS13-MDTCS and von willebrand Factor-A2: deepened insights from extensive atomistic simulations

  2022cites this paper
• Deep mutational scanning and massively parallel kinetics of plasminogen activator inhibitor-1 functional stability to probe its latency transition

  2022cites this paper
• Deep mutational scanning and massively parallel kinetics of plasminogen activator-1 functional stability

  2022cites this paper
• Phage Display Broadly Identifies Inhibitor-reactive Regions in von Willebrand Factor

  2021cites this paper
• Mechanobiology of shear-induced platelet aggregation leading to occlusive arterial thrombosis: A multiscale in silico analysis.

  2021cites this paper
• Deep mutational scanning of the plasminogen activator inhibitor-1 functional landscape

  2021cites this paper
• Functional Characterization of Fibrinolysis-Modulating Proteins Using High Throughput Phage Display

  2020cites this paper
• Expanding the Chemical Diversity of Genetically Encoded Libraries.

  2020cites this paper
• Quantitative profiling of protease specificity

  2020cites this paper
• Exploring the Post-Translational Enzymology of PaaA by mRNA Display.

  2020cites this paper
• ADAMTS proteases in cardiovascular physiology and disease

  2020cites this paper
• Phylogenetic and functional analysis of ADAMTS13 identifies highly conserved domains essential for allosteric regulation.

  2019cites this paper
• Crystal structure and substrate-induced activation of ADAMTS13

  2019cites this paper
• MaveDB: an open-source platform to distribute and interpret data from multiplexed assays of variant effect

  2019cites this paper
• High throughput protease profiling comprehensively defines active site specificity for thrombin and ADAMTS13

  2018cites this paper
• Computational insight into the broad substrate specificity of enzymes that process nucleic acids

  2018cites this paper
• Mapping the Substrate Recognition Landscapes of Metalloproteases Using Comprehensive Mutagenesis.

  2017cites this paper
• ADAMTS‐13 and von Willebrand factor: a dynamic duo

  2017cites this paper
• Evaluating the Substrate Selectivity of Alkyladenine DNA Glycosylase: The Synergistic Interplay of Active Site Flexibility and Water Reorganization.

  2016cites this paper
• Family-Specific Variants and the Limits of Human Genetics.

  2016cites this paper
• Conformational quiescence of ADAMTS‐13 prevents proteolytic promiscuity

  2016cites this paper