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Pathogen activators of plasminogen

https://doi.org/10.1111/jth.12939
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1006/jmbi.2001.4646openalex-snapshot
Structure and binding determinants of the recombinant kringle-2 domain of human plasminogen to an internal peptide from a group A Streptococcal surface protein 1 1Edited by R. Huber
inferredcites →https://doi.org/10.1007/82_2012_280openalex-snapshot
Group A Streptococcal Diseases and Their Global Burden
inferredcites →https://doi.org/10.1007/s00018-004-4285-7openalex-snapshot
The staphylocoagulase family of zymogen activator and adhesion proteins
inferredcites →https://doi.org/10.1007/s00253-013-5200-7openalex-snapshot
Toxin–antitoxin-stabilized reporter plasmids for biophotonic imaging of Group A streptococcus
inferredcites →https://doi.org/10.1016/0014-5793(76)80443-7openalex-snapshot
Induction of the bovine trypsinogen—trypsin transition by peptides sequentially similar to the N‐terminus of trypsin
inferredcites →https://doi.org/10.1016/0049-3848(95)00131-aopenalex-snapshot
Activating effect of the plasminogen activators on plasminogens of different mammalia species
inferredcites →https://doi.org/10.1016/0305-0491(83)90345-0openalex-snapshot
Species specificity of streptokinase
inferredcites →https://doi.org/10.1016/0888-7543(90)90225-jopenalex-snapshot
Characterization of the cDNA coding for mouse plasminogen and localization of the gene to mouse chromosome 17
inferredcites →https://doi.org/10.1016/j.celrep.2012.02.012openalex-snapshot
The X-ray Crystal Structure of Full-Length Human Plasminogen
inferredcites →https://doi.org/10.1016/j.tim.2005.05.006openalex-snapshot
Is plasminogen deployed as a Streptococcus pyogenes virulence factor?
inferredcites →https://doi.org/10.1016/s0014-5793(99)01214-4openalex-snapshot
Crystal structure of streptokinase β‐domain
inferredcites →https://doi.org/10.1016/s0021-9258(19)74408-1openalex-snapshot
PAM, a novel plasminogen-binding protein from Streptococcus pyogenes.
inferredcites →https://doi.org/10.1016/s0968-0004(99)01521-2openalex-snapshot
Molecular mechanisms of plasminogen activation: bacterial cofactors provide clues
inferredcites →https://doi.org/10.1016/s1473-3099(03)00576-0openalex-snapshot
Molecular basis of group A streptococcal virulence
inferredcites →https://doi.org/10.1021/ar50123a006openalex-snapshot
Structural basis of the activation and action of trypsin
inferredcites →https://doi.org/10.1021/bi000594iopenalex-snapshot
Streptokinase Binds Preferentially to the Extended Conformation of Plasminogen through Lysine Binding Site and Catalytic Domain Interactions
inferredcites →https://doi.org/10.1021/bi00691a018openalex-snapshot
Kinetic mechanism of the activation of human plasminogen by streptokinase
inferredcites →https://doi.org/10.1021/bi011309dopenalex-snapshot
Domain Interactions between Streptokinase and Human Plasminogen
inferredcites →https://doi.org/10.1021/bi060914jopenalex-snapshot
X-ray Crystallographic Structure of the Angiogenesis Inhibitor, Angiostatin, Bound to a Peptide from the Group A Streptococcal Surface Protein PAM,
inferredcites →https://doi.org/10.1021/bi981915hopenalex-snapshot
Deletion of Ile1 Changes the Mechanism of Streptokinase: Evidence for the Molecular Sexuality Hypothesis
inferredcites →https://doi.org/10.1021/bi992028xopenalex-snapshot
Epsilon Amino Caproic Acid Inhibits Streptokinase−Plasminogen Activator Complex Formation and Substrate Binding through Kringle-Dependent Mechanisms
inferredcites →https://doi.org/10.1038/nature01962openalex-snapshot
Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation
inferredcites →https://doi.org/10.1038/nature09967openalex-snapshot
Streptococcal M1 protein constructs a pathological host fibrinogen network
inferredcites →https://doi.org/10.1042/bj20131305openalex-snapshot
Site-restricted plasminogen activation mediated by group A streptococcal streptokinase variants
inferredcites →https://doi.org/10.1046/j.1365-2958.2003.03557.xopenalex-snapshot
Identification of a novel plasmin(ogen)‐binding motif in surface displayed α‐enolase of Streptococcus pneumoniae
inferredcites →https://doi.org/10.1073/pnas.1201031109openalex-snapshot
Inhibitor of streptokinase gene expression improves survival after group A streptococcus infection in mice
inferredcites →https://doi.org/10.1074/jbc.273.11.6424openalex-snapshot
Molecular Co-operation between Protein PAM and Streptokinase for Plasmin Acquisition by Streptococcus pyogenes
inferredcites →https://doi.org/10.1074/jbc.275.19.14579openalex-snapshot
Streptokinase Binds to Human Plasmin with High Affinity, Perturbs the Plasmin Active Site, and Induces Expression of a Substrate Recognition Exosite for Plasminogen
inferredcites →https://doi.org/10.1074/jbc.c600171200openalex-snapshot
Binding of the COOH-terminal Lysine Residue of Streptokinase to Plasmin(ogen) Kringles Enhances Formation of the Streptokinase·Plasmin(ogen) Catalytic Complexes
inferredcites →https://doi.org/10.1074/jbc.m003963200openalex-snapshot
Leucine 42 in the Fibronectin Motif of Streptokinase Plays a Critical Role in Fibrin-independent Plasminogen Activation
inferredcites →https://doi.org/10.1074/jbc.m101966200openalex-snapshot
Streptokinase Triggers Conformational Activation of Plasminogen through Specific Interactions of the Amino-terminal Sequence and Stabilizes the Active Zymogen Conformation
inferredcites →https://doi.org/10.1074/jbc.m108422200openalex-snapshot
Involvement of a Nine-residue Loop of Streptokinase in the Generation of Macromolecular Substrate Specificity by the Activator Complex through Interaction with Substrate Kringle Domains
inferredcites →https://doi.org/10.1074/jbc.m109.005512openalex-snapshot
Plasminogen Substrate Recognition by the Streptokinase-Plasminogen Catalytic Complex Is Facilitated by Arg253, Lys256, and Lys257 in the Streptokinase β-Domain and Kringle 5 of the Substrate
inferredcites →https://doi.org/10.1074/jbc.m110.107730openalex-snapshot
Skizzle Is a Novel Plasminogen- and Plasmin-binding Protein from Streptococcus agalactiae That Targets Proteins of Human Fibrinolysis to Promote Plasmin Generation
inferredcites →https://doi.org/10.1074/jbc.m112.417808openalex-snapshot
Characterization of Streptokinases from Group A Streptococci Reveals a Strong Functional Relationship That Supports the Coinheritance of Plasminogen-binding M Protein and Cluster 2b Streptokinase
inferredcites →https://doi.org/10.1074/jbc.m113.477935openalex-snapshot
Full Time Course Kinetics of the Streptokinase-Plasminogen Activation Pathway
inferredcites →https://doi.org/10.1074/jbc.m114.589077openalex-snapshot
Rapid Binding of Plasminogen to Streptokinase in a Catalytic Complex Reveals a Three-step Mechanism
inferredcites →https://doi.org/10.1074/jbc.m405264200openalex-snapshot
Resolution of Conformational Activation in the Kinetic Mechanism of Plasminogen Activation by Streptokinase
inferredcites →https://doi.org/10.1074/jbc.m405265200openalex-snapshot
Coupling of Conformational and Proteolytic Activation in the Kinetic Mechanism of Plasminogen Activation by Streptokinase
inferredcites →https://doi.org/10.1074/jbc.m411637200openalex-snapshot
Role of the Streptokinase α-Domain in the Interactions of Streptokinase with Plasminogen and Plasmin
inferredcites →https://doi.org/10.1074/jbc.m705063200openalex-snapshot
The Lack of Binding of VEK-30, an Internal Peptide from the Group A Streptococcal M-like Protein, PAM, to Murine Plasminogen Is due to Two Amino Acid Replacements in the Plasminogen Kringle-2 Domain
inferredcites →https://doi.org/10.1074/jbc.m804038200openalex-snapshot
Rapid-reaction Kinetic Characterization of the Pathway of Streptokinase-Plasmin Catalytic Complex Formation
inferredcites →https://doi.org/10.1086/314654openalex-snapshot
Interaction between Group A Streptococci and the Plasmin(ogen) System Promotes Virulence in a Mouse Skin Infection Model
inferredcites →https://doi.org/10.1086/377100openalex-snapshot
Plasminogen Enhances Virulence of Group A Streptococci by Streptokinase‐Dependent and Streptokinase‐Independent Mechanisms
inferredcites →https://doi.org/10.1093/emboj/16.16.4797openalex-snapshot
Lysine 156 promotes the anomalous proenzyme activity of tPA: X‐ray crystal structure of single‐chain human tPA
inferredcites →https://doi.org/10.1096/fj.06-5804fjeopenalex-snapshot
Trigger for group A streptococcal M1T1 invasive disease
inferredcites →https://doi.org/10.1096/fj.08-109348openalex-snapshot
Allelic variants of streptokinase from Streptococcus pyogenes display functional differences in plasminogen activation
inferredcites →https://doi.org/10.1110/ps.8.12.2791openalex-snapshot
Function of the central domain of streptokinase in substrate plasminogen docking and processing revealed by site‐directed mutagenesis
inferredcites →https://doi.org/10.1111/j.1432-1033.1979.tb02040.xopenalex-snapshot
Kinetics of the Reactions between Streptokinase, Plasmin and alpha2-Antiplasmin
inferredcites →https://doi.org/10.1111/j.1538-7836.2011.04316.xopenalex-snapshot
Exploration of the host haemostatic system by group A streptococcus: implications in searching for novel antimicrobial therapies
inferredcites →https://doi.org/10.1111/j.1538-7836.2012.04765.xopenalex-snapshot
Crystal structure of the native plasminogen reveals an activation‐resistant compact conformation
inferredcites →https://doi.org/10.1111/mmi.12037openalex-snapshot
Streptokinase variants from S treptococcus pyogenes isolates display altered plasminogen activation characteristics – implications for pathogenesis
inferredcites →https://doi.org/10.1126/science.1101245openalex-snapshot
Plasminogen Is a Critical Host Pathogenicity Factor for Group A Streptococcal Infection
inferredcites →https://doi.org/10.1126/science.281.5383.1662openalex-snapshot
Crystal Structure of the Catalytic Domain of Human Plasmin Complexed with Streptokinase
inferredcites →https://doi.org/10.1128/iai.69.5.3350-3358.2001openalex-snapshot
Visualizing Pneumococcal Infections in the Lungs of Live Mice Using Bioluminescent Streptococcus pneumoniae Transformed with a Novel Gram-Positive lux Transposon
inferredcites →https://doi.org/10.1128/jb.186.1.110-121.2004openalex-snapshot
Natural Selection and Evolution of Streptococcal Virulence Genes Involved in Tissue-Specific Adaptations
inferredcites →https://doi.org/10.1172/jci110631openalex-snapshot
Catabolic Pathways for Streptokinase, Plasmin, and Streptokinase Activator Complex in Mice
inferredcites →https://doi.org/10.1186/bcr1647openalex-snapshot
Plasminogen binding and activation at the breast cancer cell surface: the integral role of urokinase activity
inferredcites →https://doi.org/10.2174/138945012799424589openalex-snapshot
The Role of Streptokinase as a Virulence Determinant of Streptococcus pyogenes – Potential for Therapeutic Targeting

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4180334openalex-extracted
Identification of the Multiple Roles of Enolase as Plasminogen Receptor and Adhesin in Mycoplasma hyopneumoniae
inferred← citeshttps://doi.org/10.1007/978-1-4939-8814-3_20openalex-snapshot
Proteases: Pivot Points in Functional Proteomics
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N-glycoprotein macroheterogeneity: biological implications and proteomic characterization
inferred← citeshttps://doi.org/10.1016/j.actatropica.2018.02.020openalex-snapshot
Identification and characterization of Taenia solium enolase as a plasminogen-binding protein
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Unraveling Spiroplasma eriocheiris: Morphological motility, virulence mechanisms, and host defense strategies in crustacean pathogenesis
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Interactions of surface-displayed glycolytic enzymes of Mycoplasma pneumoniae with components of the human extracellular matrix
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Pathogenic conversion of coagulase-negative staphylococci
inferred← citeshttps://doi.org/10.1016/j.micpath.2022.105934openalex-snapshot
Identification of the multiple roles of enolase as an plasminogen receptor and adhesin in Mycoplasma hyopneumoniae
inferred← citeshttps://doi.org/10.1016/j.vetmic.2024.110297openalex-snapshot
Dihydrolipoamide acetyltransferase is a key factor mediating adhesion and invasion of host cells by Mycoplasma synoviae
inferred← citeshttps://doi.org/10.1093/femsre/fuae019openalex-snapshot
Mechanisms of host adaptation by bacterial pathogens
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Single-chain factor XII: a new form of activated factor XII
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Tranexamic acid and inflammation in trauma
inferred← citeshttps://doi.org/10.1126/sciadv.abe3362openalex-snapshot
The fibrinolytic system enables the onset of Plasmodium infection in the mosquito vector and the mammalian host
inferred← citeshttps://doi.org/10.1128/9781683670131.ch15openalex-snapshot
Genetics and Pathogenicity Factors of Group C and G Streptococci
inferred← citeshttps://doi.org/10.1128/microbiolspec.gpp3-0002-2017openalex-snapshot
Genetics and Pathogenicity Factors of Group C and G Streptococci
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Immunohaemostasis: a new view on haemostasis during sepsis
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The Fibrinolytic System in the Interstitial Space
inferred← citeshttps://doi.org/10.3389/fcimb.2021.679792openalex-snapshot
Lysine Residues in the MK-Rich Region Are Not Required for Binding of the PbsP Protein From Group B Streptococci to Plasminogen
inferred← citeshttps://doi.org/10.3389/fimmu.2019.01852openalex-snapshot
Spiroplasma eriocheiris Invasion Into Macrobrachium rosenbergii Hemocytes Is Mediated by Pathogen Enolase and Host Lipopolysaccharide and β-1, 3-Glucan Binding Protein
inferred← citeshttps://doi.org/10.3389/fmicb.2020.02054openalex-snapshot
The Multivalent Role of Fibronectin-Binding Proteins A and B (FnBPA and FnBPB) of Staphylococcus aureus in Host Infections
inferred← citeshttps://doi.org/10.3389/fmicb.2023.1335658openalex-snapshot
Mycoplasma synoviae LP78 is a fibronectin/plasminogen binding protein, putative adhesion, and potential diagnostic antigen
inferred← citeshttps://doi.org/10.3390/microorganisms11020305openalex-snapshot
The Cell Wall Deacetylases Spy1094 and Spy1370 Contribute to Streptococcus pyogenes Virulence
inferred← citeshttps://doi.org/10.5772/intechopen.88182openalex-snapshot
Toward Better Understanding on How Group AStreptococcusManipulates Human Fibrinolytic System
inferred← citeshttps://doi.org/10.70675/95d49fabz6ca4z4b31z8099zc3c87d8000b4openalex-snapshot
Modulateurs synthétiques de la kallikréine 6, protéase à sérine impliquée dans les maladies neurodégénératives : identification, mécanisme d’action et validation de concept
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