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Identification of the Multiple Roles of Enolase as Plasminogen Receptor and Adhesin in Mycoplasma hyopneumoniae

https://doi.org/10.2139/ssrn.4180334
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inferredcites →https://doi.org/10.1007/s12033-020-00291-7openalex-extracted
Dramatic Changes in Oligomerization Property Caused by Single Residue Deletion in Staphylococcus aureus Enolase
inferredcites →https://doi.org/10.1016/j.bbagen.2016.08.018openalex-extracted
Enolase of Mycobacterium tuberculosis is a surface exposed plasminogen binding protein
inferredcites →https://doi.org/10.1016/j.micpath.2019.103651openalex-extracted
Cloning and identification of Bartonella α-enolase as a plasminogen-binding protein
inferredcites →https://doi.org/10.1016/j.tim.2004.12.003openalex-extracted
Bacterial metastasis: the host plasminogen system in bacterial invasion
inferredcites →https://doi.org/10.1016/j.vetmic.2011.10.010openalex-extracted
The surface-localised α-enolase of Mycoplasma suis is an adhesion protein
inferredcites →https://doi.org/10.1021/pr400903sopenalex-extracted
P159 fromMycoplasma hyopneumoniaeBinds Porcine Cilia and Heparin and Is Cleaved in a Manner Akin to Ectodomain Shedding
inferredcites →https://doi.org/10.1039/c7mb00252aopenalex-extracted
Insights into the Giardia intestinalis enolase and human plasminogen interaction
inferredcites →https://doi.org/10.1042/bsr20180705openalex-extracted
Plasminogen-binding proteins as an evasion mechanism of the host’s innate immunity in infectious diseases
inferredcites →https://doi.org/10.1098/rsob.140175openalex-extracted
MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae
inferredcites →https://doi.org/10.1099/mic.0.061184-0openalex-extracted
Characterization of pyruvate dehydrogenase subunit B and enolase as plasminogen-binding proteins in Mycoplasma pneumoniae
inferredcites →https://doi.org/10.1111/j.1365-2141.2005.05444.xopenalex-extracted
Molecular mechanisms of fibrinolysis
inferredcites →https://doi.org/10.1111/j.1365-2958.2010.07345.xopenalex-extracted
Repeat regions R1 and R2 in the P97 paralogue Mhp271 of Mycoplasma hyopneumoniae bind heparin, fibronectin and porcine cilia
inferredcites →https://doi.org/10.1111/j.1462-5822.2011.01702.xopenalex-extracted
Mhp182 (P102) binds fibronectin and contributes to the recruitment of plasmin(ogen) to the Mycoplasma hyopneumoniae cell surface
inferredcites →https://doi.org/10.1111/jth.12064openalex-extracted
Plasminogen receptors and their role in the pathogenesis of inflammatory, autoimmune and malignant disease
inferredcites →https://doi.org/10.1111/jth.12939openalex-extracted
Pathogen activators of plasminogen
inferredcites →https://doi.org/10.1128/iai.72.1.94-105.2004openalex-extracted
Role of the C-Terminal Lysine Residues of Streptococcal Surface Enolase in Glu- and Lys-Plasminogen-Binding Activities of Group A Streptococci
inferredcites →https://doi.org/10.1128/iai.73.11.7784-7787.2005openalex-extracted
In Vivo Expression Analysis of the P97 and P102 Paralog Families of Mycoplasma hyopneumoniae
inferredcites →https://doi.org/10.1152/physrev.00030.2002openalex-extracted
Interaction of Mycoplasmas With Host Cells
inferredcites →https://doi.org/10.1159/000094058openalex-extracted
Mycoplasmas: A Distinct Cytoskeleton for Wall-Less Bacteria
inferredcites →https://doi.org/10.1186/s13567-020-00807-8openalex-extracted
Coinfections and their molecular consequences in the porcine respiratory tract
inferredcites →https://doi.org/10.1186/s13567-022-01041-0openalex-extracted
A multifunctional enolase mediates cytoadhesion and interaction with host plasminogen and fibronectin in Mycoplasma hyorhinis
inferredcites →https://doi.org/10.1371/journal.pone.0206338openalex-extracted
The influence of truncating the carboxy-terminal amino acid residues of streptococcal enolase on its ability to interact with canine plasminogen
inferredcites →https://doi.org/10.1590/s0074-02762011000900011openalex-extracted
Surface-expressed enolases of Plasmodium and other pathogens
inferredcites →https://doi.org/10.3109/1040841x.2015.1080214openalex-extracted
Bacterial pathogens activate plasminogen to breach tissue barriers and escape from innate immunity
inferredcites →https://doi.org/10.3389/fcimb.2013.00085openalex-extracted
Interaction of streptococcal plasminogen binding proteins with the host fibrinolytic system
inferredcites →https://doi.org/10.3389/fcimb.2018.00054openalex-extracted
Extracellular Actin Is a Receptor for Mycoplasma hyopneumoniae
inferredcites →https://doi.org/10.3389/fcimb.2019.00209openalex-extracted
Featured Species-Specific Loops Are Found in the Crystal Structure of Mhp Eno, a Cell Surface Adhesin From Mycoplasma hyopneumoniae
inferredcites →https://doi.org/10.3389/fmicb.2018.00974openalex-extracted
Elongation Factor Thermo Unstable (EF-Tu) Moonlights as an Adhesin on the Surface of Mycoplasma hyopneumoniae by Binding to Fibronectin
inferredcites →https://doi.org/10.3389/fmolb.2021.811106openalex-extracted
Evidence for the Rapid and Divergent Evolution of Mycoplasmas: Structural and Phylogenetic Analysis of Enolases
inferredcites →https://doi.org/10.3892/etm.2015.2399openalex-extracted
Comparison between the clot-protecting activity of a mutant plasminogen activator inhibitor-1 with a very long half-life and 6-aminocaproic acid
inferredcites →https://doi.org/10.5582/bst.2017.01195openalex-extracted
Expression, purification, and biological characterization of Anaplasma phagocytophilum enolase
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