Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Role of the C-terminal lysine residues of streptococcal surface enolase in Glu- and Lys-plasminogen-binding activities of group A streptococci.

Infection and immunity - 1 Jan 2004

Derbise Anne, Song Youngmia P, Parikh Sonia, Fischetti Vincent A, Pancholi Vijay

Abstract excerpt

Streptococcal surface enolase (SEN) is a major plasminogen-binding protein of group A streptococci. Our earlier biochemical studies have suggested that the region responsible for this property is likely located at the C-terminal end of the SEN molecule. In the present study, the gene encoding SEN was cloned from group A streptococci M6 isolate D471. A series of mutations in the sen gene corresponding to the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Proteins
Share to Lysine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Peptide Fragments

Share to Phosphopyruvate Hydratase

Share to Plasma

Share to Plasminogen

Share to Streptococcus pyogenes

Source

Open in PubMed Open full text

Identifiers

PMID: 14688086
DOI: 10.1128/IAI.72.1.94-105.2004
PMCID: PMC343989

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of the C-terminal lysine residues of streptococcal surface enolase in Glu- and Lys-plasminogen-binding activities of group A streptococci.PMID 14688086Read ↗

Group A Streptococcus exploits human plasminogen for bacterial translocation across epithelial barrier via tricellular tight junctionsSemantic proximity Read ↗

The nine residue plasminogen-binding motif of the pneumococcal enolase is the major cofactor of plasmin-mediated degradation of extracellular matrix, dissolution of fibrin and transmigration.Semantic proximity Read ↗

Identification of a novel plasmin(ogen)‐binding motif in surface displayed α‐enolase of Streptococcus pneumoniaeSemantic proximity Read ↗

Enolases from Gram-positive bacterial pathogens and commensal lactobacilli share functional similarity in virulence-associated traitsSemantic proximity Read ↗

Biochemical and Biophysical Analysis of the Interaction of a Recombinant form of Staphylococcus Aureus Enolase With PlasminogenSemantic proximity Read ↗

Contribution of plasminogen activation towards the pathogenic potential of oral streptococci.Semantic proximity Read ↗

Identification of a plasminogen-binding motif in PAM, a bacterial surface protein.Semantic proximity Read ↗

Staphylokinase Requires NH2-terminal Proteolysis for Plasminogen ActivationSemantic proximity Read ↗

Identification of a new exosite involved in catalytic turnover by the streptokinase-plasmin activator complex during human plasminogen activation.Semantic proximity Read ↗

Allelic variants of streptokinase from Streptococcus pyogenes display functional differences in plasminogen activation.Semantic proximity Read ↗

The Plasminogen-Binding Group A Streptococcal M Protein-Related Protein Prp Binds Plasminogen via Arginine and Histidine ResiduesSemantic proximity Read ↗

Structural correlates of a functional streptokinase antigenic epitope: serine 138 is an essential residue for antibody binding.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.