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UnknownA human monoclonal antibody bivalently binding two different epitopes in streptococcal M protein mediates immune function.
Not available
S-EPMC9906385 | biostudies-literature
UnknownGreedy de novo motif discovery to construct motif repositories for bacterial proteomes.
Not available
S-EPMC6471678 | biostudies-literature
UnknownStreptococcus pyogenes Forms Serotype- and Local Environment-Dependent Interspecies Protein Complexes.
Not available
S-EPMC8547449 | biostudies-literature
UnknownStructural determination of Streptococcus pyogenes M1 protein interactions with human immunoglobulin G using integrative structural biology.
Not available
S-EPMC7817036 | biostudies-literature
UnknownThe hinge-engineered IgG1-IgG3 hybrid subclass IgGh47 potently enhances Fc-mediated function of anti-streptococcal and SARS-CoV-2 antibodies.
Not available
S-EPMC11055898 | biostudies-literature
UnknownImplementation of cloud computing in the German healthcare system.
Not available
S-EPMC10787755 | biostudies-literature
UnknownMultienzyme deep learning models improve peptide de novo sequencing by mass spectrometry proteomics.
Not available
S-EPMC9891523 | biostudies-literature
ProteomicsMultienzyme deep learning models improve peptide de novo sequencing by mass spectrometry proteomics
Generating and analyzing overlapping peptides through multienzymatic digestion is an efficient procedure for de novo protein using from bottom-up mass spectrometry (MS). Despite improved instrumentation and software, de novo MS data analysis remains challenging. In recent years, deep learning models...
ORGANISM(S): Homo sapiens (Human) 
2023-01-16 | PXD037803 | Pride
Monoclonal antibody Mass spectrometry De novo sequencing Deepnovo 
UnknownA quantitative Streptococcus pyogenes-human protein-protein interaction map reveals localization of opsonizing antibodies.
Not available
S-EPMC6588558 | biostudies-literature
ProteomicsAffinity-purification mass spectrometry on i) streptolysin O or C5a peptidase with human plasma or saliva; ii) human plasminogen with streptococcal proteins
In this project, we tried to use affinity-purification mass spectrometry (AP-MS) to study host-pathogen protein interaction, focusing initially on two major virulence factors of group A streptococcus (GAS), streptolysin O (SLO) and C5a peptidase (C5AP) with the immediate host microenvironment (human...
ORGANISM(S): Streptococcus pyogenes M1 GAS Homo sapiens (Human) Streptococcus pyogenes MGAS315 
2026-03-16 | PXD069402 | Pride
Group a streptococcus Protein-protein interaction Host-pathogen interaction Ap-ms 
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