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UnknownInvestigation of the Binding Affinity of a Broad Array of l-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin.
Not available
S-EPMC6631993 | biostudies-literature
UnknownResponses of signal crayfish Pacifastacus leniusculus to single short-term pulse exposure of pesticides at environmentally relevant concentrations.
Not available
S-EPMC10119208 | biostudies-literature
UnknownSynthesis of β-d-galactopyranoside-Presenting Glycoclusters, Investigation of Their Interactions with Pseudomonas aeruginosa Lectin A (PA-IL) and Evaluation of Their Anti-Adhesion Potential.
Not available
S-EPMC6920806 | biostudies-literature
UnknownMicroscopy examination of red blood and yeast cell agglutination induced by bacterial lectins.
Not available
S-EPMC6657890 | biostudies-literature
UnknownBurkholderia cenocepacia BC2L-C is a super lectin with dual specificity and proinflammatory activity.
Not available
S-EPMC3164656 | biostudies-literature
ProteomicsLimited proteolysis of SARS-CoV-2 Spike treated at pH 2 or pH 7
SARS-CoV-2 is a respiratory virus spreading via aerosol particles. Aerosol particles can exhibit extreme environmental conditions affecting contained viruses, including acidic pH. Here, we study how harsh pH conditions, such as pH 2, can affect the structure of Spike, which is the main protein media...
ORGANISM(S): Homo sapiens (Human) Severe acute respiratory syndrome coronavirus 2 
2025-07-17 | PXD064612 | Pride
Sars-cov-2 Lc-ms Spike Acidic ph Lip 
UnknownModification of the Emergency Severity Index Improves Mortality Prediction in Older Patients.
Not available
S-EPMC6625680 | biostudies-literature
UnknownMolecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates.
Not available
S-EPMC3418301 | biostudies-literature
UnknownDictyostelium discoideum has a highly Q/N-rich proteome and shows an unusual resilience to protein aggregation.
Not available
S-EPMC4443358 | biostudies-literature
UnknownPromiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules.
Not available
S-EPMC4522596 | biostudies-literature
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