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ProteomicsRepurposing E3 ubiquitin ligases as cell surface protein degraders using Proteolysis Targeting Antibodies
The majority of current therapeutics targeting plasma membrane receptors function by antagonizing ligand binding or enzymatic activities. Typical mammalian proteins, however, consist of multiple domains executing discrete but coordinated activities, and saturating inhibition of one functional domain...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2022-05-25 | MSV000089542 | MassIVE
ProteomicsStructure-guided development of chemically tailored peptide binders of RNF43/ZNRF3 to enable versatile design of membrane protein-targeting PROTACs
Targeted membrane protein degradation using cell surface E3 ligases RNF43/ZNRF3 via proteolysis targeting chimeras (PROTACs) represents an effective strategy for treating membrane drug targets that cannot be fully inhibited using traditional inhibitors. Several ingenious chimeras have been developed...
ORGANISM(S): Homo Sapiens 
2025-03-04 | PXD061425 |
TranscriptomicsBuffering and proteolysis are induced upon segmental haploidy in Drosophila melanogaster.
Aneuploidy, i.e., variation in the number of individual chromosomes (chromosomal aneuploidy) or chromosome segment (segmental aneuploidy) is associated with developmental abnormalities and reduced fitness in all species examined, is the leading cause of miscarriages and mental retardations and a hal...
ORGANISM(S): Drosophila melanogaster 
2012-04-04 | E-GEOD-34400 | biostudies-arrayexpress
GenomicsRepurposing E3 ubiquitin ligases as cell surface protein degraders using Proteolysis Targeting Antibodies
Repurposing E3 ubiquitin ligases as cell surface protein degraders using Proteolysis Targeting Antibodies
PRJNA859706 | ENA
ProteomicsIdentification of the effect of a CRISPR interference knockdown of Borrelia burgdorferi strain B31 BB0838, a outer membrane lipoprotein flippase candidate, on surface lipoprotein secretion using Multidimensional Protein Identification Technology.
To identify the effect of a CRISPR interference knockdown of Borrelia burgdorferi strain B31 BB0838, a outer membrane lipoprotein flippase candidate, on surface lipoprotein secretion using Multidimensional Protein Identification Technology.
ORGANISM(S): Borrelia Burgdorferi B31 (ncbitaxon:224326) 
2022-07-27 | MSV000089990 | MassIVE
ProteomicsAn affinity switch controls hierarchical Type III protein targeting and secretion
Surface proteolysis of EPEC IMVs, before and after urea treatment
ORGANISM(S): Escherichia coli 
2017-11-03 | PXD007087 | Pride
Imvs T3ss Epec Surface proteolysis 
ProteomicsComprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome
Localization of lipoproteins endogenously expressed under standard culture conditions was determined using multidimensional protein identification technology (MudPIT) mass spectrometry. B. burgdorferi B31A3 intact spirochetes were subjected to surface proteolysis with proteinase K.
ORGANISM(S): Borrelia Burgdorferi B31 (ncbitaxon:224326) 
2016-12-21 | MSV000080434 | MassIVE
ProteomicsExoproteome and surfaceome of toxigenic Corynebacterium diphtheriae 1737 and their response to iron-restriction and growth on human hemoglobin
Diphtheria is a severe upper respiratory disease that can cause fatal infections. It is known to produce diphtheria toxin and a range of other virulence factors, particularly when it encounters low levels of iron at sites of infection. Genomic sequencing of the NCTC13129 reference strain and its rel...
ORGANISM(S): Corynebacterium diphtheriae NCTC 13129 Bacteria 
2025-05-06 | PXD051674 | Pride
Proteomics Cell surface Diphtheria Label-free quantification Exoproteome Differential expression Corynebacterium diphtheriae Cell envelope Surface proteome Proteomic profiling Virulence factors 
TranscriptomicsRepurposing E3 ubiquitin ligases as cell surface protein degraders using Proteolysis Targeting Antibodies
The majority of current therapeutics targeting plasma membrane receptors function by antagonizing ligand binding or enzymatic activities. Typical mammalian proteins, however, consist of multiple domains executing discrete but coordinated activities, and saturating inhibition of one functional domain...
ORGANISM(S): Mus musculus 
2022-07-21 | GSE208372 | GEO
ProteomicsGlobal identification of biofilm-specific proteolysis in Candida albicans
The global extracellular protease substrate specificity of C. albicans under biofilm and planktonic (suspension) conditions was determined with a synthetic library of 14-mer peptide substrates using an approach termed Multiplex Substrate Profiling by Mass Spectrometry (MSP-MS). Shotgun proteomics an...
ORGANISM(S): Candida Albicans (ncbitaxon:5476) 
2016-03-09 | MSV000079564 | MassIVE
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