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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 
ProteomicsLeveraging immonium ions for identifying and targeting acyl-lysine modifications in proteomic datasets
Acyl modifications vary greatly in terms of elemental composition and site of protein modification. Developing methods to identify these modifications more confidently can help assess the scope of these modifications in large proteomic datasets. Herein we analyze the utility of acyl-lysine immonium ...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2020-09-09 | PXD018758 | Pride
Stepped collision energy Lysine acylation Immonium ion 3-hydroxypimelylation Lysine acetylation Bsa Lc-ms/ms 
ProteomicsThe acyl-proteome of Syntrophus aciditrophicus reveals metabolic relationship with benzoate degradation
Syntrophus aciditrophicus is a model syntrophic bacterium that degrades fatty and aromatic acids into acetate, CO2, formate and H2 that are utilized by methanogens and other hydrogen-consuming microbes. The degradation of benzoate by S. aciditrophicus proceeds by a multi-step pathway that involves m...
ORGANISM(S): Syntrophus aciditrophicus SB 
2022-03-16 | PXD025631 | Pride
Syntrophs Lysine acetylation 2d-page Lysine acylation Lc-ms/ms 
ProteomicsBlue native gel electrophoresis of Syntrophus aciditrophicus proteome
Blue native gel electrophoresis of Syntrophus aciditrophicus proteome
ORGANISM(S): Syntrophus Aciditrophicus Sb 
2019-04-29 | PXD011101 | JPOST Repository
ProteomicsAnalyze key proteins in Syntrophus aciditrophicus
Pure cultures of S. aciditrophicus grown in 250 ml of 20 mM crotonate medium in 500-ml Schott bottles were used for proteomic analysis after 2-dimensional (2-D) PAGE.
ORGANISM(S): Syntrophus Aciditrophicus Sb 
2019-04-29 | PXD011100 | JPOST Repository
TranscriptomicsZinc deficiency impacts CO2 assimilation and disrupts copper homeostasis in Chlamydomonas reinhardtii
Zinc is an essential nutrient because of its role in catalysis and in stabilizing protein structure, but excess zinc can also be deleterious. Four nutritional zinc states have been identified in the alga Chlamydomonas reinhardtii: zinc toxic, zinc replete, zinc deficient and zinc limited. Growth is ...
ORGANISM(S): Chlamydomonas reinhardtii 
2013-05-03 | E-GEOD-41096 | biostudies-arrayexpress
ProteomicsPRM and DDA Data for IR5 WIW and WIW Nanobodies
Journal Article: Structure-based design of nanobodies that inhibit seeding of Alzheimer's patient-extracted tau fibrils
ORGANISM(S): Synthetic Antibodies Nanobodies 
2023-06-16 | MSV000092197 | MassIVE
UnknownGenomic admixture analysis in European Populus spp. reveals unexpected patterns of reproductive isolation and mating.
Not available
S-EPMC2954470 | biostudies-literature
TranscriptomicsSystems analysis of Chlamydomonas Cu nutrition reveals connections between Cu and multiple O2-dependent metabolic steps
We used digital gene expression (NlaIII sequence tags) and RNA-Seq to compare the transcriptomes of Cu-replete vs. Cu–deficient Chlamydomonas wild-type cells to reveal dozens of mRNAs whose abundance is modified. Half of the corresponding genes are targets of CRR1, a master regulator of nutritional ...
ORGANISM(S): Chlamydomonas reinhardtii 
2011-10-23 | E-GEOD-25124 | biostudies-arrayexpress
ProteomicsStructural basis for L-isoaspartyl-containing protein recognition by the PCMTD1 cullin-RING E3 ubiquitin ligase
LC/MS identification of proteins co-immunoprecipitated with PCMTD1 and PCMTD1 P243 F247 stably expressed in FlpIn 293 cells.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2025-05-19 | MSV000097912 | MassIVE
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