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TranscriptomicsTranscription profiling of human intestinal cells (Caco-2) and tissues from all intestinal segments (duodenum, jejunum, ileum, colon)
Affymetrix U95Av2 expression data from human intestinal cells (Caco-2) and tissues from all intestinal segments (duodenum, jejunum, ileum, colon). Entries contain the search terms glycosylase, phosphorylase, cytochrome or nucleoside, which were relevant to our search for enzymes capable of cleaving...
ORGANISM(S): Homo sapiens 
2007-06-21 | E-GEOD-1862 | biostudies-arrayexpress
UnknownEarly amphibians evolved distinct vertebrae for habitat invasions.
Not available
S-EPMC8189462 | biostudies-literature
TranscriptomicsNext generation sequencing of Pseudomonas aruginosa PAO1 in the presence of Free Nitrous Acid stress
Purpose: Free nitrous acid (FNA) has recently been demonstrated as an antimicrobial agent to a range of microorganisms. However, its antimicrobial mechanism is largely unknown. For this study Pseudomonas aeruginosa PAO1 was selected to gain a systematic understanding of the antimicrobial mechanism o...
ORGANISM(S): Pseudomonas aeruginosa 
2016-04-06 | E-GEOD-73323 | biostudies-arrayexpress
UnknownValidation of 'lock-and-key' mechanism of a metal-organic framework in selective sensing of triethylamine.
Not available
S-EPMC9061581 | biostudies-literature
ProteomicsAlternate covalent form of platelet αIIbβ3
The αIIbβ3 integrin receptor coordinates platelet adhesion, activation and mechanosensing in thrombosis and haemostasis. Using differential cysteine alkylation and mass spectrometry, we have identified a disulfide bond in the αIIb subunit linking cysteines 490 and 545 that is missing in about one in...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD025907 | Pride
Αiibβ3 Platelet Disulfide Covalent Integrin 
UnknownAnalysis of the Structural Mechanism of ATP Inhibition at the AAA1 Subunit of Cytoplasmic Dynein-1 Using a Chemical "Toolkit".
Not available
S-EPMC8304172 | biostudies-literature
ProteomicsMultiple disulfide-bonded states confer conformational diversity in fibrinogen
Disulfide bonds constrain the polypeptide backbone and reduce conformational variability in proteins. The blood clotting protein fibrinogen is constitutively produced as multiple partially disulfide-bonded states, suggesting that individual fibrinogen molecules have a variety of conformational forms...
ORGANISM(S): Homo sapiens (Human) 
2026-04-13 | PXD076459 | Pride
Human Fibrinogen Disulfide bonds 
UnknownStructural comparison of two CSPG-binding DBL domains from the VAR2CSA protein important in malaria during pregnancy.
Not available
S-EPMC3778748 | biostudies-literature
UnknownSynthesis, spectroscopic findings, SEM/EDX, DFT, and single-crystal structure of Hg/Pb/Cu-SCN complexes: In silico ADME/T profiling and promising antibacterial activities.
Not available
S-EPMC10213201 | biostudies-literature
UnknownSynthesis, characterization, crystal engineering, DFT, and biological evaluation of a novel Cu(II)-perchlorate Schiff base complex.
Not available
S-EPMC12312248 | biostudies-literature
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