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UnknownIn-depth, high-accuracy proteomics of sea urchin tooth organic matrix.
Not available
S-EPMC2614417 | biostudies-literature
UnknownThe Lottia gigantea shell matrix proteome: re-analysis including MaxQuant iBAQ quantitation and phosphoproteome analysis.
Not available
S-EPMC4094399 | biostudies-literature
ProteomicsProteomics of valve silica deposition vesicles from the diatom Thalassiosira pseudonana
Biomineral forming organisms produce inorganic materials with complex, genetically encoded morphologies that are inaccessible by current synthetic chemistry. It is poorly understood which genes are involved in biomineral morphogenesis and how the encoded proteins guide this process. We addressed the...
ORGANISM(S): Thalassiosira pseudonana CCMP1335 
2022-11-21 | PXD033943 | Pride
Silica deposition vesicles (sdv) Thalassiosira pseudonana ccmp1335 
UnknownPhosphoproteomes of Strongylocentrotus purpuratus shell and tooth matrix: identification of a major acidic sea urchin tooth phosphoprotein, phosphodontin.
Not available
S-EPMC2830187 | biostudies-literature
UnknownThe molecular basis for pore pattern morphogenesis in diatom silica.
Not available
S-EPMC9894196 | biostudies-literature
UnknownThe sea urchin (Strongylocentrotus purpuratus) test and spine proteomes.
Not available
S-EPMC2527298 | biostudies-literature
ProteomicsLymnaea shell proteomics - Molecular modularity and asymmetry of the molluscan mantle revealed by a gene expression atlas
The calcifying matrix proteins embedded within the shell biomineral structure is a mixture of proteins, glycoproteins, and polysaccharides that are involved in the shell formation processes. Here with develop bottom-up shotgun proteomic investigation of these proteins, thanks to specific transcripto...
ORGANISM(S): Lymnaea stagnalis 
2018-04-05 | PXD008547 | Pride
Lymnaea stagnalis Biomineralization Shell matrix proteins 
ProteomicsProteins are well-preserved in shells toasted at 300°C revealed by proteomics
The development of protein anti-degradation strategy is important for their storage at ambient conditions. Despite that it is known that biominerals, typical inorganic-organic composites, can preserve proteins at room temperature for a long time, it is unclear the extent of protein degradation under...
ORGANISM(S): Haliotis discus hannai 
2022-07-01 | PXD030901 | Pride
Shell matrix proteins  biomineralization  high temperature 
UnknownData set for the proteomic inventory and quantitative analysis of chicken uterine fluid during eggshell biomineralization.
Not available
S-EPMC4459565 | biostudies-literature
ProteomicsSilica associated proteomes of three diatoms reveal conservation of sequence motifs, proteins highly conserved among diatoms, and proteins targeted to specific silica structures
Proteins associated with diatom silica are likely involved in the biogenesis of the complex, species-specific morphologies of the biomineral, but only very few such proteins have been identified. In this project we extracted and identified proteins from three related, but morphologically distinct, s...
ORGANISM(S): Thalassiosira pseudonana CCMP1335 Cyclotella cryptica Thalassiosira cf. oceanica 
2022-05-30 | PXD026496 | Pride
Biomineralization Proteomics Silaffin Intrinsically disordered proteins Valve Morphogenesis Girdle band Cell wall Fultoportula 
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