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ProteomicsLys-C/Arg-C, a New Enzyme Combination for Next-Generation Proteomics
Today, the most widely used bottom-up proteomics studies necessitate a proteolysis step prior to MS analysis. Trypsin is often the best protease in choice due to its high specificity and MS-favored proteolytic products. Trypsin has been challenged for its low cleavage efficiency at Lys-X bonds, and ...
ORGANISM(S): Homo sapiens (Human) 
2018-07-24 | PXD009797 | Pride
Lys-c / arg-c / trypsin / dia / mass spectrometry 
ProteomicsSystematic optimization of C-TAILS approach for deep screening of C-terminomics
It is well known that protein C-termini play important roles in various biological processes, and thus the precise characterization of C-termini is essential for fully elucidating protein structure and understanding protein functions. Although many efforts have been made in the fields during the lat...
ORGANISM(S): Escherichia coli 
2015-09-15 | PXD002409 | Pride
Protein c-termini Acetylation Scii 
ProteomicsReversible Lysine Derivatization Enables High Specificity of Arg-C Digestion Using Trypsin
Bottom-up proteomics approach has become an important strategy in diverse areas of biological research, and the enzymatic digestion is essential for this technology. Endopeptidase Arg-C catalyzing the hydrolytic cleavage of peptide bonds C-terminal to arginine could be an important protease in botto...
ORGANISM(S): Homo sapiens (Human) Escherichia coli 
2018-01-04 | PXD007994 | Pride
Proteomics Arg-c Trypsin Lys-c Citraconylation Lc-ms/ms 
UnknownInfluence of Ligand and Nuclearity on the Cytotoxicity of Cyclometallated C^N^C Platinum(II) Complexes.
Not available
S-EPMC7756510 | biostudies-literature
ProteomicsShort-term mild temperature-stress-induced alterations in C. elegans phosphoproteome
Exposure to mild early-life stresses can slow down the aging process, in which protein phosphorylation might be an essential regulator. Currently, the understanding of phosphorylation-based regulatory networks under mild early-life stress remains elusive. Herein, we systematically analyzed the phosp...
ORGANISM(S): Caenorhabditis elegans 
2020-09-17 | PXD021081 | Pride
Phosphoproteomics  c. elegans  mild temperature  lifespan  mild stresses 
UnknownThe Born in Bradford COVID-19 Research Study: Protocol for an adaptive mixed methods research study to gather actionable intelligence on the impact of COVID-19 on health inequalities amongst families living in Bradford.
Not available
S-EPMC7523536 | biostudies-literature
ProteomicsBasic Strong Cation Exchange Chromatography, BaSCX, a Highly Efficient Approach for C-Terminomic Studies Using LysargiNase Digestion
Decoding protein C-termini is a challenging task in protein chemistry using conventional chemical/enzymatic approaches. With the rapid development in modern mass spectrometer, many advanced mass spectrometry (MS) based protein C-termini analysis approaches have been established. Although great progr...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) Caenorhabditis elegans 
2020-02-28 | PXD016317 | Pride
C-terminomics / lysarginase / scx / bascx / mass spectrometry 
UnknownUnderstanding the patterns and health impact of indoor air pollutant exposures in Bradford, UK: a study protocol.
Not available
S-EPMC10711829 | biostudies-literature
ProteomicsAP-MS of tissue-specific protein complexes in C. elegans
We present a method for the tissue-specific purification of protein complexes from the nematode C. elegans, based on cell-type specific biotinylation. To purify proteins from specific C. elegans tissues, we adapted a system based on in vivo biotinylation of a protein of interest. In this approach, a...
ORGANISM(S): Caenorhabditis elegans 
2016-07-18 | PXD002139 | Pride
Bira biotin ligase C. elegans Ap-ms 
UnknownChanges in children's wellbeing in Bradford during COVID-19: The Born in Bradford COVID-19 longitudinal research study.
Not available
S-EPMC9971641 | biostudies-literature
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