2018
DOI: 10.1016/j.jprot.2018.04.018
|View full text |Cite
|
Sign up to set email alerts
|

A tandem mass tag (TMT) proteomic analysis during the early phase of experimental pancreatitis reveals new insights in the disease pathogenesis

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1

Citation Types

0
24
1
1

Year Published

2018
2018
2023
2023

Publication Types

Select...
6

Relationship

1
5

Authors

Journals

citations
Cited by 12 publications
(26 citation statements)
references
References 49 publications
0
24
1
1
Order By: Relevance
“…In its turn, lysosomal cysteine protease cathepsin B appears to be an important factor in the activation of trypsinogen to trypsin [62]. This model has also been used in the study of the identification of new protein alterations and biomarkers [63] characterizing pancreatic inflammatory damage with proteomic [64] and metabolomic [65] analysis. The advantages of this model are its noninvasiveness, inexpensiveness, rapid induction, and wide reproducibility and applicability.…”
Section: Murine Models: a Practical Overviewmentioning
confidence: 99%
“…In its turn, lysosomal cysteine protease cathepsin B appears to be an important factor in the activation of trypsinogen to trypsin [62]. This model has also been used in the study of the identification of new protein alterations and biomarkers [63] characterizing pancreatic inflammatory damage with proteomic [64] and metabolomic [65] analysis. The advantages of this model are its noninvasiveness, inexpensiveness, rapid induction, and wide reproducibility and applicability.…”
Section: Murine Models: a Practical Overviewmentioning
confidence: 99%
“…The data reported here includes a shotgun proteomic experiment involving sixplex Tandem Mass Tag (TMT 6 ) labeling that allowed the simultaneous identification and quantification of the early phase of AP proteome from the soluble and the whole membrane pancreatic fractions from three AP and three control animals [1] .…”
Section: Datamentioning
confidence: 99%
“…We identified 997 unique proteins, of which 353 were significantly different (22, 276 or 55 in both, the soluble or the membrane fractions, respectively). Accordingly, using TMT proteomics and bioinformatic tools, in García-Hernández et al, 2018- [1] we were able to detect significant changes in protein expression related to many pathobiological pathways of AP as from the early phase of the disease, including some changes never described before in this disease. Proteomics data are publicly available in ProteomeXchange via PRIDE through the identifier PXD007096.…”
mentioning
confidence: 92%
See 2 more Smart Citations