2017
DOI: 10.1016/j.bmhimx.2017.03.009
|View full text |Cite
|
Sign up to set email alerts
|

Proteomics: a tool to develop novel diagnostic methods and unravel molecular mechanisms of pediatric diseases

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2

Citation Types

0
2
0

Year Published

2019
2019
2019
2019

Publication Types

Select...
1

Relationship

0
1

Authors

Journals

citations
Cited by 1 publication
(2 citation statements)
references
References 23 publications
0
2
0
Order By: Relevance
“…The same protein in different physiological states, different subcellular localization, different amino acid site modification, may correspond to different functions. 47 Ostareck-Lederer et al 48 showed that hnRNP K phosphorylation by c-Src reversibly impairs the binding between hnRNP K and the differentiation control element (DICE) of LOX mRNA, and activates the DICE-bearing mRNAs. For this phenomenon, Ostareck et al 49 explained the mechanism.…”
Section: Hnrnp K Involves In Posttranslational Modificationmentioning
confidence: 99%
See 1 more Smart Citation
“…The same protein in different physiological states, different subcellular localization, different amino acid site modification, may correspond to different functions. 47 Ostareck-Lederer et al 48 showed that hnRNP K phosphorylation by c-Src reversibly impairs the binding between hnRNP K and the differentiation control element (DICE) of LOX mRNA, and activates the DICE-bearing mRNAs. For this phenomenon, Ostareck et al 49 explained the mechanism.…”
Section: Hnrnp K Involves In Posttranslational Modificationmentioning
confidence: 99%
“…Protein modification (PTM) is vital in the life process, which is closely related to gene expression, signaling pathway, cell division, and other processes. The same protein in different physiological states, different subcellular localization, different amino acid site modification, may correspond to different functions . Ostareck‐Lederer et al showed that hnRNP K phosphorylation by c‐Src reversibly impairs the binding between hnRNP K and the differentiation control element (DICE) of LOX mRNA, and activates the DICE‐bearing mRNAs.…”
Section: Hnrnp K Involves In Posttranslational Modificationmentioning
confidence: 99%