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Heejin Park

Publications and source records attributed to Heejin Park.

3 recordsLinked to original sources

MODi: a powerful and convenient web server for identifying multiple post-translational peptide modifications from tandem mass spectra.

MOD(i) (http://modi.uos.ac.kr/modi/) is a powerful and convenient web service that facilitates the interpretation of tandem mass spectra for identifying post-translational modifications (PTMs) in a peptide. It is powerful in that it can interpret a tandem mass spectrum even when hundreds of modification types are considered and the number of potential PTMs in a peptide is large, in contrast to most of the methods currently available for spectra interpretation that limit the number of PTM sites and types being used for PTM analysis. For example, using MOD(i), one can consider for analysis both the entire PTM list published on the unimod webpage (http://www.unimod.org) and user-defined PTMs simultaneously, and one can also identify multiple PTM sites in a spectrum. MOD(i) is convenient in that it can take various input file formats such as .mzXML, .dta, .pkl and .mgf files, and it is equipped with a graphical tool called MassPective developed to display MOD(i)'s output in a user-friendly manner and helps users understand MOD(i)'s output quickly. In addition, one can perform manual de novo sequencing using MassPective.

Computer Graphics↗

Extracellular potassium deprivation reversibly dephosphorylates cofilin.

Cofilin is essential for actin filament remodeling in various cell types. We previously reported that ouabain leads to dephosphorylation of cofilin, resulting in cytoskeletal reorganization and cell volume change. We report here that the extracellular [K(+)](e) deprivation causes dephosphorylation of cofilin with disruption of cytoskeletal structures and cell shrinkage. These changes can be reversed by time-dependent restoration of [K(+)](e). Thus, these results suggest that the acute shift of [K(+)](e) triggers a reversible change of cofilin phosphorylation which may be an essential event in the regulation of cytoskeletal architecture and cell volume.

Actin Depolymerizing Factors↗