PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 9723731

Elucidation of functionally significant structural modifications by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry with post-source decay.

J J Gorman·A W Purcell·B L Ferguson·S Lopaticki·C J Morrow·E Mineva
View original source ↗Export metadata ↓

Abstract

The source did not provide an abstract. Follow the original record for more information.

Explore related subjects

Newcastle disease virusNucleocapsid ProteinsPhosphorylationProtein ConformationSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

J J Gorman, A W Purcell, B L Ferguson, S Lopaticki, C J Morrow, E Mineva. 1998. Elucidation of functionally significant structural modifications by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry with post-source decay.. https://pubmed.ncbi.nlm.nih.gov/9723731/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2004

Identification of phosphoprotein:phosphoprotein and phosphoprotein:nucleocapsid protein interaction domains of the Newcastle disease virus.

The yeast two-hybrid system has been used to identify domains of the Newcastle disease virus (NDV) phosphoprotein (P) involved in self-association and interaction with the nucleocapsid protein (NP). Deletion analysis was used to map the domain(s) of the P protein involved in P:P and P:NP interactions. The C-terminal 45 amino acids (residues 247-291) were shown to play a major role in both of the interactions. Comparison of these findings with other reports suggests that paramyxoviruses are different with respect to interaction domain(s) between these two essential viral proteins involved in genome replication.

Newcastle disease virus↗
PubMed1984

Protein kinase associated with Newcastle disease virus.

Purified virions of Newcastle disease virus (NDV) were found to contain protein kinase activity which was, like other virion-associated kinases, stimulated by Mg2+, and totally independent of Ca2+ and cAMP. The kinase phosphorylated preferentially the P and NP polypeptides of NDV. Triton-KCl fractionation of the virions has shown that the protein kinase activity may be associated with glycoprotein-free subviral particles, but not with nucleocapsids containing either only NP or some L and P proteins together with NP as protein constituent.

Newcastle disease virus↗