PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 13998950

A multiple ribosomal structure in protein synthesis.

J R WARNER·P M KNOPF·A RICH
View original source ↗Export metadata ↓

Abstract

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

Explore related subjects

NucleoproteinsProtein BiosynthesisRNAReticulocytesRibosomesNUCLEOPROTEINSRETICULOCYTESJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

J R WARNER, P M KNOPF, A RICH. 1963-01-15. A multiple ribosomal structure in protein synthesis.. https://doi.org/10.1073/pnas.49.1.122

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

KEEP EXPLORING

Related citations

PubMed2004

Structural studies on the Ebola virus matrix protein VP40 indicate that matrix proteins of enveloped RNA viruses are analogues but not homologues.

Matrix proteins are the driving force of assembly of enveloped viruses. Their main function is to interact with and polymerize at cellular membranes and link other viral components to the matrix-membrane complex resulting in individual particle shapes and ensuring the integrity of the viral particle. Although matrix proteins of different virus families show functional analogy, they share no sequence or structural homology, Their diversity is also evident in that they use a variety of late domain motifs to commit the cellular vacuolar protein sorting machinery to virus budding. Here, we discuss the structural and functional aspects of teh filovirus matrix protein VP40 and compare them to other known matrix protein structures from vesicular stomatitis virus adn retroviral matrix protein.

Nucleoproteins↗