The influence of truncating the carboxy-terminal amino acid residues of streptococcal enolase on its ability to interact with canine plasminogen.

Autor: Sasmit S Deshmukh, M Judith Kornblatt, Jack A Kornblatt

Publikováno v: PLoS ONE, Vol 14, Iss 1, p e0206338 (2019)

The native octameric structure of streptococcal enolase from Streptococcus pyogenes increasingly dissociates as amino acid residues are removed one by one from the carboxy-terminus. These truncations gradually convert native octameric enolase into mo

Externí odkaz: https://doaj.org/article/49084ada2e01462d908bf3bc2be6c76c

The interaction of canine plasminogen with Streptococcus pyogenes enolase: they bind to one another but what is the nature of the structures involved?

Autor: M Judith Kornblatt, Jack A Kornblatt, Mark A Hancock

Publikováno v: PLoS ONE, Vol 6, Iss 12, p e28481 (2011)

For years it has been clear that plasminogen from different sources and enolase from different sources interact strongly. What is less clear is the nature of the structures required for them to interact. This work examines the interaction between can

Externí odkaz: https://doaj.org/article/c51f0c17ea604d46b532ee4b34af46fc

The fate of the prion protein in the prion/plasminogen complex

Autor: Claude Balny, Michael C. Marden, Reinhard Lange, Stéphane Marchal, M. Judith Kornblatt, Jeanne Grosclaude, Marie-Pascale Debey, Gaston Hui Bon Hoa, Jack A. Kornblatt, Human Rezaei

Publikováno v: Biochemical and Biophysical Research Communications
Biochemical and Biophysical Research Communications, Elsevier, 2003, 305 (3), pp.518-522. ⟨10.1016/S0006-291X(03)00804-0⟩

International audience; The cellular prion protein (PrPc) forms complexes with plasminogen. Here, we show that the PrPc in this complex is cleaved to yield fragments of PrPc. The cleavage is accelerated by plasmin but does not appear to be dependent

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5945c6f1580ae2a0c0f0b98d394b1926
https://doi.org/10.1016/s0006-291x(03)00804-0

Altering Residue 134 Confers an Increased Substrate Range of Alkylated Nucleosides to the E. coli OGT Protein

Autor: Anne M. Noronha, Nadia M. Schoonhoven, M. Judith Kornblatt, Lauralicia Sacre, Derek K. O'Flaherty, Francis P. McManus, Christopher J. Wilds

Publikováno v: Molecules; Volume 22; Issue 11; Pages: 1948
Molecules, Vol 22, Iss 11, p 1948 (2017)
Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry

O6-Alkylguanine-DNA alkyltransferases (AGTs) are proteins responsible for the removal of mutagenic alkyl adducts at the O6-atom of guanine and O4-atom of thymine. In the current study we set out to understand the role of the Ser134 residue in the Esc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e89bceaf0588df8cd9a4c295b0aa8c2c
https://doi.org/10.3390/molecules22111948

Use of hydrostatic pressure to produce 'native' monomers of yeast enolase

Autor: M Judith, Kornblatt, Reinhard, Lange, Claude, Balny

Publikováno v: European journal of biochemistry. 271(19)

The effects of hydrostatic pressure on yeast enolase have been studied in the presence of 1 mm Mn(2+). When compared with apo-enolase, and Mg-enolase, the Mn-enzyme differs from the others in three ways. Exposure to hydrostatic pressure does not inac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8347978d695dcfb3eece15d3a63b1d73
https://pubmed.ncbi.nlm.nih.gov/15373835