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PubMed Publications| Keyword search (4,163 papers available) |  |
"Kornblatt MJ" Authored Publications:
| Title | Authors | PubMed ID | |
|---|---|---|---|
| 1 | The binding of Na(+) to apo-enolase permits the binding of substrate. | Lin T, Kornblatt MJ | 10669792 CHEMBIOCHEM |
| 2 | Cloning, expression and mutagenesis of a subunit contact of rabbit muscle-specific (betabeta) enolase. | Kornblatt MJ, Zheng SX, Lamandé N, Lazar M | 12044909 CHEMBIOCHEM |
| 3 | The Energetics of Streptococcal Enolase Octamer Formation: The Quantitative Contributions of the Last Eight Amino Acids at the Carboxy-Terminus. | Kornblatt JA, Quiros V, Kornblatt MJ | 26287818 BIOLOGY |
| 4 | Altering Residue 134 Confers an Increased Substrate Range of Alkylated Nucleosides to the E. coli OGT Protein. | Schoonhoven NM, O'Flaherty DK, McManus FP, Sacre L, Noronha AM, Kornblatt MJ, Wilds CJ | 29137116 CHEMBIOCHEM |
| 5 | The influence of truncating the carboxy-terminal amino acid residues of streptococcal enolase on its ability to interact with canine plasminogen. | Deshmukh SS, Kornblatt MJ, Kornblatt JA | 30653526 BIOLOGY |
| Title: | Altering Residue 134 Confers an Increased Substrate Range of Alkylated Nucleosides to the E. coli OGT Protein. | ||||
| Authors: | Schoonhoven NM, O'Flaherty DK, McManus FP, Sacre L, Noronha AM, Kornblatt MJ, Wilds CJ | ||||
| Link: | https://www.ncbi.nlm.nih.gov/pubmed/29137116?dopt=Abstract | ||||
| Publication: | |||||
| Keywords: | |||||
| PMID: | 29137116 | Category: | Molecules | Date Added: | 2019-05-31 |
| Dept Affiliation: |
CHEMBIOCHEM
1 Department of Chemistry and Biochemistry, Concordia University, Montréal, QC H4B 1R6, Canada. nadiaschoonhoven@hotmail.com. 2 Department of Chemistry and Biochemistry, Concordia University, Montréal, QC H4B 1R6, Canada. derek_oflaherty@hotmail.com. 3 Howard Hughes Medical Institute, Department of Molecular Biology and Center for Computational and Integrative Biology, Massachusetts General Hospital, Boston, MA 02114, USA. derek_oflaherty@hotmail.com. 4 Department of Chemistry and Biochemistry, Concordia University, Montréal, QC H4B 1R6, Canada. shent13@hotmail.com. 5 Institute for Research in Immunology and Cancer, Université de Montréal, Montréal, QC H3T 1J4, Canada. shent13@hotmail.com. 6 Department of Chemistry and Biochemistry, Concordia University, Montréal, QC H4B 1R6, Canada. dlsacre@hotmail.com. 7 Department of Chemistry and Biochemistry, Concordia University, Montréal, QC H4B 1R6, Canada. anne.noronha@concordia.ca. 8 Department of Chemistry and Biochemistry, Concordia University, Montréal, QC H4B 1R6, Canada. Judith.Kornblatt@concordia.ca. 9 Department of Chemistry and Biochemistry, Concordia University, Montréal, QC H4B 1R6, Canada. Chris.Wilds@concordia.ca. |
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Description: |
Altering Residue 134 Confers an Increased Substrate Range of Alkylated Nucleosides to the E. coli OGT Protein. Molecules. 2017 Nov 11;22(11): Authors: Schoonhoven NM, O'Flaherty DK, McManus FP, Sacre L, Noronha AM, Kornblatt MJ, Wilds CJ Abstract PMID: 29137116 [PubMed - indexed for MEDLINE] |
