DPH1 (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "DPH1" in English language version.

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doi.org (Global: 2^nd place; English: 2^nd place)

Phillips NJ, Zeigler MR, Deaven LL (May 1996). "A cDNA from the ovarian cancer critical region of deletion on chromosome 17p13.3". Cancer Lett. 102 (1–2): 85–90. doi:10.1016/0304-3835(96)04169-9. PMID 8603384.
Liu S, Milne GT, Kuremsky JG, Fink GR, Leppla SH (Oct 2004). "Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2". Mol Cell Biol. 24 (21): 9487–97. doi:10.1128/MCB.24.21.9487-9497.2004. PMC 522255. PMID 15485916.
Webb TR, Cross SH, McKie L, Edgar R, Vizor L, Harrison J, Peters J, Jackson IJ (2008). "Diphthamide modification of eEF2 requires a J-domain protein and is essential for normal development". J. Cell Sci. 121 (Pt 19): 3140–5. doi:10.1242/jcs.035550. PMC 2592597. PMID 18765564. Diphthamide modification is present in all eukaryotic organisms, in which it is restricted to a histidine residue of translation elongation factor 2 (eEF2, also known as EFT1; position 715 in mammals and 699 in yeast)

"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Liu S, Milne GT, Kuremsky JG, Fink GR, Leppla SH (Oct 2004). "Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2". Mol Cell Biol. 24 (21): 9487–97. doi:10.1128/MCB.24.21.9487-9497.2004. PMC 522255. PMID 15485916.
"Entrez Gene: DPH1 DPH1 homolog (S. cerevisiae)".
Webb TR, Cross SH, McKie L, Edgar R, Vizor L, Harrison J, Peters J, Jackson IJ (2008). "Diphthamide modification of eEF2 requires a J-domain protein and is essential for normal development". J. Cell Sci. 121 (Pt 19): 3140–5. doi:10.1242/jcs.035550. PMC 2592597. PMID 18765564. Diphthamide modification is present in all eukaryotic organisms, in which it is restricted to a histidine residue of translation elongation factor 2 (eEF2, also known as EFT1; position 715 in mammals and 699 in yeast)

Phillips NJ, Zeigler MR, Deaven LL (May 1996). "A cDNA from the ovarian cancer critical region of deletion on chromosome 17p13.3". Cancer Lett. 102 (1–2): 85–90. doi:10.1016/0304-3835(96)04169-9. PMID 8603384.
Liu S, Milne GT, Kuremsky JG, Fink GR, Leppla SH (Oct 2004). "Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2". Mol Cell Biol. 24 (21): 9487–97. doi:10.1128/MCB.24.21.9487-9497.2004. PMC 522255. PMID 15485916.
Webb TR, Cross SH, McKie L, Edgar R, Vizor L, Harrison J, Peters J, Jackson IJ (2008). "Diphthamide modification of eEF2 requires a J-domain protein and is essential for normal development". J. Cell Sci. 121 (Pt 19): 3140–5. doi:10.1242/jcs.035550. PMC 2592597. PMID 18765564. Diphthamide modification is present in all eukaryotic organisms, in which it is restricted to a histidine residue of translation elongation factor 2 (eEF2, also known as EFT1; position 715 in mammals and 699 in yeast)