Peptide Elongation Factors
"Peptide Elongation Factors" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Protein factors uniquely required during the elongation phase of protein synthesis.
Below are MeSH descriptors whose meaning is more general than "Peptide Elongation Factors".
Below are MeSH descriptors whose meaning is more specific than "Peptide Elongation Factors".
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Below are the most recent publications written about "Peptide Elongation Factors" by people in Profiles.
Mitochondrial fission links ECM mechanotransduction to metabolic redox homeostasis and metastatic chemotherapy resistance. Nat Cell Biol. 2022 02; 24(2):168-180.
An epigenetic increase in mitochondrial fission by MiD49 and MiD51 regulates the cell cycle in cancer: Diagnostic and therapeutic implications. FASEB J. 2020 04; 34(4):5106-5127.
Epigenetic Dysregulation of the Dynamin-Related Protein 1 Binding Partners MiD49 and MiD51 Increases Mitotic Mitochondrial Fission and Promotes Pulmonary Arterial Hypertension: Mechanistic and Therapeutic Implications. Circulation. 2018 07 17; 138(3):287-304.
The role of Drp1 adaptor proteins MiD49 and MiD51?in mitochondrial fission: implications for human disease. Clin Sci (Lond). 2016 11 01; 130(21):1861-74.
Mandibulofacial Dysostosis with Microcephaly: Mutation and Database Update. Hum Mutat. 2016 Feb; 37(2):148-54.
Mechanistic insights on the folding of a large ribozyme during transcription. Biochemistry. 2005 May 24; 44(20):7535-42.
The elongation factor ELL (eleven-nineteen lysine-rich leukemia) is a selective coregulator for steroid receptor functions. Mol Endocrinol. 2005 May; 19(5):1158-69.
ELL and EAF1 are Cajal body components that are disrupted in MLL-ELL leukemia. Mol Biol Cell. 2003 Apr; 14(4):1517-28.
The elongation factors Pandora/Spt6 and Foggy/Spt5 promote transcription in the zebrafish embryo. Development. 2002 Apr; 129(7):1623-32.
The elongation domain of ELL is dispensable but its ELL-associated factor 1 interaction domain is essential for MLL-ELL-induced leukemogenesis. Mol Cell Biol. 2001 Aug; 21(16):5678-87.