Cited by 17RNA and protein synthesis mechanismsAcute Myeloid Leukemia ResearchGenomics and Rare Diseases

Not every polymorphism close to the AUG codon can be explained by invoking context effects on initiation of translation

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Kozak, Marilyn·2003·Blood

Abstract

The −1C>T change in the annexin V gene, which reduces the risk of myocardial infarction,[1][1] cannot be explained as simply as your editorial note suggests.[2][2] The demonstration by Gonzalez-Conejero et al[1][1] that −1T increases the efficiency of translation might be correct (the fourth

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Crossref · 10.1182/blood-2002-10-3194

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  • The effect of +4G and downstream nucleotides on translation initiation has been inconclusive.

    “First, while the -3R (site 4 in the first column of Table 5) has been demonstrated repeatedly to enhance translation initiation, the effect of +4G (site 10 in Table 5), as well as nucleotides downstream, on translation initiation has been inconclusive [46,49,50,51].”

    From Detailed Dissection and Critical Evaluation of the Pfizer/BioNTech and Moderna mRNA Vaccines (2021) · cites this paper as [50]

    In the letter “Not every polymorphism close to the AUG codon can be explained by invoking context effects on initiation of translation,” Kozak says mutagenesis experiments found that +4G makes one of the strongest contributions to translation initiation. That is contrary to describing the effect of +4G as inconclusive. The References section also identifies a study reporting that +4G augments initiation, while nucleotides at +5 and +6 generally do not affect it. (LLM, conf=0.88)

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  • There is little evidence that +4G and downstream nucleotides contribute to translation initiation.

    “There is little evidence that +4G and downstream nucleotides contribute to translation initiation.”

    From Detailed Dissection and Critical Evaluation of the Pfizer/BioNTech and Moderna mRNA Vaccines (2021) · cites this paper as [50]

    In the letter “Not every polymorphism close to the AUG codon can be explained by invoking context effects on initiation of translation” (page not supplied), Kozak says that G at +4 makes one of the strongest contributions to start-codon recognition. The paper also says downstream secondary structure can compensate for a suboptimal initiation context. Its caution about a particular −1 polymorphism does not support the broad claim that there is little evidence for a contribution from +4G. (LLM, conf=0.90)

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    Experimental — accuracy not yet measured
  • The -3R has been demonstrated repeatedly to enhance translation initiation.

    “First, while the -3R (site 4 in the first column of Table 5) has been demonstrated repeatedly to enhance translation initiation, the effect of +4G (site 10 in Table 5), as well as nucleotides downstream, on translation initiation has been inconclusive [46,49,50,51].”

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Cites

No references could be resolved yet.

Research works printed but not linked: 11

  1. Gonzalez-Conejero R, Corral J, Roldan V, et al. A common polymorphism in the annexin V Kozak sequence (Ϫ1CϾT) increases translation efficiency and plasma levels of annexin V, and decreases the risk of myocardial infarction in young patients. Blood. 2002;100:2081-2086.
  2. Neufeld E. Starting out right: Kozak sequences and clots. Blood. 2002;100:1933.
  3. Kozak M. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell. 1986;44:283-292.
  4. Kozak M. Recognition of AUG and alternative initiator codons is augmented by G in position ϩ4 but is not generally affected by the nucleotides in positions ϩ5 and ϩ6. EMBO J. 1997;16:2482-2492.
  5. Kozak M. At least six nucleotides preceding the AUG initiator codon enhance translation in mammalian cells. J Mol Biol. 1987;196:947-950.
  6. Kozak M. Evaluation of the fidelity of initiation of translation in reticulocyte ly- sates from commercial sources. Nucleic Acids Res. 1990;18:2828.
  7. Kozak M. Initiation of translation in prokaryotes and eukaryotes. Gene. 1999; 234:187-208. References
  8. Bagot M, Moretta M, Sivori S, et al. CD4 ϩ cutaneous T-cell lymphoma cells ex- press the P140-killer cell immunoglobulin-like receptor. Blood. 2001; 97:1388- 1391.
  9. Nikolova M, Bagot M, Boumsell L, Bensussan A. Identification of cell surface molecules characterizing human cutaneous T-cell lymphomas. Leuk Lymph. 2002;43:741-746.
  10. Mingari MC, Moretta A, Moretta L. Regulation of KIR expression in human T lymphocytes: a safety mechanism which may impair protective T cell re- sponses. Immunol Today. 1998;19:153-157.
  11. Gardiner CM, Guethlein LA, Shilling HG, et al. Different NK cell surface pheno- types defined by DX9 antibody are due to KIR3DL1 gene polymorphism. J Im- munol. 2001;166:2992-3001.

Authors
Kozak, M.
Affiliations
Rutgers, The State University of New Jersey (US)
Corresponding author
Kozak, Marilyn
Venue
Blood
Published
2003-02-01
Volume
101
Issue
3
Pages
1202-1202
ISSN
  • 0006-4971 (ISSN-L)
  • 1528-0020
OpenAlex
W2030058321
Cited by
17
References
0
Citations by year
2022: 1 · 2021: 1 · 2016: 1 · 2014: 1 · 2012: 1
Type
journal article
Language
en
Open access
Locations
  • Blood (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Health Sciences › Medicine › Hematology › Acute Myeloid Leukemia Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genomics and Rare Diseases
Keywords
AUG codon, translation initiation, context effects, codon usage bias, start codon
MeSH terms
Animals, Humans, Polymorphism, Genetic, Protein Biosynthesis, Annexin A5, Codon, Initiator

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