ReviewOrigins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life2004
N-phosphoryl amino acids and biomolecular origins.
Review in Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed.
- How Prebiotic Chemistry and Early Life Chose Phosphate.Life (Basel, Switzerland) · 2019Review
- Natural Products Containing 'Rare' Organophosphorus Functional Groups.Molecules (Basel, Switzerland) · 2019Review
- An isotope (18O, 15N, and 2H) technique to investigate the metal ion interactions between the phosphoryl group and amino acid side chains by electrospray ionization mass spectrometry.Journal of the American Society for Mass Spectrometry · 2011Article
- Amino acid homochirality may be linked to the origin of phosphate-based life.Journal of molecular evolution · 2010Article
- Apoptosis induced by (di-isopropyloxyphoryl-Trp)2-Lys-OCH3 in K562 and HeLa cells.Journal of biosciences · 2008Article
- Steps towards the formation of a protocell: the possible role of short peptides.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2007Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The possible role of phosphoryl amino acids for biomolecular origins is briefly reviewed. Peptide formation, ester formation, ester exchange on phosphorus and N to O migration occurred when the N-phosphoryl amino acid was incubated at room temperature. Short nucleotides and peptides were formed when nucleoside was reacted with N-phosphoryl amino acid at room temperature. Serine and threonine residues in their conjugate with different nucleosides (mediated with phosphorus) showed different self-cleavage activities. N-phosphoryl Histine and Ser-His dipeptide could cleave nucleic acids, proteins and esters in neutral medium. Based on a simple model, a pathway of 'co-evolution of protein and nucleic acid' was proposed.
Indexed as
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15573496What OpenQuestion holds
Registered trials
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