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The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Glutamine deamidation: an indicator of antiquity, or preservational quality?

Schroeter, Elena R., Cleland, Timothy P.·2016·Rapid Communications in Mass Spectrometry
DOI 10.1002/rcm.7445
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Abstract

Rationale: Much credence has been given in the paleoproteomic community to glutamine deamidation as a proxy for the age of proteins derived from fossil and subfossil material, and this modification has been invoked as a means for determining the endogeneity of molecules recovered from very old fossil specimens. Methods: We re‐evaluated the relationship between glutamine deamidation and geologic time by examining previously published data from five recent mass spectrometry studies of archeaological fossils. Deamidation values recovered for fossils were graphed against their reported chronologic age using WebPlotDigitizer. Results: The experimental data that has been produced from fossil material to date show that the extent of glutamine deamidation does not correspond to the absolute age of the specimens being examined, but rather show extreme variation between specimens of similar age and taxonomic affinity. Conclusions: Because deamidation rates and levels can be greatly affected by numerous chemical and environmental factors, we propose that glutamine deamidation is better suited as an indicator of preservational quality and/or environmental conditions than a mark of the endogeneity or authenticity of ancient proteins. Copyright © 2015 John Wiley & Sons, Ltd.

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Crossref · 10.1002/rcm.7445

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  • Modifications to amino acid side chains have been linked to age-induced degradation, which may be a useful indicator of protein degradation or authentically ancient proteins, although other factors such as heat may also induce modifications.

    “While PTMs can be the result of biological processes integral to protein function, modifications to amino acid side chains have also been linked to age-induced degradation, which may be a useful indicator of protein degradation or even authentically ancient proteins, although other factors, such as heat, may also induce modifications (76).”

    From Ancient protein analysis in archaeology (2021) · cites this paper as [76]

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Metadata

Authors
Schroeter, E. R., & Cleland, T. P.
Affiliations
  • Department of Biological Sciences North Carolina State University Raleigh NC 27695 USA
  • Department of Biomedical Engineering Rensselaer Polytechnic Institute Troy NY 12182 USA
Venue
Rapid Communications in Mass Spectrometry
Publisher
Wiley
Published
2015-12-17
Volume
30
Issue
2
Pages
251-255
ISSN
  • 0951-4198
  • 1097-0231
DOI
10.1002/rcm.7445
Cited by
118
References
2
Language
en
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor)

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