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Cited by 4Thyroid Disorders and TreatmentsProtein Structure and DynamicsEnzyme Structure and Function

The Molecular Weight of Thyroglobulin

Heidelberger, Michael, Svedberg, The·1934·Science
DOI 10.1126/science.80.2079.414.a
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  • TG is a protein dimer of 600 kDa with an unusually high number of ~60 disulfide bonds per monomer and 17 glycosylation sites, which confer remarkable stability and solubility to the protein.

    “TG, a protein dimer of 600 kDa, has an unusually high number of ~ 60 disulfide bonds per monomer and 17 glycosylation sites, which confer remarkable stability and solubility to the protein1,2,9.”

    From The structure of human thyroglobulin (2020) · cites this paper as [9]

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Authors
Heidelberger, M., & Svedberg, T.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1934-11-02
Volume
80
Issue
2079
Pages
414-414
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.80.2079.414.a
OpenAlex
W4242076665
Cited by
4
References
0
Citations by year
2021: 1 · 2020: 3
FWCI
0.00
Type
journal article
Language
en
Open access
closed
Locations
Science (publishedVersion)
Topics
  • Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Disorders and Treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
thyroglobulin, molecular weight, thyroid gland

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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

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