Cited by 84

The DOI matches its Crossref record, with a small difference in title or year.

THE ISOELECTRIC POINT OF INSULIN

Wintersteiner, Oskar, Abramson, Harold A.·1933·Journal of Biological Chemistry

Overview

Integrity signals

Registry

Crossref · 10.1016/s0021-9258(18)76023-7

Cites

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Claims the paper makes

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Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Many proteins lose hydrophilicity near their isoelectric point.

    “Many proteins are known to lose hydrophilicity near their IEP.”

    From Reversal of ApoE4-induced recycling block as a novel prevention approach for Alzheimer’s disease (2018) · cites this paper as Wintersteiner and Abramson, 1933

  • Reduced solubility at or near their isoelectric point is a general property of many proteins including insulin.

    “reduced solubility at or near their isoelectric point is a general property of many proteins including insulin (Wintersteiner and Abramson, 1933).”

    From Reversal of ApoE4-induced recycling block as a novel prevention approach for Alzheimer’s disease (2018) · cites this paper as Wintersteiner and Abramson, 1933

  • The propensity of many proteins to lose hydrophilicity at or near their isoelectric point makes them prone to aggregation and precipitation.

    “As a mechanistic basis we propose the propensity of many proteins to lose hydrophilicity at or near their isoelectric point, which makes them prone to aggregation and precipitation, a seminal discovery that made the purification of insulin on an industrial scale possible (Wintersteiner and Abramson, 1933).”

    From Reversal of ApoE4-induced recycling block as a novel prevention approach for Alzheimer’s disease (2018) · cites this paper as Wintersteiner and Abramson, 1933

Citations

Cites

No references could be resolved yet.

Research works printed but not linked: 10

  1. Abel, 1926, Proc. Nat. Acad. Sc., 12, 132, 10.1073/pnas.12.2.132 · DOI
  2. Sörensen, 1930, Compt.-rend. trav. Lab. Carlsberg, 18
  3. Freudenberg, 1931, Z. physiol. Chem., 202, 192, 10.1515/bchm2.1931.202.4-6.192 · DOI
  4. Abel, 1927, J. Pharmacol. and Exp. Therap., 31, 65, 10.1016/S0022-3565(25)00006-0 · DOI
  5. Rosebury, 1932, Ind. and Eng. Chem., Anal. Ed., 4, 398, 10.1021/ac50080a027 · DOI
  6. MacInnes, 1929, Ind. and Eng. Chem., Anal. Ed., 1, 57, 10.1021/ac50066a001 · DOI
  7. Abramson, 1932, J. Gen. Physiol., 15, 575, 10.1085/jgp.15.5.575 · DOI
  8. Tiselius, A., Dissertation, Upsala (1930).
  9. Abramson, 1931, Physic. Rev., 37, 1714
  10. Howitt, 1932, Proc. Roy. Soc. London, Series B, 112, 13, 10.1098/rspb.1932.0073 · DOI

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Metadata

Authors
Wintersteiner, O., & Abramson, H. A.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1933-02
Volume
99
Issue
3
Pages
741-753
ISSN
0021-9258
Cited by
84
References
0
Language
en

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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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