Structural studies on bovine γ-crystallin is a research paper published in Biochemical Journal (1971). On theSindex it has a DataRank of 0.723. It has been cited 11 times, with 6 citing works in its 1-hop citation network.
The amino acid sequences around the cysteine residues in the lens protein, γ-crystallin, were studied. Fraction II of the γ-crystallin from calf lens (Björk, 1964) was used. The protein was oxidized with performic acid and then hydrolysed with trypsin. Six peptides containing cysteic acid were isolated. One of the peptides contained three residues of cysteic acid and the others contained one residue of cysteic acid. We conclude that there are eight unique residues of cysteic acid in the oxidized protein. Amino acid analysis suggests that there are also eight residues of cysteic acid in the molecule, which thus contains only one polypeptide chain.
FAIR checklist signals are shown for context only and do not affect DataRank scoring.
Base Score Contribution
0.373
From this paper's citation signal
Citation Network Contribution
0.350
From 6 citing papers with measurable signal
Ranked by citation count — the same ordering the engine uses when summing log1p(Cq) over citers.
DataRank blends this paper's own citation count with the influence of the papers that cite it. Here, roughly 52% comes from its base citations and 48% from the citation network (6 citing papers contributed measurable signal).
Citers are pulled from OpenAlex sorted by cited_by_count:descand capped per paper, so when the cap binds we keep the highest-signal references and the score is reproducible across reruns.
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