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The homologous angiogenin and ribonuclease N-terminal fragments fold into very similar helices when isolated

Data up to Jan 2025

Published1992
Citations14
References24

Total Citations Per Year

Abstract

References (24)

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1989 • 5,198 citations

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1984 • 189 citations

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1989 • 154 citations

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1990 • 140 citations

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1990 • 106 citations

Thermodynamic parameters for the helix-coil thermal transition of ribonuclease-S-peptide and derivatives from1H-nmr data

1986 • 65 citations

Low‐temperature 1H‐NMR evidence of the folding of isolated ribonuclease S‐peptide

1983 • 64 citations

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1984 • 50 citations

Characterization of low populated peptide helical structures in solution by means of NMR proton conformational shifts

1990 • 35 citations

Location of an .alpha.-helix in fragment 96-133 from bovine somatotropin by proton NMR spectroscopy

1988 • 32 citations

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1983 • 24 citations

Conformational properties of the isolated 1–23 fragment of human hemoglobin α-chain

1988 • 24 citations

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1990 • 22 citations

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1985 • 15 citations

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1986 • 10 citations

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The homologous angiogenin and ribonuclease N-terminal fragments fold into very similar… (1992) – Biochemical and Biophysical Research Communications | Metascience Observatory Explorer