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Studies by 1H nuclear magnetic resonance and distance geometry of the solution conformation of the α-amylase inhibitor Tendamistat

Data up to Jan 2025

Published1986
Citations170
References21

Total Citations Per Year

Abstract

References (21)

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1981 • 504 citations

An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformations in solution

1985 • 373 citations

Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance

1983 • 336 citations

A distance geometry program for determining the structures of small proteins and other macromolecules from nuclear magnetic resonance measurements of intramolecular H-H proximities in solution

1984 • 288 citations

Combined use of proton-proton overhauser enhancements and a distance geometry algorithm for determination of polypeptide conformations. Application to micelle-bound glucagon

1981 • 267 citations

Secondary structure of the α-amylase polypeptide inhibitor Tendamistat from Streptomyces tendae determined in solution by 1H nuclear magnetic resonance

1985 • 200 citations

Crystal structure determination, refinement and the molecular model of the α-amylase inhibitor Hoe-467A

1986 • 189 citations

Tendamistat (HOE 467), a tight-binding alpha-amylase inhibitor from Streptomyces tendae 4158. Isolation, biochemical properties

1984 • 111 citations

Interactive program for investigation of protein structures based on 1H NMR experiments

1985 • 45 citations

Amino Acid Sequence of Protein α-Amylase Inhibitor from Streptomyces griseosporeus YM-25

1985 • 37 citations

Isolation and structure elucidation of an α‐amylase inhibitor, AI‐3688, from Streptomyces aureofaciens

1985 • 32 citations

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1983 • 22 citations

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Studies by 1H nuclear magnetic resonance and distance geometry of the solution… (1986) – Journal of Molecular Biology | Metascience Observatory Explorer