Inactivation of Dip-Allatostatin 5 by Membrane Preparations from the CockroachDiploptera punctata

A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding

Mark A. Bradford · Analytical Biochemistry · 1976 · 225.3K citations

Protein Chemistry, Biochemistry, Protein Folding +13

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Marion M. Bradford · Analytical Biochemistry · 1976 · 209.3K citations

Protein Chemistry, Biochemistry, Protein Folding +13

Comprehensive insect physiology, biochemistry and pharmacology

Journal of Insect Physiology · 1985 · 4.8K citations

Biology, Physiology, Entomology +3

Primary structure of four allatostatins: neuropeptide inhibitors of juvenile hormone synthesis.

Andrea P. Woodhead, Barbara Stay, Sharon L. Seidel et al. · Proceedings of the National Academy of Sciences · 1989 · 414 citations

Glycobiology, Neuropeptide Inhibitors, Chemical Biology +19

Substance P and [Leu]enkephalin are hydrolyzed by an enzyme in pig caudate synaptic membranes that is identical with the endopeptidase of kidney microvilli.

Rebecca Matsas, I S Fulcher, A J Kenny et al. · Proceedings of the National Academy of Sciences · 1983 · 373 citations · Full text

Protein Secretion, Enzymatic Modification, Substance P +17