Krouse ME, Lester HA, Wassermann NH, Erlanger BF (1985)
Rates and equilibria for a photoisomerizable antagonist at the acetylcholine receptor of Electrophorus electroplaques
Journal of General Physiology 86: 235

Nargeot J, Lester HA, Birdsall NJ, Stockton J, Wassermann NH, Erlanger BF (1982)
A photoisomerizable muscarinic antagonist. Studies of binding and of conductance relaxations in frog heart
Journal of General Physiology 79: 657

Lester HA, Krouse ME, Nass MM, Wassermann NH, Erlanger BF (1980)
A covalently bound photoisomerizable agonist: comparison with reversibly bound agonists at Electrophorus electroplaques
Journal of General Physiology 75: 207

Lester HA, Nass MM, Krouse ME, Nerbonne JM, Wassermann NH, Erlanger BF (1980)
Electrophysiological experiments with photoisomerizable cholinergic compounds: review and progress report
Annals of the New York Academy of Sciences 346: 475

Wassermann NH, Bartels E, Erlanger BF (1979)
Conformational properties of the acetylcholine receptor as revealed by studies with constrained depolarizing ligands
Proc Natl Acad Sci U S A 76: 256

Bieth J, Vratsanos SM, Wassermann NH, Cooper AG, Erlanger BF (1973)
Photoregulation of biological activity by photochromic reagents. Inactivators of acetylcholinesterase
Biochemistry 12: 3023

Bartels E, Wassermann NH, Erlanger BF (1971)
Photochromic activators of the acetylcholine receptor
Proc Natl Acad Sci U S A 68: 1820

Bieth J, Vratsanos SM, Wassermann N, Erlanger BF (1969)
Photoregulation of biological activity by photocromic reagents. II. Inhibitors of acetylcholinesterase
Proc Natl Acad Sci U S A 64: 1103

Deal WJ, Erlanger BF, Nachmansohn D (1969)
Photoregulation of biological activity by photochromic reagents. 3. Photoregulation of bioelectricity by acetylcholine receptor inhibitors
Proc Natl Acad Sci U S A 64: 1230

Kaufman H, Vratsanos SM, Erlanger BF (1968)
Photoregulation of an enzymic process by means of a light-sensitive ligand
Science 162: 1487

Erlanger BF, Cohen W, Vratsanos SM, Castleman H, Cooper AG (1965)
Postulated chemical basis for observed differences in the enzymatic behavior of chymotrypsin and trypsine
Nature 205: 868