W. Welches

A comparison of the properties and enzymatic activities of three angiotensin processing enzymes: angiotensin converting enzyme, prolyl endopeptidase and neutral endopeptidase 24.11.

C. Ferrario, K. Brosnihan, W. Welches, 1993, Life sciences.

Evidence that prolyl endopeptidase participates in the processing of brain angiotensin.

C. Ferrario, M. Chappell, K. Brosnihan, 1991, Journal of hypertension.

A new class of phospholipases A2 with lysine in place of aspartate 49. Functional consequences for calcium and substrate binding.

R. Heinrikson, J. Maraganore, W. Cho, 1984, The Journal of biological chemistry.

Inhibition of angiotensin converting enzyme by the metalloendopeptidase 3.4.24.15 inhibitor c-phenylpropyl-alanyl-alanyl-phenylalanyl-p-aminobenzoate

C. Ferrario, M. Chappell, K. Brosnihan, 1992, Peptides.

An examination of structural interactions presumed to be of importance in the stabilization of phospholipase A2 dimers based upon comparative protein sequence analysis of a monomeric and dimeric enzyme from the venom ofAgkistrodon p. piscivorus

I. Reardon, R. Heinrikson, W. Welches, 1993, Journal of protein chemistry.

Characterization by high performance liquid chromatography of angiotensin peptides in the plasma and cerebrospinal fluid of the dog

C. Ferrario, M. Chappell, W. Welches, 1987, Peptides.

Active center studies on bacterial luciferase: modification of the enzyme with 2,4-dinitrofluorobenzene.

T. Baldwin, W. Welches, 1981, Biochemistry.

Confirmation of mendelian properties of heterodimeric fibrinogen molecules in a heterozygotic dysfibrinogenemia, "fibrinogen Amarillo," using gprphoresis to differentiate semifibrin molecules from fibrinogen and fibrin.

H. Lill, G. Smejkal, J. Shainoff, 2001, Thrombosis research.

A rapid method for the purification of monomeric and/or dimeric phospholipases A2 in crotalid snake venoms.

J. Maraganore, W. Welches, D. Felsher, 1985, Toxicon : official journal of the International Society on Toxinology.