J. P. Lee

发表

Studies on the biosynthesis of the alpha-glucosidase inhibitor acarbose: valienamine, a m-C7N unit not derived from the shikimate pathway.

J. M. Beale, H. Floss, P. Keller, 1987, Journal of antibiotics (Tokyo. 1968).

Isolation of Assimilatory- and Dissimilatory-Type Sulfite Reductases from Desulfovibrio vulgaris

H. D. Peck, J. Legall, J. P. Lee, 1973, Journal of bacteriology.

Isolation of a protein containing tightly bound 5-methoxybenzimidazolylcobamide (factor 3m) from Clostridium thermoaceticum.

L. Ljungdahl, J. Legall, J. P. Lee, 1973, Biochemistry.

Detection and characterization of a phospholactoyl-enzyme adduct in the reaction catalyzed by UDP-N-acetylglucosamine enolpyruvoyl transferase, MurZ.

E. Brown, C. Walsh, K. Anderson, 1994, Biochemistry.

Further studies on the biosynthesis of chlorothricin.

J. J. Lee, H. Zähner, H. Floss, 1986, The Journal of antibiotics.

Purification of the enzyme reducing bisulfite to trithionate from Desulfovibrio gigas and its identification as desulfoviridin.

H. D. Peck, J. P. Lee, H. D. Peck, 1971, Biochemical and biophysical research communications.

An iron tetrahydroporphyrin prosthetic group common to both assimilatory and dissimilatory sulfite reductases.

H. Kamin, H. D. Peck, J. Legall, 1973, Biochemical and biophysical research communications.

Isolation of a New Pigment, Desulforubidin, from Desulfovibrio desulfuricans (Norway Strain) and Its Role in Sulfite Reduction

H. D. Peck, J. Legall, J. P. Lee, 1973, Journal of bacteriology.

1H NMR of A beta amyloid peptide congeners in water solution. Conformational changes correlate with plaque competence.

J R Ghilardi, P W Mantyh, P. Mantyh, 1995, Biochemistry.

Evidence for the involvement of non-heme iron in the active site of hydrogenase from Desulfovibrio vulgaris.

E. Spilker, H. D. Peck, J. Legall, 1971, Biochimica et biophysica acta.

Reactivity of Desulfovibrio gigas hydrogenase toward artificial and natural electron donors or acceptors.

G. R. Bell, H. D. Peck, J. P. Lee, 1978, Biochimie.