Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene by Capitani, G, Hohenester, E, Feng, L, Storici, P, Kirsch, J.F, Jansonius, J.N

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Is Aspartate 52 Essential for Catalysis by Chicken Egg White Lysozyme? The Role of Natural Substrate-Assisted Hydrolysis by Matsumura, Ichiro, Kirsch, Jack F

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Kinetic and Spectroscopic Investigations of Wild-Type and Mutant Forms of Apple 1-Aminocyclopropane-1-carboxylate Synthase by Li, Yishan, Feng, Liang, Kirsch, Jack F.

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Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms by White, M.F. (University of California, Berkeley, CA.), Vasquez, J, Yang, S.F, Kirsch, J.F

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Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis by Cronin, Ciaran N., Kirsch, Jack F.

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High-Resolution Mapping of the HyHEL-10 Epitope of Chicken Lysozyme by Site-Directed Mutagenesis by Lauren N. W. Kam-Morgan, Smith-Gill, Sandra J., Taylor, Marc G., Zhang, Lei, Wilson, Allan C., Kirsch, Jack F.

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Synergistic Contributions of Asparagine 46 and Aspartate 52 to the Catalytic Mechanism of Chicken Egg White Lysozyme by Matsumura, Ichiro, Kirsch, Jack F

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A Rapid Method for Determination of Endoproteinase Substrate Specificity: Specificity of the 3C Proteinase from Hepatitis A Virus by Petithory, J R, Masiarz, F R, Kirsch, J F, Santi, D V, Malcolm, B A

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Kinetic isotope effect studies on aspartate aminotransferase: evidence for a concerted 1,3 prototropic shift mechanism for the cytoplasmic isozyme and L-aspartate and dichotomy in... by Julin, Douglas A, Kirsch, Jack F

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Accumulation of the Quinonoid Intermediate in the Reaction Catalyzed by Aspartate Aminotransferase with Cysteine Sulfinic Acid by Furumo, N.C., Kirsch, J.F.

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The K258R mutant of aspartate aminotransferase stabilizes the quinonoid intermediate by TONEY, M. D, KIRSCH, J. F

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Estimation of free energy barriers in the cytoplasmic and mitochondrial aspartate aminotransferase reactions probed by hydrogen-exchange kinetics of C alpha-labeled amino acids wit... by Julin, D A, Wiesinger, H, Toney, M D, Kirsch, J F

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Aspartate aminotransferase catalyzed oxygen exchange with solvent from oxygen-18-enriched .alpha.-ketoglutarate: evidence for slow exchange of enzyme-bound water by McLeish, Michael J, Julin, Douglas A, Kirsch, Jack F

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Absence of carbonyl oxygen exchange concurrent with the alkaline hydrolysis of substituted methyl benzoates by Shain, Sydney A, Kirsch, Jack F

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The Activation of Papain and the Inhibition of the Active Enzyme by Carbonyl Reagents by Klein, I B, Kirsch, J F

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Amino acid incorporation in vitro by ribonucleoprotein particles detached from guinea pig liver microsomes by KIRSCH, J F, SIEKEVITZ, P, PALADE, G E

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Assessment of individual tumor buds using keratin immunohistochemistry: moderate interobserver agreement suggests a role for machine learning by Bokhorst, J. M., Blank, A., Lugli, A., Zlobec, I., Dawson, H., Vieth, M., Rijstenberg, L. L., Brockmoeller, S., Urbanowicz, M., Flejou, J. F., Kirsch, R., Ciompi, F., van der Laak, J. A. W. M., Nagtegaal, I. D.

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Correction to: Assessment of individual tumor buds using keratin immunohistochemistry: moderate interobserver agreement suggests a role for machine learning by Bokhorst, J. M., Blank, A., Lugli, A., Zlobec, I., Dawson, H., Vieth, M., Rijstenberg, L. L., Brockmoeller, S., Urbanowicz, M., Flejou, J. F., Kirsch, R., Ciompi, F., van der Laak, J. A. W. M., Nagtegaal, I. D.

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The muon system of the Run II DØ detector by Abazov, V.M., Alkhazov, G., Baldin, B., Banerjee, S., Bardon, O., Bartlett, J.F., Baturitsky, M.A., Beutel, D., Bezzubov, V.A., Bodyagin, V., Cease, H., Chi, E., Denisov, D., Doulas, S., Dugad, S.R., Dvornikov, O.V., Dyshkant, A., Evdokimov, A., Evdokimov, V.N., Fitzpatrick, T., Gavrilov, V., Golovtsov, V., Gómez, B., Gornushkin, Yu.A., Green, D.R., Gupta, A., Gurzhiev, S.N., Haggerty, H., Hansen, S., Hazen, E., Hedin, D., Hoeneisen, B., Jayanti, R., Johns, K., Jouravlev, N., Kalinin, A.M., Kalmani, S.D., Kirsch, N., Komissarov, E.V., Korablev, V.M., Kravchuk, N.P., Kuchinsky, N.A., Kupco, A., Larwill, M., Lipaev, V.V., Lobodenko, A., Machado, E., Maity, M., Malyshev, V.L., Marcus, M., Marshall, T., Mayorov, A.A., Merekov, Y.P., Mikhailov, V.A., Mondal, N.K., Nagaraj, P., Negret, J.P., Neustroev, P., Nozdrin, A.A., Parua, N., Podstavkov, V.M., Polozov, P., Porokhovoi, S.Y., Rao, M.V.S., Reddy, L.V., Regan, T., Rotolo, C., Russakovich, N.A., Sabirov, B.M., Satyanarayana, B., Schukin, A.A., Shankar, H.C., Shishkin, A.A., Shpakov, D., Shupe, M., Simak, V., Sirotenko, V., Soustruznik, K., Stefanik, A., Steinberg, J., Stolin, V., Stoyanova, D.A., Stutte, L., Temple, J., Terentyev, N., Teterin, V.V., Tokmenin, V.V., Tompkins, D., Uvarov, L., Uvarov, S., Vasilyev, I.A., Vishwanath, P.R., Vorobyov, A., Willutzki, H., Wobisch, M., Wood, D.R., Yamada, R., Yatsunenko, Y.A., Zhao, T., Zieminska, D.

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Impact of the addition of sufentanil 5 μg or clonidine 75 μg on the minimum local analgesic concentration of ropivacaine for epidural analgesia in labour: a randomized comparison by Dewandre, P.Y, Kirsch, M, Bonhomme, V, Columb, M, Hans, P, Brichant, J.F

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