Exploring the complex information processes underlying plant behavior von Novoplansky, A., Souza, G.M., Brenner, E.D., Bhatla, S.C., Van Volkenburgh, E.

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Plant neurobiology: an integrated view of plant signaling von Brenner, Eric D., Stahlberg, Rainer, Mancuso, Stefano, Vivanco, Jorge, Baluška, František, Van Volkenburgh, Elizabeth

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Identification of genes whose transcripts accumulate rapidly in tomato after root-knot nematode infection von LAMBERT, K.N, FERRIE, B.J, NOMBELA, G, BRENNER, E.D, WILLIAMSON, V.M

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Characterization of LeMir, a root-knot nematode-induced gene in tomato with an encoded product secreted from the root von Brenner, E.D. (University of California, Davis, CA.), Lambert, K.N, Kaloshian, I, Williamson, V.M

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A Quantitative Test for Copper Using Bicinchoninic Acid von Brenner, A.J., Harris, E.D.

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Substoichiometric concentrations of cytochalasin D inhibit actin polymerization. Additional evidence for an F-actin treadmill von Brenner, S L, Korn, E D

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Spectrin/actin complex isolated from sheep erythrocytes accelerates actin polymerization by simple nucleation. Evidence for oligomeric actin in the erythrocyte cytoskeleton von Brenner, S L, Korn, E D

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Volume 226, Number 1 (1995), in the article "A Quantitative Test for Copper Using Bicinchoninic Acid," by Andrew J. Brenner and Edward D. Harris, pages 80–84 von Brenner, A.J., Harris, E.D.

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Identical short peptide sequences in unrelated proteins can have different conformations: a testing ground for theories of immune recognition von Wilson, I.A, Haft, D.Hj, Getzoff, E.D, Tainer, J.A, Lerner, R.A, Brenner, S

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The effects of cytochalasins on actin polymerization and actin ATPase provide insights into the mechanism of polymerization von Brenner, S L, Korn, E D

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Spectrin-actin interaction. Phosphorylated and dephosphorylated spectrin tetramer cross-link F-actin von Brenner, S L, Korn, E D

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Stimulation of actin ATPase activity by cytochalasins provides evidence for a new species of monomeric actin von Brenner, S L, Korn, E D

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Spectrin/actin complex isolated from sheep erythrocytes accelerates actin polymerization by simple nucleation. Evidence for oligomeric actin in the erthrocyte cytoskeleton von Brenner, S.L, Korn, E.D

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