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Results:
1-23
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Results: 23
Authors:
Macol, CP
Tsuruta, H
Stec, B
Kantrowitz, ER
Citation: Cp. Macol et al., Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase, NAT ST BIOL, 8(5), 2001, pp. 423-426
Authors:
Kelley-Loughnane, N
Kantrowitz, ER
Citation: N. Kelley-loughnane et Er. Kantrowitz, Binding of AMP to two of the four subunits of pig kidney fructose-1,6-bisphosphatase induces the allosteric transition, PROTEINS, 44(3), 2001, pp. 255-261
Authors:
Kelley-Loughnane, N
Kantrowitz, ER
Citation: N. Kelley-loughnane et Er. Kantrowitz, AMP inhibition of pig kidney fructose-1,6-bisphosphatase, BBA-PROT ST, 1548(1), 2001, pp. 66-71
Authors:
McIninch, JK
Kantrowitz, ER
Citation: Jk. Mcininch et Er. Kantrowitz, Use of silicate sol-gels to trap the R and T quaternary conformational states of pig kidney fructose-1,6-bisphosphatase, BBA-PROT ST, 1547(2), 2001, pp. 320-328
Authors:
Sakash, JB
Williams, MK
Tsuruta, H
Kantrowitz, ER
Citation: Jb. Sakash et al., Domain bridging interactions - A necessary contribution to the function and structure of Escherichia coli aspartate transcarbamoylase, J BIOL CHEM, 276(28), 2001, pp. 26441-26447
Authors:
Holtz, KM
Stec, B
Myers, JK
Antonelli, SM
Widlanski, TS
Kantrowitz, ER
Citation: Km. Holtz et al., Alternate modes of binding in two crystal structures of alkaline phosphatase-inhibitor complexes, PROTEIN SCI, 9(5), 2000, pp. 907-915
Authors:
Sakash, JB
Tsen, A
Kantrowitz, ER
Citation: Jb. Sakash et al., The use of nucleotide analogs to evaluate the mechanism of the heterotropic response of Escherichia coli aspartate transcarbamoylase, PROTEIN SCI, 9(1), 2000, pp. 53-63
Authors:
Vitali, J
Vorobyova, T
Webster, G
Kantrowitz, ER
Citation: J. Vitali et al., Crystallization and structure determination of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase, ACT CRYST D, 56, 2000, pp. 1061-1063
Authors:
Hehir, MJ
Murphy, JE
Kantrowitz, ER
Citation: Mj. Hehir et al., Characterization of heterodimeric alkaline phosphatases from Escherichia coli: An investigation of intragenic complementation, J MOL BIOL, 304(4), 2000, pp. 645-656
Authors:
Stec, B
Holtz, KM
Kantrowitz, ER
Citation: B. Stec et al., A revised mechanism for the alkaline phosphatase reaction involving three metal ions, J MOL BIOL, 299(5), 2000, pp. 1303-1311
Authors:
Sakash, JB
Kantrowitz, ER
Citation: Jb. Sakash et Er. Kantrowitz, The contribution of individual interchain interactions to the stabilization of the T and R states of Escherichia coli aspartate transcarbamoylase, J BIOL CHEM, 275(37), 2000, pp. 28701-28707
Authors:
Hack, ES
Vorobyova, T
Sakash, JB
West, JM
Macol, CP
Herve, G
Williams, MK
Kantrowitz, ER
Citation: Es. Hack et al., Characterization of the aspartate transcarbamoylase from Methanococcus jannaschii, J BIOL CHEM, 275(21), 2000, pp. 15820-15827
Authors:
Sakash, JB
Chan, RS
Tsuruta, H
Kantrowitz, ER
Citation: Jb. Sakash et al., Three of the six possible intersubunit stabilizing interactions involving Glu-239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase, J BIOL CHEM, 275(2), 2000, pp. 752-758
Authors:
Holtz, KM
Catrina, IE
Hengge, AC
Kantrowitz, ER
Citation: Km. Holtz et al., Mutation of Arg-166 of alkaline phosphatase alters the thio effect but notthe transition state for phosphoryl transfer. Implications for the interpretation of thio effects in reactions of phosphatases, BIOCHEM, 39(31), 2000, pp. 9451-9458
Authors:
Jin, L
Stec, B
Kantrowitz, ER
Citation: L. Jin et al., A cis-proline to alanine mutant of E. coli aspartate transcarbamoylase: Kinetic studies and three-dimensional crystal structures, BIOCHEM, 39(27), 2000, pp. 8058-8066
Authors:
Macol, C
Dutta, M
Stec, B
Tsuruta, H
Kantrowitz, ER
Citation: C. Macol et al., The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity, PROTEIN SCI, 8(6), 1999, pp. 1305-1313
Authors:
Martin, DC
Pastra-Landis, SC
Kantrowitz, ER
Citation: Dc. Martin et al., Amino acid substitutions at the subunit interface of dimeric Escherichia coli alkaline phosphatase cause reduced structural stability, PROTEIN SCI, 8(5), 1999, pp. 1152-1159
Authors:
Jin, L
Stec, B
Lipscomb, WN
Kantrowitz, ER
Citation: L. Jin et al., Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 angstrom, PROTEINS, 37(4), 1999, pp. 729-742
Authors:
Strater, N
Sun, L
Kantrowitz, ER
Lipscomb, WN
Citation: N. Strater et al., A bicarbonate ion as a general base in the mechanism of peptide hydrolysisby dizinc leucine aminopeptidase, P NAS US, 96(20), 1999, pp. 11151-11155
Authors:
Holtz, KM
Stec, B
Kantrowitz, ER
Citation: Km. Holtz et al., A model of the transition state in the alkaline phosphatase reaction, J BIOL CHEM, 274(13), 1999, pp. 8351-8354
Authors:
Holtz, KM
Kantrowitz, ER
Citation: Km. Holtz et Er. Kantrowitz, The mechanism of the alkaline phosphatase reaction: insights from NMR, crystallography and site-specific mutagenesis, FEBS LETTER, 462(1-2), 1999, pp. 7-11
Authors:
Sun, L
Martin, DC
Kantrowitz, ER
Citation: L. Sun et al., Rate-determining step of Escherichia coli alkaline phosphatase altered by the removal of a positive charge at the active center, BIOCHEM, 38(9), 1999, pp. 2842-2848
Authors:
Williams, MK
Kantrowitz, ER
Citation: Mk. Williams et Er. Kantrowitz, Threonine 82 in the regulatory chain is important for nucleotide affinity and for the allosteric stabilization of Escherichia coli aspartate transcarbamoylase, BBA-PROT ST, 1429(1), 1998, pp. 249-258
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