Search Results - "Nikaido, K"

Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand by Oh, B.H., Pandit, J., Kang, C.H., Nikaido, K., Gokcen, S., Ames, G.F., Kim, S.H.

“…Many proteins exhibit a large-scale movement of rigid globular domains. Among these, bacterial periplasmic binding proteins involved in substrate transport, or…”
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Identification and characterization of porins in Pseudomonas aeruginosa by Nikaido, H, Nikaido, K, Harayama, S

“…Earlier studies have shown that the major porin species in Pseudomonas aeruginosa outer membrane is protein F (OprF), which produces channels wider than those…”
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The bacterial periplasmic histidine-binding protein. structure/function analysis of the ligand-binding site and comparison with related proteins by BYUNG-HA OH, CHUL-HEE KANG, DE BONDT, H, SUNG-HOU KIM, NIKAIDO, K, JOSHI, A. K, AMES, G. F.-L

“…Bacterial periplasmic binding proteins are initial receptors in the process of active transport across cell membranes and/or chemotaxis. Among them, the…”
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Utilization of snow cooling for preservation of asparagus spears by Nikaido, K., Jishi, T., Maeda, T., Suzuki, T., Yokota, T., Araki, H.

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The histidine-binding protein undergoes conformational changes in the absence of ligand as analyzed with conformation-specific monoclonal antibodies by Wolf, A, Shaw, E W, Nikaido, K, Ames, G F

“…The periplasmic histidine-binding protein, HisJ, and the lysine-, arginine-, ornithine-binding protein (LAO) are receptors for histidine transport via the…”
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Purification and characterization of the periplasmic lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium by NIKAIDO, K, FERRO-LUZZI AMES, G

“…The lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium has been purified to homogeneity and characterized. The dissociation…”
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Reconstitution of periplasmic transport in inside-out membrane vesicles. Energization by ATP by Ames, G F, Nikaido, K, Groarke, J, Petithory, J

“…The periplasmic histidine permease of Salmonella typhimurium has been reconstituted in inside-out vesicles (IOV) of Escherichia coli by disrupting the cells…”
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Formaldehyde and photoactivatable cross-linking of the periplasmic binding protein to a membrane component of the histidine transport system of Salmonella typhimurium by Prossnitz, E, Nikaido, K, Ulbrich, S J, Ames, G F

“…The histidine permease of Salmonella typhimurium consists of four protein components, one located in the periplasm and three in the cytoplasmic membrane…”
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Nitrogen regulation in Salmonella typhimurium. Identification of an ntrC protein‐binding site and definition of a consensus binding sequence by Ferro‐Luzzi Ames, G., Nikaido, K.

“…We have investigated the DNA‐binding ability of a nitrogen regulatory protein, the product of the ntrC gene, to several nitrogen‐regulated promoters in…”
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Complete nucleotide sequence and identification of membrane components of the histidine transport operon of S. typhimurium by Higgins, C. F, Haag, P. D, Nikaido, K, Ardeshir, F, Garcia, G, Ames, G. Ferro-Luzzi

“…The nucleotide sequence of the entire histidine transport operon from Salmonella typhimurium has been determined and is shown to consist of four genes, hisJ,…”
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Crystal structure of the ATP-binding subunit of an ABC transporter by Kim, Sung-Hou, Hung, Li-Wei, Wang, Iris Xiaoyan, Nikaido, Kishiko, Liu, Pei-Qi, Ames, Giovanna Ferro-Luzzi

“…ABC transporters (also known as traffic ATPases) form a large family of proteins responsible for the translocation of a variety ofcompounds across membranes of…”
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Identification of a Membrane Protein as a Histidine Transport Component in Salmonella typhimurium by Ames, Giovanna Ferro-Luzzi, Nikaido, Kishiko

“…A component of high-affinity histidine transport in Salmonella typhimurium has been identified. It is a basic (pI about 9.0) membrane-bound protein, the P…”
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Nitrogen regulation in Salmonella typhimurium. Identification of an ntrC protein-binding site and definition of a consensus binding sequence by AMES, G. F.-L, NIKAIDO, K

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One Intact ATP-binding Subunit Is Sufficient to Support ATP Hydrolysis and Translocation in an ABC Transporter, the Histidine Permease by Nikaido, Kishiko, Ames, Giovanna Ferro-Luzzi

“…The membrane-bound complex of the Salmonella typhimurium histidine permease, a member of the ABC transporters (or traffic ATPases) superfamily, is composed of…”
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Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubility, dimerization, and ATPase activity by Nikaido, K, Liu, P Q, Ames, G F

“…The nucleotide-binding subunit, HisP, of the histidine permease, a traffic ATPase (ABC transporter), has been purified as a soluble protein and characterized…”
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GENETIC VARIATION IN PROTEINS: COMPARISON OF ONE-DIMENSIONAL AND TWO-DIMENSIONAL GEL ELECTROPHORESIS by McLellan, Tracy, Ames, Giovanna Ferro-Luzzi, Nikaido, Kishiko

“…Two proteins with known characteristics on one-dimensional gels were studied by two-dimensional electrophoresis to compare the sensitivities of the two methods…”
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Glucosylation of lipopolysaccharide in Salmonella: biosynthesis nof O antigen factor n12 2 . II. Structure of the lipid intermediate by Nikaido, K, Nikaido, H

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Fine-structure map of the histidine transport genes in Salmonella typhimurium by Ames, G F, Noel, K D, Taber, H, Spudich, E N, Nikaido, K, Afong, J

“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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Protein Globularization During Folding. A Study by Synchrotron Small-angle X-ray Scattering by Semisotnov, Gennady V., Kihara, Hiroshi, Kotova, Nina V., Kimura, Kazumoto, Amemiya, Yoshiyuki, Wakabayashi, Katsuzo, Serdyuk, Igor N., Timchenko, Alexander A., Chiba, Kaori, Nikaido, Kiyokazu, Ikura, Teikichi, Kuwajima, Kunihiro

“…Various conformational states of polypeptide chains were investigated by synchrotron small-angle X-ray scattering (SAXS). SAXS patterns of proteins and model…”
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The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state by Okazaki, Akira, Ikura, Teikichi, Nikaido, Kiyokazu, Kuwajima, Kunihiro

“…We investigate here the interaction between GroEL and two kinds of non-native alpha-lactalbumin. alpha-Lactalbumin is a Ca(2+)-binding protein which assumes a…”
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