About: Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase

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scientific article published on 02 May 2006

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в травні 2006 (uk) artículu científicu espublizáu en mayu de 2006 (ast) scientific article published on 02 May 2006 (en)
publication date	wds:Q83275780-492FA8E8-8A65-4A1E-8790-F35A9F2DFD94
publication date	2006-05-02 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q83275780-5F1C1A4B-0FD3-4412-8428-D3DB1A67124E
language of work or name	English
cites work	wds:Q83275780-01774CEC-443C-4933-9C04-8ADAC488D8F2 wds:Q83275780-13CE910F-B438-4111-A5CF-DA2480C68A26 wds:Q83275780-252839CA-3E63-4C68-97F9-057A9E8A3113 wds:Q83275780-274C2FA5-2E8E-400D-9700-182A17B425C6 wds:Q83275780-2C263552-18F4-4089-A248-7661166B32E8 wds:Q83275780-2F22B9C3-79FF-4D5F-891A-053F36042B5B wds:Q83275780-2F3976A8-D0A6-49E3-B7B5-F329F8F248B5 wds:Q83275780-3FF2E5DE-3A9C-4943-A15C-38339E53F1F3 wds:Q83275780-45FD542F-8518-452C-8DA8-EE3CA078D952 wds:Q83275780-49538665-0FB5-4D83-9CAE-70426FD6C34E wds:Q83275780-4F568C9D-536B-4D21-B11A-EE67F56E0513 wds:Q83275780-50F90708-73EE-42C9-846C-B0E9980F60FE wds:Q83275780-6B3B4742-0CC1-4CC2-A012-A6FC089517AA wds:Q83275780-7B636223-1494-4DE6-9FCD-D43D274D615E wds:Q83275780-82054703-A067-4BA8-A641-783AC0C00217 wds:Q83275780-83FA2ABD-A9E9-40AA-B8BE-7991968FFAFE wds:Q83275780-843FA214-315A-4F9E-85A5-9057DD11472E wds:Q83275780-845A454F-9D2F-42E5-9725-474E84FDEB31 wds:Q83275780-86D97968-0754-4F0F-B65C-36873DC08593 wds:Q83275780-8C4B4ACE-4E03-494E-A3B0-92F7E057A40E wds:Q83275780-931000FE-F4B2-4802-9737-4DFFB219FFE9 wds:Q83275780-9FDB0569-5D13-4652-AC0B-478A404E80BA wds:Q83275780-AB0AF00E-566C-4F88-906F-8B7674BBB740 wds:Q83275780-B16E1226-3B2A-4E19-974B-EAF0674AA286 wds:Q83275780-B5539562-E078-4498-8448-8850462D30BC wds:Q83275780-BC760B40-BC41-475B-8A7B-1DF573E65B13 wds:Q83275780-C13F5501-D65B-41F2-B1FD-3092849FAE29 wds:Q83275780-C343D5BF-1E07-48E1-BEE8-6487E97636D8 wds:Q83275780-C739593C-7100-4F4B-B72B-89B68A491297 wds:Q83275780-C88E6D85-63E1-4DC8-BF59-436193DF35AC wds:Q83275780-CB5FDCE2-8A6F-4D01-BE05-FD5821E3451C wds:Q83275780-CE5CB2CD-528D-4135-B0FD-C88708D5A78C wds:Q83275780-D1FB257C-BDE5-4061-9D38-E9A470870B94 wds:Q83275780-D9E260B3-83A1-44F5-8FA5-10C06753D621 wds:Q83275780-E38DB434-2BEF-4797-9EA0-C8F9374827A8 wds:Q83275780-E46C8CF1-E7CE-4505-8191-939443168D58 wds:Q83275780-F018A717-3399-4F64-B1EE-ACBFE6341D86 wds:Q83275780-F6763D39-EF14-4BAC-9772-9FA667F411DB
cites work	Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes The specific fructose diphosphatase of Escherichia coli: properties and partial purification Rapid and sensitive sequence comparison with FASTP and FASTA Purification and characterization of glpX-encoded fructose 1, 6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli The first crystal structure of the novel class of fructose-1,6-bisphosphatase present in thermophilic archaea. Fructose bisphosphatase from Escherichia coli. Purification and characterization Inhibition of Escherichia coli fructose-1,6-bisphosphatase by fructose 2,6-bisphosphate AMoRe: an automated package for molecular replacement Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 Anilinoquinazoline inhibitors of fructose 1,6-bisphosphatase bind at a novel allosteric site: synthesis, in vitro characterization, and X-ray crystallography Inhibition of Fructose-1,6-bisphosphatase by a New Class of Allosteric Effectors MB06322 (CS-917): A potent and selective inhibitor of fructose 1,6-bisphosphatase for controlling gluconeogenesis in type 2 diabetes. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures A solution for the best rotation to relate two sets of vectors Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase The CCP4 suite: programs for protein crystallography Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding The finer things in X-ray diffraction data collection Hormonal regulation of hepatic gluconeogenesis and glycolysis On the treatment of negative intensity observations Accurate bond and angle parameters for X-ray protein structure refinement Fructose-1, 6-bisphosphatase of an extreme thermophile Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium Crystal structure of spinach chloroplast fructose-1,6-bisphosphatase at 2.8 A resolution Univalent cation activation of fructose 1,6-diphosphatase. Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphatase Purification, kinetic studies, and homology model of Escherichia coli fructose-1,6-bisphosphatase. The N-terminal segment of recombinant porcine fructose-1,6-bisphosphatase participates in the allosteric regulation of catalysis Spontaneous subunit exchange in porcine liver fructose-1,6-bisphosphatase Hybrid tetramers of porcine liver fructose-1,6-bisphosphatase reveal multiple pathways of allosteric inhibition R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase Sequence of the Escherichia coli fructose-1,6-bisphosphatase gene Biochemical properties of mutant and wild-type fructose-1,6-bisphosphatases are consistent with the coupling of intra- and intersubunit conformational changes in the T- and R-state transition Binding of AMP to two of the four subunits of pig kidney fructose-1,6-bisphosphatase induces the allosteric transition
author name string	wds:Q83275780-970E90D9-BBE0-4F2C-8405-5E07900AB9F9 wds:Q83275780-E7EE2F9C-CCA6-44CD-9E4E-98B9A14BE0D5 wds:Q83275780-EF857752-B582-45E1-96FF-513756A56FB1
author name string	Richard B Honzatko Justin K Hines Herbert J Fromm
rdfs:label	Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase (en) Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase (nl)
skos:prefLabel	Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase (en) Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase (nl)
name	Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase (en) Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase (nl)
title	wds:Q83275780-14060AA3-F054-4E3E-81C8-E9B66C5AAF0E
title	Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase (en)
page(s)	wds:Q83275780-07527847-BB3E-4887-9B7A-4E96DBAB722A

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