(en) Janet L. Donahue, Jennifer L. Bownas, Walter G. Niehaus et Timothy J. Larson, « Purification and Characterization of glpX-Encoded Fructose 1,6-Bisphosphatase, a New Enzyme of the Glycerol 3-Phosphate Regulon of Escherichia coli », Journal of Bacteriology, vol. 182, no 19, , p. 5624-5627 (PMID10986273, DOI10.1128/JB.182.19.5624-5627.2000, lire en ligne)
(en) Yasutaro Fujita, Ken-Ichi Yoshida, Yasuhiko Miwa, Nobuo Yanai, Eishi Nagakawa et Yasuhiro Kasahara, « Identification and Expression of the Bacillus subtilis Fructose-1,6-Bisphosphatase Gene (fbp) », Journal of Bacteriology, vol. 180, no 16, , p. 4309-4313 (PMID9696785, lire en ligne)
cell.com
(en) Hiroshi Nishimasu, Shinya Fushinobu, Hirofumi Shoun et Takayoshi Wakagi, « The First Crystal Structure of the Novel Class of Fructose-1,6-Bisphosphatase Present in Thermophilic Archaea », Structure, vol. 12, no 6, , p. 949-959 (PMID15274916, DOI10.1016/j.str.2004.03.026, lire en ligne)
degruyter.com
(en) Alina Kępka, Sławomir Dariusz Szajda, Anna Stypułkowska, Napoleon Waszkiewicz, Anna Jankowska, Sylwia Chojnowska et Krzysztof Zwierz, « Urinary fructose-1,6-bisphosphatase activity as a marker of the damage to the renal proximal tubules in children with idiopathic nephrotic syndrome », Clinical Chemistry and Laboratory Medicine (CCLM), vol. 46, no 6, , p. 831-835 (PMID18601606, DOI10.1515/CCLM.2008.171, lire en ligne)
doi.org
dx.doi.org
(en) Frank Marcus et Peter B. Harrsch, « Amino acid sequence of spinach chloroplast fructose-1,6-bisphosphatase », Archives of Biochemistry and Biophysics, vol. 279, no 1, , p. 151-157 (PMID2159755, DOI10.1016/0003-9861(90)90475-E, lire en ligne)
(en) Frank Marcus, Brigitte Gontero, Peter B. Harrsch et Judith Rittenhouse, « Amino acid sequence homology among fructose-1,6-bisphosphatases », Biochemical and Biophysical Research Communications, vol. 135, no 2, , p. 374-381 (PMID3008716, DOI10.1016/0006-291X(86)90005-7, lire en ligne)
(en) Alina Kępka, Sławomir Dariusz Szajda, Anna Stypułkowska, Napoleon Waszkiewicz, Anna Jankowska, Sylwia Chojnowska et Krzysztof Zwierz, « Urinary fructose-1,6-bisphosphatase activity as a marker of the damage to the renal proximal tubules in children with idiopathic nephrotic syndrome », Clinical Chemistry and Laboratory Medicine (CCLM), vol. 46, no 6, , p. 831-835 (PMID18601606, DOI10.1515/CCLM.2008.171, lire en ligne)
(en) Y.P. Zhang, J.Y. Liang et W.N. Lipscomb, « Structural Similarities between Fructose-1,6-bisphosphatase and Inositol Monophosphatase », Biochemical and Biophysical Research Communications, vol. 190, no 3, , p. 1080-1083 (PMID8382485, DOI10.1006/bbrc.1993.1159, lire en ligne)
(en) J. D. York, J. W. Ponder et P. W. Majerus, « Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure », Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no 11, , p. 5149-5153 (PMID7761465, DOI10.1073/pnas.92.11.5149, lire en ligne)
(en) Janet L. Donahue, Jennifer L. Bownas, Walter G. Niehaus et Timothy J. Larson, « Purification and Characterization of glpX-Encoded Fructose 1,6-Bisphosphatase, a New Enzyme of the Glycerol 3-Phosphate Regulon of Escherichia coli », Journal of Bacteriology, vol. 182, no 19, , p. 5624-5627 (PMID10986273, DOI10.1128/JB.182.19.5624-5627.2000, lire en ligne)
(en) Boguslaw Stec, Hongying Yang, Kenneth A. Johnson, Liangjing Chen et Mary F. Roberts, « MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase », Nature Structural & Molecular Biology, vol. 7, , p. 1046-1050 (PMID11062561, DOI10.1038/80968, lire en ligne)
(en) Naeem Rashid, Hiroyuki Imanaka, Tamotsu Kanai, Toshiaki Fukui, Haruyuki Atomi et Tadayuki Imanaka, « A Novel Candidate for the True Fructose-1,6-bisphosphatase in Archaea », Journal of Biological Chemistry, vol. 277, no 34, , p. 30649-30655 (PMID12065581, DOI10.1074/jbc.M202868200, lire en ligne)
(en) Hiroshi Nishimasu, Shinya Fushinobu, Hirofumi Shoun et Takayoshi Wakagi, « The First Crystal Structure of the Novel Class of Fructose-1,6-Bisphosphatase Present in Thermophilic Archaea », Structure, vol. 12, no 6, , p. 949-959 (PMID15274916, DOI10.1016/j.str.2004.03.026, lire en ligne)
jbc.org
(en) Naeem Rashid, Hiroyuki Imanaka, Tamotsu Kanai, Toshiaki Fukui, Haruyuki Atomi et Tadayuki Imanaka, « A Novel Candidate for the True Fructose-1,6-bisphosphatase in Archaea », Journal of Biological Chemistry, vol. 277, no 34, , p. 30649-30655 (PMID12065581, DOI10.1074/jbc.M202868200, lire en ligne)
(en) Y. Fujita et E. Freese, « Purification and properties of fructose-1,6-bisphosphatase of Bacillus subtilis », Journal of Biological Chemistry, vol. 254, no 12, , p. 5340-5349 (PMID221467, lire en ligne)
nature.com
(en) Boguslaw Stec, Hongying Yang, Kenneth A. Johnson, Liangjing Chen et Mary F. Roberts, « MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase », Nature Structural & Molecular Biology, vol. 7, , p. 1046-1050 (PMID11062561, DOI10.1038/80968, lire en ligne)
nih.gov
ncbi.nlm.nih.gov
(en) Frank Marcus et Peter B. Harrsch, « Amino acid sequence of spinach chloroplast fructose-1,6-bisphosphatase », Archives of Biochemistry and Biophysics, vol. 279, no 1, , p. 151-157 (PMID2159755, DOI10.1016/0003-9861(90)90475-E, lire en ligne)
(en) Frank Marcus, Brigitte Gontero, Peter B. Harrsch et Judith Rittenhouse, « Amino acid sequence homology among fructose-1,6-bisphosphatases », Biochemical and Biophysical Research Communications, vol. 135, no 2, , p. 374-381 (PMID3008716, DOI10.1016/0006-291X(86)90005-7, lire en ligne)
(en) Alina Kępka, Sławomir Dariusz Szajda, Anna Stypułkowska, Napoleon Waszkiewicz, Anna Jankowska, Sylwia Chojnowska et Krzysztof Zwierz, « Urinary fructose-1,6-bisphosphatase activity as a marker of the damage to the renal proximal tubules in children with idiopathic nephrotic syndrome », Clinical Chemistry and Laboratory Medicine (CCLM), vol. 46, no 6, , p. 831-835 (PMID18601606, DOI10.1515/CCLM.2008.171, lire en ligne)
(en) Y.P. Zhang, J.Y. Liang et W.N. Lipscomb, « Structural Similarities between Fructose-1,6-bisphosphatase and Inositol Monophosphatase », Biochemical and Biophysical Research Communications, vol. 190, no 3, , p. 1080-1083 (PMID8382485, DOI10.1006/bbrc.1993.1159, lire en ligne)
(en) J. D. York, J. W. Ponder et P. W. Majerus, « Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure », Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no 11, , p. 5149-5153 (PMID7761465, DOI10.1073/pnas.92.11.5149, lire en ligne)
(en) Janet L. Donahue, Jennifer L. Bownas, Walter G. Niehaus et Timothy J. Larson, « Purification and Characterization of glpX-Encoded Fructose 1,6-Bisphosphatase, a New Enzyme of the Glycerol 3-Phosphate Regulon of Escherichia coli », Journal of Bacteriology, vol. 182, no 19, , p. 5624-5627 (PMID10986273, DOI10.1128/JB.182.19.5624-5627.2000, lire en ligne)
(en) Boguslaw Stec, Hongying Yang, Kenneth A. Johnson, Liangjing Chen et Mary F. Roberts, « MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase », Nature Structural & Molecular Biology, vol. 7, , p. 1046-1050 (PMID11062561, DOI10.1038/80968, lire en ligne)
(en) Naeem Rashid, Hiroyuki Imanaka, Tamotsu Kanai, Toshiaki Fukui, Haruyuki Atomi et Tadayuki Imanaka, « A Novel Candidate for the True Fructose-1,6-bisphosphatase in Archaea », Journal of Biological Chemistry, vol. 277, no 34, , p. 30649-30655 (PMID12065581, DOI10.1074/jbc.M202868200, lire en ligne)
(en) Hiroshi Nishimasu, Shinya Fushinobu, Hirofumi Shoun et Takayoshi Wakagi, « The First Crystal Structure of the Novel Class of Fructose-1,6-Bisphosphatase Present in Thermophilic Archaea », Structure, vol. 12, no 6, , p. 949-959 (PMID15274916, DOI10.1016/j.str.2004.03.026, lire en ligne)
(en) Y. Fujita et E. Freese, « Purification and properties of fructose-1,6-bisphosphatase of Bacillus subtilis », Journal of Biological Chemistry, vol. 254, no 12, , p. 5340-5349 (PMID221467, lire en ligne)
(en) Yasutaro Fujita, Ken-Ichi Yoshida, Yasuhiko Miwa, Nobuo Yanai, Eishi Nagakawa et Yasuhiro Kasahara, « Identification and Expression of the Bacillus subtilis Fructose-1,6-Bisphosphatase Gene (fbp) », Journal of Bacteriology, vol. 180, no 16, , p. 4309-4313 (PMID9696785, lire en ligne)
pnas.org
(en) J. D. York, J. W. Ponder et P. W. Majerus, « Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure », Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no 11, , p. 5149-5153 (PMID7761465, DOI10.1073/pnas.92.11.5149, lire en ligne)
sciencedirect.com
(en) Frank Marcus et Peter B. Harrsch, « Amino acid sequence of spinach chloroplast fructose-1,6-bisphosphatase », Archives of Biochemistry and Biophysics, vol. 279, no 1, , p. 151-157 (PMID2159755, DOI10.1016/0003-9861(90)90475-E, lire en ligne)
(en) Frank Marcus, Brigitte Gontero, Peter B. Harrsch et Judith Rittenhouse, « Amino acid sequence homology among fructose-1,6-bisphosphatases », Biochemical and Biophysical Research Communications, vol. 135, no 2, , p. 374-381 (PMID3008716, DOI10.1016/0006-291X(86)90005-7, lire en ligne)
(en) Y.P. Zhang, J.Y. Liang et W.N. Lipscomb, « Structural Similarities between Fructose-1,6-bisphosphatase and Inositol Monophosphatase », Biochemical and Biophysical Research Communications, vol. 190, no 3, , p. 1080-1083 (PMID8382485, DOI10.1006/bbrc.1993.1159, lire en ligne)