The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Structural Basis for Allosteric Regulation of the Monomeric Allosteric Enzyme Human Glucokinase
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Cites
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
The CCP4 suite: programs for protein crystallography
Collaborative Computational Project, N. 4. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,270
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,715
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,085
Jones, T. A., Zou, J. Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,648
On the nature of allosteric transitions: A plausible model
Monod, J., Wyman, J., & Changeux, J.-P. (1965) · Journal of Molecular Biology · doi:10.1016/s0022-2836(65)80285-6 · Cited by 8,825
AMoRe: an automated package for molecular replacement
Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,953
Raster3D Version 2.0. A program for photorealistic molecular graphics
Merritt, E. A., & Murphy, M. E. P. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994006396 · Cited by 2,504
Structural Mechanisms for Domain Movements in Proteins
Gerstein, M., Lesk, A. M., & Chothia, C. (1994) · Biochemistry · doi:10.1021/bi00188a001 · Cited by 744
Nonsense mutation in the glucokinase gene causes early-onset non-insulin-dependent diabetes mellitus
Vionnet, N., Stoffel, M., Takeda, J., Yasuda, K., Bell, G. I., Zouali, H., Lesage, S., Velho, G., Iris, F., Passa, P., et al. (1992) · Nature · doi:10.1038/356721a0 · Cited by 604
Familial Hyperinsulinism Caused by an Activating Glucokinase Mutation
Glaser, B., Kesavan, P., Heyman, M., Davis, E., Cuesta, A., Buchs, A., Stanley, C. A., Thornton, P. S., Permutt, M. A., Matschinsky, F. M., et al. (1998) · New England Journal of Medicine · doi:10.1056/nejm199801223380404 · Cited by 564
Allosteric Activators of Glucokinase: Potential Role in Diabetes Therapy
Grimsby, J., Sarabu, R., Corbett, W. L., Haynes, N.-E., Bizzarro, F. T., Coffey, J. W., Guertin, K. R., Hilliard, D. W., Kester, R. F., Mahaney, P. E., et al. (2003) · Science · doi:10.1126/science.1084073 · Cited by 526
Regulation of Pancreatic β-Cell Glucokinase
Matschinsky, F. M. (2002) · Diabetes · doi:10.2337/diabetes.51.2007.s394 · Cited by 345
Matschinsky, F. M., Glaser, B., & Magnuson, M. A. (1998) · Diabetes · doi:10.2337/diabetes.47.3.307 · Cited by 333
Multiple forms of hexokinase in the rat: tissue distribution, age dependency, and properties.
Katzen, H. M., & Schimke, R. T. (1965) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.54.4.1218 · Cited by 309
Glucose-induced conformational change in yeast hexokinase.
Bennett, W. S., & Steitz, T. A. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.10.4848 · Cited by 306
The allosteric transition of glycogen phosphorylase
Barford, D., & Johnson, L. N. (1989) · Nature · doi:10.1038/340609a0 · Cited by 294
Structural basis of the allosteric behaviour of phosphofructokinase
Schirmer, T., & Evans, P. R. (1990) · Nature · doi:10.1038/343140a0 · Cited by 271
Short‐term control of glucokinase activity: role of a regulatory protein
Van Schaftingen, E., Detheux, M., & Da Cunha, M. V. (1994) · The FASEB Journal · doi:10.1096/fasebj.8.6.8168691 · Cited by 232
The Second Activating Glucokinase Mutation (A456V)
Christesen, H. B. T., Jacobsen, B. B., Odili, S., Buettger, C., Cuesta-Munoz, A., Hansen, T., Brusgaard, K., Massa, O., Magnuson, M. A., Shiota, C., et al. (2002) · Diabetes · doi:10.2337/diabetes.51.4.1240 · Cited by 171
Davis, E. A., Cuesta-Muñoz, A., Raoul, M., Buettger, C., Sweet, I., Moates, M., Magnuson, M. A., & Matschinsky, F. M. (1999) · Diabetologia · doi:10.1007/s001250051289 · Cited by 164
Storer, A. C., & Cornish-Bowden, A. J. (1976) · Biochemical Journal · doi:10.1042/bj1590007 · Cited by 145
Aleshin, A. E., Zeng, C., Bourenkov, G. P., Bartunik, H. D., Fromm, H. J., & Honzatko, R. B. (1998) · Structure · doi:10.1016/s0969-2126(98)00006-9 · Cited by 140
Kinetic evidence for a ‘mnemonical’ mechanism for rat liver glucokinase
Storer, A. C., & Cornish-Bowden, A. J. (1977) · Biochemical Journal · doi:10.1042/bj1650061 · Cited by 135
Shiota, C., Coffey, J., Grimsby, J. S., Grippo, J. F., & Magnuson, M. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37125 · Cited by 132
Aleshin, A. E., Kirby, C. A., Liu, X., Bourenkov, G. P., Bartunik, H. D., Fromm, H. J., & Honzatko, R. B. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3494 · Cited by 113
The Role of the Regulatory Protein of Glucokinase in the Glucose Sensory Mechanism of the Hepatocyte
de la Iglesia, N., Mukhtar, M. H., Seoane, J., Guinovart, J. J., & Agius, L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.14.10597 · Cited by 110
Aleshin, A. E., Zeng, C., Bartunik, H. D., Fromm, H. J., & Honzatko, R. B. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2017 · Cited by 100
Iwata, S., Kamata, K., Yoshida, S., Minowa, T., & Ohta, T. (1994) · Nature Structural Biology · doi:10.1038/nsb0394-176 · Cited by 96
Self-citationDemonstration of a slow conformational change in liver glucokinase by fluorescence spectroscopy.
Lin, S., & Neet, K. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38722-8 · Cited by 91
Co-operativity in monomeric enzymes
Cornish-Bowden, A. J., & Cárdenas, M. L. (1987) · Journal of Theoretical Biology · doi:10.1016/s0022-5193(87)80248-5 · Cited by 91
Methods in Enzymology, volume 265
Nimmo, M. (1997) · TrAC Trends in Analytical Chemistry · doi:10.1016/s0165-9936(97)81509-9 · Cited by 73
Sequencing a protein by X-ray crystallography
Anderson, C. M., McDonald, R. C., & Steitz, T. A. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90373-x · Cited by 63
Takeda, J., Gidh‐Jain, M., Xu, L. Z., Froguel, P., Velho, G., Vaxillaire, M., Cohen, D., Shimada, F., Makino, H., & Nishi, S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82456-5 · Cited by 61
Amino Acid Conservation in Animal Glucokinases
Veiga‐da‐Cunha, M., Courtois, S. J., Michel, A., Gosselain, E., & SCHAFTINGEN, E. V. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.11.6292 · Cited by 59
Human liver glucokinase gene: cloning and sequence determination of two alternatively spliced cDNAs.
Tanizawa, Y., Koranyi, L. I., Welling, C. M., & Permutt, M. A. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.16.7294 · Cited by 56
Rosano, C., Sabini, E., Rizzi, M., Deriu, D., Murshudov, G. N., Bianchi, M., Serafini, G., Magnani, M., & Bolognesi, M. (1999) · Structure · doi:10.1016/s0969-2126(00)80032-5 · Cited by 55
Maintenance of the monomeric structure of glucokinase under reacting conditions
Cárdenas, M. L., Rabajille, E., & Niemeyer, H. M. (1978) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(78)90261-8 · Cited by 52
A recombinant human ‘mini’-hexokinase is catalytically active and regulated by hexose 6-phosphates
Magnani, M., Bianchi, M., Casabianca, A., Stocchi, V., Daniele, A., Altruda, F., Ferrone, M., & Silengo, L. (1992) · Biochemical Journal · doi:10.1042/bj2850193 · Cited by 44
Moukil, M. A., Veiga‐da‐Cunha, M., & SCHAFTINGEN, E. V. (2000) · Diabetes · doi:10.2337/diabetes.49.2.195 · Cited by 44
New structures of allosteric proteins revealing remarkable conformational changes
Mattevi, A., Rizzi, M., & Bolognesi, M. (1996) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(96)80013-3 · Cited by 37
Moukil, M. A., & SCHAFTINGEN, E. V. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008722200 · Cited by 25
Allosteric inhibition via R-state destabilization in ATP sulfurylase from Penicillium chrysogenum
MacRae, I. J., Segel, I. H., & Fisher, A. J. (2002) · Nature Structural Biology · doi:10.1038/nsb868 · Cited by 24
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Robinson, P. K. (2015) · Essays in Biochemistry · doi:10.1042/bse0590001 · Cited by 1,291
Putnam, C. D., Hammel, M., Hura, G. L., & Tainer, J. A. (2007) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583507004635 · Cited by 1,184
Osbak, K. K., Colclough, K., Saint-Martin, C., Beer, N. L., Bellanné-Chantelot, C., Ellard, S., & Gloyn, A. L. (2009) · Human Mutation · doi:10.1002/humu.21110 · Cited by 485
Allostery and the Monod-Wyman-Changeux Model After 50 Years
Changeux, J.-P. (2012) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-050511-102222 · Cited by 391
Liver glucose metabolism in humans
Adeva-Andany, M. M., Pérez-Felpete, N., Fernández-Fernández, C., Donapetry-García, C., & Pazos-García, C. (2016) · Bioscience Reports · doi:10.1042/bsr20160385 · Cited by 372
Metadata
- Authors
- Kamata, K., Mitsuya, M., Nishimura, T., Eiki, J.-I., & Nagata, Y.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2004-03
- Volume
- 12
- Issue
- 3
- Pages
- 429-438
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W2112040506
- Cited by
- 502
- References
- 43
- FWCI
- 19.69
- Type
- journal article
- Language
- en
- Open access
- bronze
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