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Allosteric inhibitors of the NS3 protease from the hepatitis C virus.
Abian O, Vega S, Sancho J, Velazquez-Campoy A. Abian O, et al. Among authors: sancho j. PLoS One. 2013 Jul 30;8(7):e69773. doi: 10.1371/journal.pone.0069773. Print 2013. PLoS One. 2013. PMID: 23936097 Free PMC article.
The active site of pepsin is formed in the intermediate conformation dominant at mildly acidic pH.
Campos LA, Sancho J. Campos LA, et al. Among authors: sancho j. FEBS Lett. 2003 Mar 13;538(1-3):89-95. doi: 10.1016/s0014-5793(03)00152-2. FEBS Lett. 2003. PMID: 12633859
How FMN binds to anabaena apoflavodoxin: a hydrophobic encounter at an open binding site.
Lostao A, Daoudi F, Irún MP, Ramon A, Fernández-Cabrera C, Romero A, Sancho J. Lostao A, et al. Among authors: sancho j. J Biol Chem. 2003 Jun 27;278(26):24053-61. doi: 10.1074/jbc.M301049200. Epub 2003 Apr 7. J Biol Chem. 2003. PMID: 12682068
The long and short flavodoxins: I. The role of the differentiating loop in apoflavodoxin structure and FMN binding.
López-Llano J, Maldonado S, Bueno M, Lostao A, Angeles-Jiménez M, Lillo MP, Sancho J. López-Llano J, et al. Among authors: sancho j. J Biol Chem. 2004 Nov 5;279(45):47177-83. doi: 10.1074/jbc.M405792200. Epub 2004 Aug 17. J Biol Chem. 2004. PMID: 15317816
The modest role played by the long loop of long flavodoxins in the structure of these proteins (and in its conformational stability, see Lopez-Llano, J., Maldonado, S., Jain, S., Lostao, A., Godoy-Ruiz, R., Sanchez-Ruiz, Cortijo, M., Fernandez-Recio, J., and Sanc
The modest role played by the long loop of long flavodoxins in the structure of these proteins (and in its conformational stability, see Lop …
Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation.
Campos LA, Garcia-Mira MM, Godoy-Ruiz R, Sanchez-Ruiz JM, Sancho J. Campos LA, et al. Among authors: sancho j. J Mol Biol. 2004 Nov 12;344(1):223-37. doi: 10.1016/j.jmb.2004.09.047. J Mol Biol. 2004. PMID: 15504413
Towards a new therapeutic target: Helicobacter pylori flavodoxin.
Cremades N, Bueno M, Toja M, Sancho J. Cremades N, et al. Among authors: sancho j. Biophys Chem. 2005 Apr 1;115(2-3):267-76. doi: 10.1016/j.bpc.2004.12.045. Epub 2005 Jan 7. Biophys Chem. 2005. PMID: 15752617
Flavodoxins: sequence, folding, binding, function and beyond.
Sancho J. Sancho J. Cell Mol Life Sci. 2006 Apr;63(7-8):855-64. doi: 10.1007/s00018-005-5514-4. Cell Mol Life Sci. 2006. PMID: 16465441 Review.
Do proteins with similar folds have similar transition state structures? A diffuse transition state of the 169 residue apoflavodoxin.
Bueno M, Ayuso-Tejedor S, Sancho J. Bueno M, et al. Among authors: sancho j. J Mol Biol. 2006 Jun 9;359(3):813-24. doi: 10.1016/j.jmb.2006.03.067. Epub 2006 Apr 19. J Mol Biol. 2006. PMID: 16647718
Common conformational changes in flavodoxins induced by FMN and anion binding: the structure of Helicobacter pylori apoflavodoxin.
Martínez-Júlvez M, Cremades N, Bueno M, Pérez-Dorado I, Maya C, Cuesta-López S, Prada D, Falo F, Hermoso JA, Sancho J. Martínez-Júlvez M, et al. Among authors: sancho j. Proteins. 2007 Nov 15;69(3):581-94. doi: 10.1002/prot.21410. Proteins. 2007. PMID: 17623845
The flavodoxin from Helicobacter pylori: structural determinants of thermostability and FMN cofactor binding.
Cremades N, Velazquez-Campoy A, Freire E, Sancho J. Cremades N, et al. Among authors: sancho j. Biochemistry. 2008 Jan 15;47(2):627-39. doi: 10.1021/bi701365e. Epub 2007 Dec 21. Biochemistry. 2008. PMID: 18095659 Free PMC article.
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