Registro:

Referencias:

• Poljak, R.J., Amzel, L.M., Avey, H.P., Becka, L.N., Structure of Fab′ New at 6 Å resolution (1972) Nat. New Biol., 235, pp. 137-140
• Allcorn, L.C., Martin, A.C.R., SACS-Self-maintaining database of antibody crystal structure information (2002) Bioinformatics, 18 (1), pp. 175-181
• Lund, O., Nielsen, M., Lundegaard, C., Kesmir, C., Brunak, S., (2005) Immunological Bioinformatics, pp. 69-102. , MIT Press, Cambridge, MA
• Sundberg, E.J., Mariuzza, R.A., Molecular recognition in antibody-antigen complexes (2002) Advances in Protein Chemistry, 61, pp. 119-160. , DOI 10.1016/S0065-3233(02)61004-6
• Wilson, I.A., Stanfield, R.L., Antibody-antigen interactions. New structures and new conformational changes (1994) Curr. Opin. Struct. Biol., 4, pp. 857-867
• Pauling, L., A theory of the structure and process formation of antibodies (1940) J. Am. Chem. Soc., 62, p. 2643
• Foote, J., Milstein, C., Conformational isomerism and the diversity of antibodies (1994) Proceedings of the National Academy of Sciences of the United States of America, 91 (22), pp. 10370-10374. , DOI 10.1073/pnas.91.22.10370
• James, L.C., Roversi, P., Tawfik, D.S., Antibody multispecificity mediated by conformational diversity (2003) Science, 299 (5611), pp. 1362-1367. , DOI 10.1126/science.1079731
• Oldstone, M.B., Molecular mimicry and immune-mediated diseases (1998) FASEB J., 12, pp. 1255-1265
• James, L.C., Tawfik, D.S., Structure and kinetics of a transient antibody binding intermediate reveal a kinetic discrimination mechanism in antigen recognition (2005) Proceedings of the National Academy of Sciences of the United States of America, 102 (36), pp. 12730-12735. , DOI 10.1073/pnas.0500909102
• Leder, L., Berger, C., Bornhauser, S., Wendt, H., Ackermann, F., Jelesarov, I., Bosshard, H.R., Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition (1995) Biochemistry, 34 (50), pp. 16509-16518. , DOI 10.1021/bi00050a035
• Berger, C., Weber-Bornhauser, S., Eggenberger, J., Hanes, J., Pluckthun, A., Bosshard, H.R., Antigen recognition by conformational selection (1999) FEBS Letters, 450 (1-2), pp. 149-153. , DOI 10.1016/S0014-5793(99)00458-5, PII S0014579399004585
• Cerutti, M.L., Ferreiro, D.U., Sanguineti, S., Goldbaum, F.A., De Prat-Gay, G., Antibody recognition of a flexible epitope at the DNA binding site of the human papillomaviras transcriptional regulator E2 (2006) Biochemistry, 45 (51), pp. 15520-15528. , DOI 10.1021/bi0615184
• Dyson, H.J., Wright, P.E., Antigenic peptides (1995) FASEB J., 9, pp. 37-42
• Eckert, B., Martin, A., Balbach, J., Schmid, F.X., Prolyl isomerization as a molecular timer in phage infection (2005) Nature Structural and Molecular Biology, 12 (7), pp. 619-623. , DOI 10.1038/nsmb946
• Feige, M.J., Groscurth, S., Marcinowski, M., Shimizu, Y., Kessler, H., Hendershot, L.M., Buchner, J., An unfolded CH1 domain controls the assembly and secretion of IgG antibodies (2009) Mol. Cell, 34, pp. 569-579
• Rajbhandari, P., Finn, G., Solodin, N.M., Singarapu, K.K., Sahu, S.C., Markley, J.L., Kadunc, K.J., Alarid, E.T., Regulation of estrogen receptor α N terminus conformation and function by peptidyl prolyl isomerase Pin1 (2012) Mol. Cell Biol., 32, pp. 445-457
• Sarkar, P., Reichman, C., Saleh, T., Birge, R.B., Kalodimos, C.G., Proline cis-trans Isomerization Controls Autoinhibition of a Signaling Protein (2007) Molecular Cell, 25 (3), pp. 413-426. , DOI 10.1016/j.molcel.2007.01.004, PII S1097276507000081
• Sibille, N., Huvent, I., Fauquant, C., Verdegem, D., Amniai, L., Leroy, A., Wieruszeski, J.M., Landrieu, I., Structural characterization by nuclear magnetic resonance of the impact of phosphorylation in the proline-rich region of the disordered Tau protein (2011) Proteins, , September 30, 10.1002/prot.23210
• Tugarinov, V., Zvi, A., Levy, R., Anglister, J., A cis proline turn linking two β-hairpin strands in the solution structure of an antibodybound HIV-1IIIB V3 peptide (1999) Nat. Struct. Biol., 6, pp. 331-335
• Tsikaris, V., Vlachoyiannopoulos, P.G., Panou-Pomonis, E., Marraud, M., Immunoreactivity and conformation of the P-P-G-M-R-P-P repetitive epitope of the Sm autoantigen (1996) International Journal of Peptide and Protein Research, 48 (4), pp. 319-327
• McLaughlin-Drubin, M.E., Münger, K., The human papillomavirus E7 oncoprotein (2009) Virology, 384, pp. 335-344
• Munger, K., Basile, J.R., Duensing, S., Eichten, A., Gonzalez, S.L., Grace, M., Zacny, V.L., Biological activities and molecular targets of the human papillomavirus E7 oncoprotein (2001) Oncogene, 20 (54 REV. ISS. 7), pp. 7888-7898. , DOI 10.1038/sj/onc/1204860
• Galloway, D.A., Serological assays for the detection of HPV antibodies (1992) IARC Sci. Publ., pp. 147-161
• Cerutti, M.L., Alonso, L.G., Tatti, S., De Prat-Gay, G., Long-lasting immunoprotective and therapeutic effects of a hyperstable E7 oligomer based vaccine in a murine human papillomavirus tumor model Int. J. Cancer, 130, pp. 1813-1820
• Hung, C.-F., Ma, B., Monie, A., Tsen, S.-W., Wu, T.-C., Therapeutic human papillomavirus vaccines: Current clinical trials and future directions (2008) Expert Opinion on Biological Therapy, 8 (4), pp. 421-439. , DOI 10.1517/14712598.8.4.421
• Uversky, V.N., Roman, A., Oldfield, C.J., Dunker, A.K., Protein intrinsic disorder and human papillomaviruses: Increased amount of disorder in E6 and E7 oncoproteins from high risk HPVs (2006) Journal of Proteome Research, 5 (8), pp. 1829-1842. , DOI 10.1021/pr0602388
• Boehr, D.D., Nussinov, R., Wright, P.E., The role of dynamic conformational ensembles in biomolecular recognition (2009) Nat. Chem. Biol., 5, pp. 789-796
• Uversky, V.N., Intrinsically disordered proteins from A to Z Int. J. Biochem. Cell Biol., 43, pp. 1090-1103
• Tokuriki, N., Oldfield, C.J., Uversky, V.N., Berezovsky, I.N., Tawfik, D.S., Do viral proteins possess unique biophysical features? (2009) Trends Biochem. Sci., 34, pp. 53-59
• Alonso, L.G., García-Alai, M.M., Nadra, A.D., Lapeña, A.N., Almeida, F.L., Gualfetti, P., Prat-Gay, G.D., High-risk (HPV16) human papillomavirus E7 oncoprotein is highly stable and extended, with conformational transitions that could explain its multiple cellular binding partners (2002) Biochemistry, 41, pp. 10510-10518
• Garcia-Alai, M.M., Alonso, L.G., De Prat-Gay, G., The N-terminal module of HPV16 E7 is an intrinsically disordered domain that confers conformational and recognition plasticity to the oncoprotein (2007) Biochemistry, 46 (37), pp. 10405-10412. , DOI 10.1021/bi7007917
• Chemes, L.B., Glavina, J., Faivovich, J., De Prat-Gay, G., Sánchez, I.E., Evolution of linear motifs within the papillomavirus E7 oncoprotein (2012) J. Mol. Biol., 422, pp. 336-346
• Dantur, K., Alonso, L., Castaño, E., Morelli, L., Centeno-Crowley, J.M., Vighi, S., De Prat-Gay, G., Cytosolic accumulation of HPV16 E7 oligomers supports different transformation routes for the prototypic viral oncoprotein. The amyloid-cancer connection (2009) Int. J. Cancer, 125, pp. 1902-1911
• Alonso, L.G., Chemes, L.B., Cerutti, M.L., Dantur, K.I., Prat-Gay, G., Biochemical and structure-function analyses of the HPV E7 oncoprotein (2012) Small Tumour Viruses, pp. 125-150. , (Gaston, K., ed) Caister Academic Press, Norfolk, UK
• Tindle, R.W., Smith, J.A., Geysen, H.M., Selvey, L.A., Frazer, I.H., Identification of B epitopes in human papillomavirus type 16 E7 open reading frame protein (1990) Journal of General Virology, 71 (6), pp. 1347-1354
• Comerford, S.A., McCance, D.J., Dougan, G., Tite, J.P., Identification of T- and B-cell epitopes of the E7 protein of human papillomavirus type 16 (1991) J. Virol., 65, pp. 4681-4690
• Chemes, L.B., Sánchez, I.E., Smal, C., De Prat-Gay, G., Targeting mechanism of the retinoblastoma tumor suppressor by a prototypical viral oncoprotein. Structural modularity, intrinsic disorder and phosphorylation of human papillomavirus E7 (2010) FEBS J., 277, pp. 973-988
• Smal, C., Wetzler, D.E., Dantur, K.I., Chemes, L.B., Garcia-Alai, M.M., Dellarole, M., Alonso, L.G., De Prat-Gay, G., The human papillomavirus E7-E2 interaction mechanism in vitro reveals a finely tuned system for modulating available E7 and E2 proteins (2009) Biochemistry, 48, pp. 11939-11949
• De Prat Gay, G., Fersht, A.R., Generation of a family of protein fragments for structure-folding studies. 1. Folding complementation of two fragments of chymotrypsin inhibitor-2 formed by cleavage at its unique methionine residue (1994) Biochemistry, 33, pp. 7957-7963
• De Prat, G.G., Ruiz-Sanz, J., Fersht, A.R., Generation of a family of protein fragments for structure-folding studies. 2. Kinetics of association of the two chymotrypsin inhibitor-2 fragments (1994) Biochemistry, 33 (25), pp. 7964-7970. , DOI 10.1021/bi00191a025
• Chemes, L.B., Sánchez, I.E., De Prat-Gay, G., Kinetic recognition of the retinoblastoma tumor suppressor by a specific protein target (2011) J. Mol. Biol., 412, pp. 267-284
• Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A., NMRPipe. A multidimensional spectral processing system based on UNIX pipes (1995) J. Biomol. NMR, 6, pp. 277-293
• Johnson, B.A., Using NMR View to visualize and analyze the NMR spectra of macromolecules (2004) Methods Mol. Biol., 278, pp. 313-352
• Hans-Ulrich, B., (2006) Papillomavirus Research. From Natural History to Vaccines and Beyond, pp. 11-17. , Caister Academic Press, Norfolk, UK
• Foote, J., Milstein, C., Kinetic maturation of an immune response (1991) Nature, 352 (6335), pp. 530-532
• Vogt, A.D., Di Cera, E., Conformational selection or induced fit?Acritical appraisal of kinetic mechanism (2012) Biochemistry, 51, pp. 5894-5902
• Harrison, R.K., Stein, R.L., Mechanistic studies of peptidyl prolyl cis-trans isomerase: Evidence for catalysis by distortion (1990) Biochemistry, 29 (7), pp. 1684-1689
• Shen, Y., Bax, A., Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts (2010) J. Biomol. NMR, 46, pp. 199-204
• Tetin, S.Y., Prendergast, F.G., Venyaminov, S.Yu., Accuracy of protein secondary structure determination from circular dichroism spectra based on immunoglobulin examples (2003) Analytical Biochemistry, 321 (2), pp. 183-187. , DOI 10.1016/S0003-2697(03)00458-5
• Batista, F.D., Neuberger, M.S., Affinity dependence of the B cell response to antigen: A threshold, a ceiling, and the importance of off-rate (1998) Immunity, 8 (6), pp. 751-759. , DOI 10.1016/S1074-7613(00)80580-4
• Foote, J., Eisen, H.N., Kinetic and affinity limits on antibodies produced during immune responses (1995) Proc. Natl. Acad. Sci. U.S.A., 92, pp. 1254-1256
• Bosshard, H.R., Molecular recognition by induced fit. How fit is the concept? (2001) News Physiol. Sci., 16, pp. 171-173
• Ferreiro, D.U., De Prat-Gay, G., A protein-DNA binding mechanism proceeds through multi-state or two-state parallel pathways (2003) Journal of Molecular Biology, 331 (1), pp. 89-99. , DOI 10.1016/S0022-2836(03)00720-4
• Accardi, L., Donà, M.G., Mileo, A.M., Paggi, M.G., Federico, A., Torreri, P., Petrucci, T.C., Giorgi, C., Retinoblastoma-independent antiproliferative activity of novel intracellular antibodies against the E7 oncoprotein in HPV 16-positive cells (2011) BMC Cancer, 11, p. 17
• Ohlenschläger, O., Seiboth, T., Zengerling, H., Briese, L., Marchanka, A., Ramachandran, R., Baum, M., Görlach, M., Solution structure of the partially folded high-risk human papilloma virus 45 oncoprotein E7 (2006) Oncogene, 25, pp. 5953-5959
• Liu, X., Clements, A., Zhao, K., Marmorstein, R., Structure of the human Papillomavirus E7 oncoprotein and its mechanism for inactivation of the retinoblastoma tumor suppressor (2006) Journal of Biological Chemistry, 281 (1), pp. 578-586. , http://www.jbc.org/cgi/reprint/281/1/578.pdf, DOI 10.1074/jbc.M508455200
• Waltho, J.P., Feher, V.A., Lerner, R.A., Wright, P.E., Conformation of a T cell stimulating peptide in aqueous solution (1989) FEBS Letters, 250 (2), pp. 400-404. , DOI 10.1016/0014-5793(89)80764-1
• Chemes, L.B., Glavina, J., Alonso, L.G., Marino-Buslje, C., De Prat-Gay, G., Sánchez, I.E., Sequence evolution of the intrinsically disordered and globular domains of a model viral oncoprotein (2012) PLoS One, 7, pp. e47661
• Davey, N.E., Van Roey, K., Weatheritt, R.J., Toedt, G., Uyar, B., Altenberg, B., Budd, A., Gibson, T.J., Attributes of short linear motifs (2012) Mol. Biosyst., 8, pp. 268-281
• Choi, U.B., McCann, J.J., Weninger, K.R., Bowen, M.E., Beyond the random coil. Stochastic conformational switching in intrinsically disordered proteins (2011) Structure, 19, pp. 566-576
• Sugase, K., Dyson, H.J., Wright, P.E., Mechanism of coupled folding and binding of an intrinsically disordered protein (2007) Nature, 447 (7147), pp. 1021-1025. , DOI 10.1038/nature05858, PII NATURE05858
• Dogan, J., Schmidt, T., Mu, X., Engström, Å., Jemth, P., Fast association and slow transitions in the interaction between two intrinsically disordered protein domains (2012) J. Biol. Chem., 287, pp. 34316-34324
• Tompa, P., Fuxreiter, M., Fuzzy complexes. Polymorphism and structural disorder in protein-protein interactions (2008) Trends Biochem. Sci., 33, pp. 2-8
• Krchnak, V., Vagner, J., Suchankova, A., Krcmar, M., Ritterova, L., Vonka, V., Synthetic peptides derived from E7 region of human papillomavirus type 16 used as antigens in ELISA (1990) Journal of General Virology, 71 (11), pp. 2719-2724
• Zeng, Q., Peng, S., Monie, A., Yang, M., Pang, X., Hung, C.F., Wu, T.C., Control of cervicovaginal HPV-16 E7-expressing tumors by the combination of therapeutic HPV vaccination and vascular disrupting agents (2011) Hum. Gene Ther., 22, pp. 809-819

Citas:

---------- APA ----------

---------- CHICAGO ----------

---------- MLA ----------

---------- VANCOUVER ----------