A Novel Interdomain Interface In Crystallins: Structural Characterization Of The Beta Gamma-Crystallin From Geodia Cydonium At 0. 99 Angstrom Resolution (414 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2013 Jun; 69(6): 960-967.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 7.232, 5-year impact factor: 9.416
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84878290879&partnerID=40&md5=d28c3350ceacccc399d02f1acafc68fa
Keywords: Atomic Resolution, Calcium Binding, Crystallins, Domain Interactions, Folding, Greek-Key Motif, Trp Corner, Tyr Corner, Animal, Article, Binding Site, Chemical Structure, Chemistry, Genetics, Geodia, Metabolism, Molecular Evolution, Protein Folding, Protein Motif, X Ray Crystallography, Amino Acid Motifs, X-Ray, Models, Geodia Cydonium, Metazoa, Vertebrata,
Affiliations:
*** IBB - CNR ***
Department of Chemical Sciences, University of Naples Federico II, Via Cintia, I-80126 Napoli, Italy
Istituto di Biostrutture e Bioimmagini (CNR), Via Mezzocannone 16, Napoli, Italy
Dipartimento di Biologia, Università Degli Studi di Napoli Federico II, Via Cintia, Napoli, Italy
References:
Andley, U.P., (2007) Prog. Retin. Eye Res., 26, pp. 78-9
Aravind, P., Mishra, A., Suman, S.K., Jobby, M.K., Sankaranar-Ayanan, R., Sharma, Y., (2009) Biochemistry, 48, pp. 12180-12190
Aravind, P., Suman, S.K., Mishra, A., Sharma, Y., Sankaranar-Ayanan, R., (2009) J. Mol. Biol., 385, pp. 163-177
Aravind, P., Wistow, G., Sharma, Y., Sankaranarayanan, R., (2008) J. Mol. Biol., 381, pp. 509-518
Bagby, S., Harvey, T.S., Eagle, S.G., Inouye, S., Ikura, M., (1994) Structure, 2, pp. 107-122
Barnwal, R.P., Jobby, M.K., Devi, K.M., Sharma, Y., Chary, K.V., (2008) J. Mol. Biol., 386, pp. 675-689
Basak, A., Bateman, O., Slingsby, C., Pande, A., Asherie, N., Ogun, O., Benedek, G.B., Pande, J., (2003) J. Mol. Biol., 328, pp. 1137-1147
Bax, B., Lapatto, R., Nalini, V., Driessen, H., Lindley, P.F., Mahadevan, D., Blundell, T.L., Slingsby, C., (1990) Nature (London), 347, pp. 776-780
Blundell, T., Lindley, P., Miller, L., Moss, D., Slingsby, C., Tickle, I., Turnell, B., Wistow, G., (1981) Nature (London), 289, pp. 771-777
Brunger, A.T., (2007) Nature Protoc., 2, pp. 2728-2733
Clout, N.J., Kretschmar, M., Jaenicke, R., Slingsby, C., (2001) Structure, 9, pp. 115-124
D'Alessio, G., (2002) Eur. J. Biochem., 269, pp. 3122-3130
Das, P., King, J.A., Zhou, R., (2010) Protein Sci., 19, pp. 131-140
Dauter, Z., Dauter, M., Dodson, E.J., (2002) Acta Cryst., D58, pp. 494-506
Di Maro, A., Pizzo, E., Cubellis, M.V., D'Alessio, G., (2002) Gene, 299, pp. 79-82
Esposito, L., Vitagliano, L., Sica, F., Sorrentino, G., Zagari, A., Mazzarella, L., (2000) J. Mol. Biol., 297, pp. 713-732
Giancola, C., Pizzo, E., Di Maro, A., Cubellis, M.V., D'Alessio, G., (2005) FEBS J., 272, pp. 1023-1035
Hamill, S.J., Cota, E., Chothia, C., Clarke, J., (2000) J. Mol. Biol., 295, pp. 641-649
Holm, L., Kääriäinen, S., Rosenström, P., Schenkel, A., (2008) Bioinformatics, 24, pp. 2780-2781
Jobby, M.K., Sharma, Y., (2005) J. Biol. Chem., 280, pp. 1209-1216
Jones, T.A., Zou, J.-Y., Cowan, S.W., Kjeldgaard, M., (1991) Acta Cryst., A47, pp. 110-119
Kappé, G., Purkiss, A.G., Van Genesen, S.T., Slingsby, C., Lubsen, N.H., (2010) J. Mol. Evol., 71, pp. 219-230
Kretschmar, M., Mayr, E.M., Jaenicke, R., (1999) Biol. Chem., 380, pp. 89-94
Langer, G., Cohen, S.X., Lamzin, V.S., Perrakis, A., (2008) Nature Protoc., 3, pp. 1171-1179
Laskowski, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M., (1993) J. Appl. Cryst., 26, pp. 283-291
Lubsen, N.H., Aarts, H.J., Schoenmakers, J.G., (1988) Prog. Biophys. Mol. Biol., 51, pp. 47-76
Najmudin, S., Nalini, V., Driessen, H.P.C., Slingsby, C., Blundell, T.L., Moss, D.S., Lindley, P.F., (1993) Acta Cryst., D49, pp. 223-233
Navaza, J., (1994) Acta Cryst., A50, pp. 157-163
Rajanikanth, V., Srivastava, S.S., Singh, A.K., Rajyalakshmi, M., Chandra, K., Aravind, P., Sankaranarayanan, R., Sharma, Y., (2012) Biochemistry, 51, pp. 8502-8513
Rajini, B., Shridas, P., Sundari, C.S., Muralidhar, D., Chandani, S., Thomas, F., Sharma, Y., (2001) J. Biol. Chem., 276, pp. 38464-38471
Ray, M.E., Wistow, G., Su, Y.A., Meltzer, P.S., Trent, J.M., (1997) Proc. Natl Acad. Sci. USA, 94, pp. 3229-3234
Van, R.G.L., De Jong, W.W., Bloemendal, H., (1992) Mol. Biol. Rep., 16, pp. 1-10
Sharma, A.K., Minke-Gogl, V., Gohl, P., Siebendritt, R., Jaenicke, R., Rudolph, R., (1990) Eur. J. Biochem., 194, pp. 603-609
Sheldrick, G.M., (2008) Acta Cryst., A64, pp. 112-122
Shimeld, S.M., Purkiss, A.G., Dirks, R.P., Bateman, O.A., Slingsby, C., Lubsen, N.H., (2005) Curr. Biol., 15, pp. 1684-1689
Smith, M.A., Bateman, O.A., Jaenicke, R., Slingsby, C., (2007) Protein Sci., 16, pp. 615-625
Srivastava, A.K., Sharma, Y., Chary, K.V., (2010) Biochemistry, 49, pp. 9746-9755
Talla, V., Narayanan, C., Srinivasan, N., Balasubramanian, D., (2006) Invest. Ophthalmol. Vis. Sci., 47, pp. 5212-5217
Talla, V., Srinivasan, N., Balasubramanian, D., (2008) Invest. Ophthalmol. Vis. Sci., 49, pp. 3483-3490
Trinkl, S., Glockshuber, R., Jaenicke, R., (1994) Protein Sci., 3, pp. 1392-1400
Van Montfort, R.L., Bateman, O.A., Lubsen, N.H., Slingsby, C., (2003) Protein Sci., 12, pp. 2606-2612
Vergara, A., Merlino, A., Pizzo, E., D'Alessio, G., Mazzarella, L., (2008) Acta Cryst., D64, pp. 167-171
Wenk, M., Baumgartner, R., Holak, T.A., Huber, R., Jaenicke, R., Mayr, E.M., (1999) J. Mol. Biol., 286, pp. 1533-1545
Wistow, G., (1990) J. Mol. Evol., 30, pp. 140-145
Wistow, G.J., Piatigorsky, J., (1988) Annu. Rev. Biochem., 57, pp. 479-504
Wistow, G., Turnell, B., Summers, L., Slingsby, C., Moss, D., Miller, L., Lindley, P., Blundell, T., (1983) J. Mol. Biol., 170, pp. 175-202
Andley, U. P., (2007) Prog. Retin. Eye Res., 26, pp. 78-9
Barnwal, R. P., Jobby, M. K., Devi, K. M., Sharma, Y., Chary, K. V., (2008) J. Mol. Biol., 386, pp. 675-689
Brunger, A. T., (2007) Nature Protoc., 2, pp. 2728-2733
Clout, N. J., Kretschmar, M., Jaenicke, R., Slingsby, C., (2001) Structure, 9, pp. 115-124
Das, P., King, J. A., Zhou, R., (2010) Protein Sci., 19, pp. 131-140
Hamill, S. J., Cota, E., Chothia, C., Clarke, J., (2000) J. Mol. Biol., 295, pp. 641-649
Holm, L., K ri inen, S., Rosenstr m, P., Schenkel, A., (2008) Bioinformatics, 24, pp. 2780-2781
Jobby, M. K., Sharma, Y., (2005) J. Biol. Chem., 280, pp. 1209-1216
Jones, T. A., Zou, J. -Y., Cowan, S. W., Kjeldgaard, M., (1991) Acta Cryst., A47, pp. 110-119
Kapp, G., Purkiss, A. G., Van Genesen, S. T., Slingsby, C., Lubsen, N. H., (2010) J. Mol. Evol., 71, pp. 219-230
Laskowski, R. A., MacArthur, M. W., Moss, D. S., Thornton, J. M., (1993) J. Appl. Cryst., 26, pp. 283-291
Lubsen, N. H., Aarts, H. J., Schoenmakers, J. G., (1988) Prog. Biophys. Mol. Biol., 51, pp. 47-76
Ray, M. E., Wistow, G., Su, Y. A., Meltzer, P. S., Trent, J. M., (1997) Proc. Natl Acad. Sci. USA, 94, pp. 3229-3234
Van, R. G. L., De Jong, W. W., Bloemendal, H., (1992) Mol. Biol. Rep., 16, pp. 1-10
Sharma, A. K., Minke-Gogl, V., Gohl, P., Siebendritt, R., Jaenicke, R., Rudolph, R., (1990) Eur. J. Biochem., 194, pp. 603-609
Sheldrick, G. M., (2008) Acta Cryst., A64, pp. 112-122
Shimeld, S. M., Purkiss, A. G., Dirks, R. P., Bateman, O. A., Slingsby, C., Lubsen, N. H., (2005) Curr. Biol., 15, pp. 1684-1689
Smith, M. A., Bateman, O. A., Jaenicke, R., Slingsby, C., (2007) Protein Sci., 16, pp. 615-625
Srivastava, A. K., Sharma, Y., Chary, K. V., (2010) Biochemistry, 49, pp. 9746-9755
Van Montfort, R. L., Bateman, O. A., Lubsen, N. H., Slingsby, C., (2003) Protein Sci., 12, pp. 2606-2612
Wistow, G. J., Piatigorsky, J., (1988) Annu. Rev. Biochem., 57, pp. 479-504
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2013 Jun; 69(6): 960-967.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 7.232, 5-year impact factor: 9.416
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84878290879&partnerID=40&md5=d28c3350ceacccc399d02f1acafc68fa
Keywords: Atomic Resolution, Calcium Binding, Crystallins, Domain Interactions, Folding, Greek-Key Motif, Trp Corner, Tyr Corner, Animal, Article, Binding Site, Chemical Structure, Chemistry, Genetics, Geodia, Metabolism, Molecular Evolution, Protein Folding, Protein Motif, X Ray Crystallography, Amino Acid Motifs, X-Ray, Models, Geodia Cydonium, Metazoa, Vertebrata,
Affiliations:
*** IBB - CNR ***
Department of Chemical Sciences, University of Naples Federico II, Via Cintia, I-80126 Napoli, Italy
Istituto di Biostrutture e Bioimmagini (CNR), Via Mezzocannone 16, Napoli, Italy
Dipartimento di Biologia, Università Degli Studi di Napoli Federico II, Via Cintia, Napoli, Italy
References:
Andley, U.P., (2007) Prog. Retin. Eye Res., 26, pp. 78-9
Aravind, P., Mishra, A., Suman, S.K., Jobby, M.K., Sankaranar-Ayanan, R., Sharma, Y., (2009) Biochemistry, 48, pp. 12180-12190
Aravind, P., Suman, S.K., Mishra, A., Sharma, Y., Sankaranar-Ayanan, R., (2009) J. Mol. Biol., 385, pp. 163-177
Aravind, P., Wistow, G., Sharma, Y., Sankaranarayanan, R., (2008) J. Mol. Biol., 381, pp. 509-518
Bagby, S., Harvey, T.S., Eagle, S.G., Inouye, S., Ikura, M., (1994) Structure, 2, pp. 107-122
Barnwal, R.P., Jobby, M.K., Devi, K.M., Sharma, Y., Chary, K.V., (2008) J. Mol. Biol., 386, pp. 675-689
Basak, A., Bateman, O., Slingsby, C., Pande, A., Asherie, N., Ogun, O., Benedek, G.B., Pande, J., (2003) J. Mol. Biol., 328, pp. 1137-1147
Bax, B., Lapatto, R., Nalini, V., Driessen, H., Lindley, P.F., Mahadevan, D., Blundell, T.L., Slingsby, C., (1990) Nature (London), 347, pp. 776-780
Blundell, T., Lindley, P., Miller, L., Moss, D., Slingsby, C., Tickle, I., Turnell, B., Wistow, G., (1981) Nature (London), 289, pp. 771-777
Brunger, A.T., (2007) Nature Protoc., 2, pp. 2728-2733
Clout, N.J., Kretschmar, M., Jaenicke, R., Slingsby, C., (2001) Structure, 9, pp. 115-124
D'Alessio, G., (2002) Eur. J. Biochem., 269, pp. 3122-3130
Das, P., King, J.A., Zhou, R., (2010) Protein Sci., 19, pp. 131-140
Dauter, Z., Dauter, M., Dodson, E.J., (2002) Acta Cryst., D58, pp. 494-506
Di Maro, A., Pizzo, E., Cubellis, M.V., D'Alessio, G., (2002) Gene, 299, pp. 79-82
Esposito, L., Vitagliano, L., Sica, F., Sorrentino, G., Zagari, A., Mazzarella, L., (2000) J. Mol. Biol., 297, pp. 713-732
Giancola, C., Pizzo, E., Di Maro, A., Cubellis, M.V., D'Alessio, G., (2005) FEBS J., 272, pp. 1023-1035
Hamill, S.J., Cota, E., Chothia, C., Clarke, J., (2000) J. Mol. Biol., 295, pp. 641-649
Holm, L., Kääriäinen, S., Rosenström, P., Schenkel, A., (2008) Bioinformatics, 24, pp. 2780-2781
Jobby, M.K., Sharma, Y., (2005) J. Biol. Chem., 280, pp. 1209-1216
Jones, T.A., Zou, J.-Y., Cowan, S.W., Kjeldgaard, M., (1991) Acta Cryst., A47, pp. 110-119
Kappé, G., Purkiss, A.G., Van Genesen, S.T., Slingsby, C., Lubsen, N.H., (2010) J. Mol. Evol., 71, pp. 219-230
Kretschmar, M., Mayr, E.M., Jaenicke, R., (1999) Biol. Chem., 380, pp. 89-94
Langer, G., Cohen, S.X., Lamzin, V.S., Perrakis, A., (2008) Nature Protoc., 3, pp. 1171-1179
Laskowski, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M., (1993) J. Appl. Cryst., 26, pp. 283-291
Lubsen, N.H., Aarts, H.J., Schoenmakers, J.G., (1988) Prog. Biophys. Mol. Biol., 51, pp. 47-76
Najmudin, S., Nalini, V., Driessen, H.P.C., Slingsby, C., Blundell, T.L., Moss, D.S., Lindley, P.F., (1993) Acta Cryst., D49, pp. 223-233
Navaza, J., (1994) Acta Cryst., A50, pp. 157-163
Rajanikanth, V., Srivastava, S.S., Singh, A.K., Rajyalakshmi, M., Chandra, K., Aravind, P., Sankaranarayanan, R., Sharma, Y., (2012) Biochemistry, 51, pp. 8502-8513
Rajini, B., Shridas, P., Sundari, C.S., Muralidhar, D., Chandani, S., Thomas, F., Sharma, Y., (2001) J. Biol. Chem., 276, pp. 38464-38471
Ray, M.E., Wistow, G., Su, Y.A., Meltzer, P.S., Trent, J.M., (1997) Proc. Natl Acad. Sci. USA, 94, pp. 3229-3234
Van, R.G.L., De Jong, W.W., Bloemendal, H., (1992) Mol. Biol. Rep., 16, pp. 1-10
Sharma, A.K., Minke-Gogl, V., Gohl, P., Siebendritt, R., Jaenicke, R., Rudolph, R., (1990) Eur. J. Biochem., 194, pp. 603-609
Sheldrick, G.M., (2008) Acta Cryst., A64, pp. 112-122
Shimeld, S.M., Purkiss, A.G., Dirks, R.P., Bateman, O.A., Slingsby, C., Lubsen, N.H., (2005) Curr. Biol., 15, pp. 1684-1689
Smith, M.A., Bateman, O.A., Jaenicke, R., Slingsby, C., (2007) Protein Sci., 16, pp. 615-625
Srivastava, A.K., Sharma, Y., Chary, K.V., (2010) Biochemistry, 49, pp. 9746-9755
Talla, V., Narayanan, C., Srinivasan, N., Balasubramanian, D., (2006) Invest. Ophthalmol. Vis. Sci., 47, pp. 5212-5217
Talla, V., Srinivasan, N., Balasubramanian, D., (2008) Invest. Ophthalmol. Vis. Sci., 49, pp. 3483-3490
Trinkl, S., Glockshuber, R., Jaenicke, R., (1994) Protein Sci., 3, pp. 1392-1400
Van Montfort, R.L., Bateman, O.A., Lubsen, N.H., Slingsby, C., (2003) Protein Sci., 12, pp. 2606-2612
Vergara, A., Merlino, A., Pizzo, E., D'Alessio, G., Mazzarella, L., (2008) Acta Cryst., D64, pp. 167-171
Wenk, M., Baumgartner, R., Holak, T.A., Huber, R., Jaenicke, R., Mayr, E.M., (1999) J. Mol. Biol., 286, pp. 1533-1545
Wistow, G., (1990) J. Mol. Evol., 30, pp. 140-145
Wistow, G.J., Piatigorsky, J., (1988) Annu. Rev. Biochem., 57, pp. 479-504
Wistow, G., Turnell, B., Summers, L., Slingsby, C., Moss, D., Miller, L., Lindley, P., Blundell, T., (1983) J. Mol. Biol., 170, pp. 175-202
Andley, U. P., (2007) Prog. Retin. Eye Res., 26, pp. 78-9
Barnwal, R. P., Jobby, M. K., Devi, K. M., Sharma, Y., Chary, K. V., (2008) J. Mol. Biol., 386, pp. 675-689
Brunger, A. T., (2007) Nature Protoc., 2, pp. 2728-2733
Clout, N. J., Kretschmar, M., Jaenicke, R., Slingsby, C., (2001) Structure, 9, pp. 115-124
Das, P., King, J. A., Zhou, R., (2010) Protein Sci., 19, pp. 131-140
Hamill, S. J., Cota, E., Chothia, C., Clarke, J., (2000) J. Mol. Biol., 295, pp. 641-649
Holm, L., K ri inen, S., Rosenstr m, P., Schenkel, A., (2008) Bioinformatics, 24, pp. 2780-2781
Jobby, M. K., Sharma, Y., (2005) J. Biol. Chem., 280, pp. 1209-1216
Jones, T. A., Zou, J. -Y., Cowan, S. W., Kjeldgaard, M., (1991) Acta Cryst., A47, pp. 110-119
Kapp, G., Purkiss, A. G., Van Genesen, S. T., Slingsby, C., Lubsen, N. H., (2010) J. Mol. Evol., 71, pp. 219-230
Laskowski, R. A., MacArthur, M. W., Moss, D. S., Thornton, J. M., (1993) J. Appl. Cryst., 26, pp. 283-291
Lubsen, N. H., Aarts, H. J., Schoenmakers, J. G., (1988) Prog. Biophys. Mol. Biol., 51, pp. 47-76
Ray, M. E., Wistow, G., Su, Y. A., Meltzer, P. S., Trent, J. M., (1997) Proc. Natl Acad. Sci. USA, 94, pp. 3229-3234
Van, R. G. L., De Jong, W. W., Bloemendal, H., (1992) Mol. Biol. Rep., 16, pp. 1-10
Sharma, A. K., Minke-Gogl, V., Gohl, P., Siebendritt, R., Jaenicke, R., Rudolph, R., (1990) Eur. J. Biochem., 194, pp. 603-609
Sheldrick, G. M., (2008) Acta Cryst., A64, pp. 112-122
Shimeld, S. M., Purkiss, A. G., Dirks, R. P., Bateman, O. A., Slingsby, C., Lubsen, N. H., (2005) Curr. Biol., 15, pp. 1684-1689
Smith, M. A., Bateman, O. A., Jaenicke, R., Slingsby, C., (2007) Protein Sci., 16, pp. 615-625
Srivastava, A. K., Sharma, Y., Chary, K. V., (2010) Biochemistry, 49, pp. 9746-9755
Van Montfort, R. L., Bateman, O. A., Lubsen, N. H., Slingsby, C., (2003) Protein Sci., 12, pp. 2606-2612
Wistow, G. J., Piatigorsky, J., (1988) Annu. Rev. Biochem., 57, pp. 479-504
A Novel Interdomain Interface In Crystallins: Structural Characterization Of The Beta Gamma-Crystallin From Geodia Cydonium At 0. 99 Angstrom Resolution
The βγ-crystallin superfamily includes highly diverse proteins belonging to all of the kingdoms of life. Based on structural topology, these proteins are considered to be evolutionarily related to the long-lived βγ-crystallins that constitute the vertebrate eye lens. This study reports the crystallographic structure at 0.99 14;Å resolution of the two-domain βγ-crystallin (geodin) from the sponge Geodia cydonium. This is the most ancient member of the βγ-crystallin superfamily in metazoans. The X-ray structure shows that the geodin domains adopt the typical βγ-crystallin fold with a paired Greek-key motif, thus confirming the hypothesis that the crystallin-type scaffold used in the evolution of bacteria and moulds was recruited very early in metazoans. As a significant new structural feature, the sponge protein possesses a unique interdomain interface made up by pairing between the second motif of the first domain and the first motif of the second domain. The atomic resolution also allowed a detailed analysis of the calcium-binding site of the protein. © 2013 International Union of Crystallography.
The βγ-crystallin superfamily includes highly diverse proteins belonging to all of the kingdoms of life. Based on structural topology, these proteins are considered to be evolutionarily related to the long-lived βγ-crystallins that constitute the vertebrate eye lens. This study reports the crystallographic structure at 0.99 14;Å resolution of the two-domain βγ-crystallin (geodin) from the sponge Geodia cydonium. This is the most ancient member of the βγ-crystallin superfamily in metazoans. The X-ray structure shows that the geodin domains adopt the typical βγ-crystallin fold with a paired Greek-key motif, thus confirming the hypothesis that the crystallin-type scaffold used in the evolution of bacteria and moulds was recruited very early in metazoans. As a significant new structural feature, the sponge protein possesses a unique interdomain interface made up by pairing between the second motif of the first domain and the first motif of the second domain. The atomic resolution also allowed a detailed analysis of the calcium-binding site of the protein. © 2013 International Union of Crystallography.
A Novel Interdomain Interface In Crystallins: Structural Characterization Of The Beta Gamma-Crystallin From Geodia Cydonium At 0. 99 Angstrom Resolution
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A Novel Interdomain Interface In Crystallins: Structural Characterization Of The Beta Gamma-Crystallin From Geodia Cydonium At 0. 99 Angstrom Resolution
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Berisio R, Sica F, Lamzin VS, Wilson KS, Zagari A, Mazzarella L
* Atomic resolution structures of ribonuclease A at six pH values (562 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2002; 58(3): 441-450.
Impact Factor: 1.76
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Berisio R, Sica F, Lamzin VS, Wilson KS, Zagari A, Mazzarella L
* Atomic Resolution Structures Of Rnase A At Six Ph Values (230 views)
Acta Crystallogr D Biol Crystallogr, 2002; N/D: 441-450.
Impact Factor: 7.232
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Berisio R, Viguera A, Serrano L, Wilmanns M
* Atomic resolution structure of a mutant of the spectrin SH3 domain (289 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2001 Feb; 57(2): 337-340.
Impact Factor: 2.124
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Oliva R, Falcigno L, D'Auria G, Zanotti G, Paolillo L
Conformation and calcium-binding properties of a bicyclic nonapeptide (380 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2000; 56(1): 27-36.
Impact Factor: 2.405
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Berisio R, Lamzin VS, Sica F, Wilson KS, Zagari A, Mazzarella L
Protein titration in the crystal state (447 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1999 Oct 1; 292(4): 845-854.
Impact Factor: 5.501
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Crisma M, Formaggio F, Valle G, Toniolo C, Saviano M, Iacovino R, Zaccaro L, Benedetti E
Experimental evidence at atomic resolution for intramolecular N- H···π (phenyl) interactions in a family of amino acid derivatives (418 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1997; 42(1): 1-6.
Impact Factor: 2.425
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* Reactive astrocytosis-induced perturbation of synaptic homeostasis is restored by nerve growth factor (455 views)
Neurobiology Of Disease (ISSN: 0969-9961), 2011 Mar; 41(3): 630-639.
Impact Factor: 5.403
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Diana D, Ziaco B, Scarabelli G, Pedone C, Colombo G, D'Andrea LD, Fattorusso R
* Structural analysis of a helical peptide unfolding pathway (461 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2010 May 10; 16(18): 5400-5407.
Impact Factor: 5.476
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Attanasio F, Cataldo S, Fisichella S, Nicoletti S, Nicoletti VG, Pignataro B, Savarino A, Rizzarelli E
* Protective effects of L- and D-carnosine on alpha-crystallin amyloid fibril formation: implications for cataract disease (352 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2009 Jul 14; 48(27): 6522-6531.
Impact Factor: 3.226
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Vitagliano L, Vergara A, Bonomi G, Merlino A, Verde C, Di Prisco G, Howes BD, Smulevich G, Mazzarella L
* Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state (400 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2008 Sep 13; 130(32): 10527-10535.
Impact Factor: 8.091
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Ruggiero A, Chambery A, Di Maro A, Parente A, Berisio R
* Atomic Resolution (1. 1 Angstrom) Structure Of The Ribosome-Inactivating Protein Pd-L4 From Phytolacca Dioica L. Leaves (388 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2008 Apr; 71(1): 8-15.
Impact Factor: 3.419
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Attanasio F, Cascio C, Fisichella S, Nicoletti VG, Pignataro B, Savarino A, Rizzarelli E
* Trehalose effects on alpha-crystallin aggregates (529 views)
Biochem Biophys Res Commun (ISSN: 0006-291x, 0006-291xlinking), 2007 Mar 23; 354(4): 899-905.
Impact Factor: 2.749
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Esposito L, Vitagliano L, Mazzarella L
* Recent advances in atomic resolution protein crystallography (455 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2002 Apr; 9(2): 95-105.
Impact Factor: 0.622
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Berisio R, Sica F, Lamzin VS, Wilson KS, Zagari A, Mazzarella L
* Atomic resolution structures of ribonuclease A at six pH values (562 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2002; 58(3): 441-450.
Impact Factor: 1.76
View Export to BibTeX Export to EndNote
Berisio R, Sica F, Lamzin VS, Wilson KS, Zagari A, Mazzarella L
* Atomic Resolution Structures Of Rnase A At Six Ph Values (230 views)
Acta Crystallogr D Biol Crystallogr, 2002; N/D: 441-450.
Impact Factor: 7.232
View Export to BibTeX Export to EndNote
Berisio R, Viguera A, Serrano L, Wilmanns M
* Atomic resolution structure of a mutant of the spectrin SH3 domain (289 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2001 Feb; 57(2): 337-340.
Impact Factor: 2.124
View Export to BibTeX Export to EndNote
Oliva R, Falcigno L, D'Auria G, Zanotti G, Paolillo L
Conformation and calcium-binding properties of a bicyclic nonapeptide (380 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2000; 56(1): 27-36.
Impact Factor: 2.405
View Export to BibTeX Export to EndNote
Berisio R, Lamzin VS, Sica F, Wilson KS, Zagari A, Mazzarella L
Protein titration in the crystal state (447 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1999 Oct 1; 292(4): 845-854.
Impact Factor: 5.501
View Export to BibTeX Export to EndNote
Crisma M, Formaggio F, Valle G, Toniolo C, Saviano M, Iacovino R, Zaccaro L, Benedetti E
Experimental evidence at atomic resolution for intramolecular N- H···π (phenyl) interactions in a family of amino acid derivatives (418 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1997; 42(1): 1-6.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
13 Records (13 excluding Abstracts).
Total impact factor: 50.433 (50.433 excluding Abstracts).
Total 5 year impact factor: 68.821 (68.821 excluding Abstracts).
Total impact factor: 50.433 (50.433 excluding Abstracts).
Total 5 year impact factor: 68.821 (68.821 excluding Abstracts).
414 views. Last view on Wednesday 15 March 2023, 18:31:44
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