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92 results on '"Guntert, P."'

1. GB1 in mammalian cells, 50 uM

Author

Gerez, J.A., primary, Prymaczok, N.C., additional, Kadavath, H., additional, Gosh, D., additional, Butikofer, M., additional, Guntert, P., additional, and Riek, R., additional

Published
2022
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2. GB1 in mammalian cells, 10 uM

Author

Gerez, J.A., primary, Prymaczok, N.C., additional, Kadavath, H., additional, Gosh, D., additional, Butikofer, M., additional, Guntert, P., additional, and Riek, R., additional

Published
2022
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3. Aplicação das escalas de personalidade EFS e EFEx no contexto organizacional

Author

Ivan Sant' Ana Rabelo, Irene F. Almeida de Sá Leme, Milena Oliveira Rossetti, Sílvia Verônica Pacanaro, Ingo Bernd Guntert, and Veridiana Leiva Barrionuevo

Subjects
Escalas de Personalidade, Avaliação Psicológica, Psicologia Organizacional, Psychology, BF1-990
Abstract

Este artigo teve como objetivo investigar os aspectos da personalidade denominados extroversão e socialização, em profissionais no contexto organizacional, além de explorar possíveis diferenças entre as variáveis sexo, idade e cargos exercidos. A amostra foi composta por 68 participantes, sendo 45,6% do sexo feminino e 54,4% do sexo masculino, com idades entre 16 e 62 anos. Aplicou-se a Escala Fatorial de Extroversão (EFEx) e a Escala Fatorial de Socialização (EFS). Foi obtido nos dois instrumentos, um bom índice de precisão (a=0,87) e observou-se correlação positiva de 0,47 entre o fator Amabilidade (EFS) com o fator Interações Sociais (EFEx). Por outro lado o Fator Pró-sociabilidade (EFS) obteve correlação negativa de -0,52 com o fator Altivez (EFEx), ambas correlações estatisticamente significantes (p

Published
2009

21. RECOORD: a recalculated coordinate database of 500+ proteins from the PDB using restraints from the BioMagResBank

Author

Nederveen, A.J., Doreleijers, J.F., Vranken, W., Miller, Z., Spronk, C.A.E.M., Nabuurs, S.B., Guntert, P., Livny, M., Markley, J.L., Nilges, M., Ulrich, E.L., Kaptein, R., Bonvin, A.M.J.J., NMR-spectroscopie, NMR Spectroscopy 1, Dep Scheikunde, Other departments, and Department of Bio-engineering Sciences

Subjects
Bioinformatics, Computer science, Protein Conformation, Protein Data Bank (RCSB PDB), 010402 general chemistry, computer.software_genre, 01 natural sciences, Biochemistry, 03 medical and health sciences, Structural Biology, Taverne, Databases, Protein, Molecular Biology, 030304 developmental biology, 0303 health sciences, Database, biology, Proteins, Reproducibility of Results, Structure validation, computer.file_format, Cyana, biology.organism_classification, Protein Data Bank, Solution structure, 0104 chemical sciences, Weak correlation, International, Reference database, Data mining, Stress, Mechanical, Cellular energy metabolism [UMCN 5.3], computer, Ramachandran plot
Abstract

State-of-the-art methods based on CNS and CYANA were used to recalculate the nuclear magnetic resonance (NMR) solution structures of 500 proteins for which coordinates and NMR restraints are available from the Protein Data Bank. Curated restraints were obtained from the BioMagResBank FRED database. Although the original NMR struc- tures were determined by various methods, they all were recalculated by CNS and CYANA and refined subsequently by restrained molecular dynamics (CNS) in a hydrated environment. We present an extensive analysis of the results, in terms of various quality indicators generated by PROCHECK and WHAT- _CHECK. On average, the quality indicators for pack- ing and Ramachandran appearance moved one stan- dard deviation closer to the mean of the reference database. The structural quality of the recalculated structures is discussed in relation to various parame- ters, including number of restraints per residue, NOE completeness and positional root mean square devia- tion (RMSD). Correlations between pairs of these quality indicators were generally low; for example, there is a weak correlation between the number of restraints per residue and the Ramachandran appear- ance according to WHAT_CHECK (r 0.31). The set of recalculated coordinates constitutes a unified data- base of protein structures in which potential user- and software-dependent biases have been kept as small as possible. The database can be used by the structural biology community for further develop- ment of calculation protocols, validation tools, struc- ture-based statistical approaches and modeling. The RECOORD database of recalculated structures is pub- licly available from http://www.ebi.ac.uk/msd/reco

Published
2005

22. RECOORD: a Recalculated COORdinates Database of 500+ proteins from PDB using restraints from the BioMagResBank

Author

Nederveen, A.J., Doreleijers, J.F., Vranken, W., Miller, Z., Spronk, C.A.E.M., Nabuurs, S.B., Guntert, P., Livny, M., Markley, J.L., Nilges, M., Ulrich, E.L., Kaptein, R., Bonvin, A.M.J.J., NMR-spectroscopie, NMR Spectroscopy 1, and Dep Scheikunde

Subjects
International, Taverne
Abstract

State‐of‐the‐art methods based on CNS and CYANA were used to recalculate the nuclear magnetic resonance (NMR) solution structures of 500+ proteins for which coordinates and NMR restraints are available from the Protein Data Bank. Curated restraints were obtained from the BioMagResBank FRED database. Although the original NMR structures were determined by various methods, they all were recalculated by CNS and CYANA and refined subsequently by restrained molecular dynamics (CNS) in a hydrated environment. We present an extensive analysis of the results, in terms of various quality indicators generated by PROCHECK and WHAT_CHECK. On average, the quality indicators for packing and Ramachandran appearance moved one standard deviation closer to the mean of the reference database. The structural quality of the recalculated structures is discussed in relation to various parameters, including number of restraints per residue, NOE completeness and positional root mean square deviation (RMSD). Correlations between pairs of these quality indicators were generally low; for example, there is a weak correlation between the number of restraints per residue and the Ramachandran appearance according to WHAT_CHECK (r = 0.31). The set of recalculated coordinates constitutes a unified database of protein structures in which potential user‐ and software‐dependent biases have been kept as small as possible. The database can be used by the structural biology community for further development of calculation protocols, validation tools, structure‐based statistical approaches and modeling. The RECOORD database of recalculated structures is publicly available from http://www.ebi.ac.uk/msd/recoord. Proteins 2005.

Published
2005

23. Solution structure of RBFOX family ASD-1 RRM and SUP-12 RRM in ternary complex with RNA

Author

Takahashi, M., primary, Kuwasako, K., additional, Unzai, S., additional, Tsuda, K., additional, Yoshikawa, S., additional, He, F., additional, Kobayashi, N., additional, Guntert, P., additional, Shirouzu, M., additional, Ito, T., additional, Tanaka, A., additional, Yokoyama, S., additional, Hagiwara, M., additional, Kuroyanagi, H., additional, and Muto, Y., additional

Published
2014
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24. Solution structure of c.elegans SUP-12 RRM in complex with RNA

Author

Takahashi, M., primary, Kuwasako, K., additional, Unzai, S., additional, Tsuda, K., additional, Yoshikawa, S., additional, He, F., additional, Kobayashi, N., additional, Guntert, P., additional, Shirouzu, M., additional, Ito, T., additional, Tanaka, A., additional, Yokoyama, S., additional, Hagiwara, M., additional, Kuroyanagi, H., additional, and Muto, Y., additional

Published
2014
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25. Solution structure of the 162 residue C-terminal domain of human elongation factor 1B gamma

Author

Vanwetswinkel, S., Kriek, J., Andersen, G.R., Guntert, P., Dijk, J., Canters, G.W., and Siegal, G.

Abstract

The multisubunit elongation factor 1 (eEF1) is required for the elongation step of eukaryotic protein synthesis. The eEF1 complex consists of four subunits: eEF1A, a G-protein that shuttles aminoacylated tRNAs to the ribosome; eEF1Balpha and eEF1Bbeta, two guanine nucleotide exchange factors, and eEF1Bgamma. Although its exact function remains unknown, this latter subunit is present in all eukaryotes. Recombinant human eEF1Bgamma has been purified and shown to consist of two independent domains. We have utilized high resolution NMR to determine the three-dimensional structure of the 19 kDa C-terminal fragment (domain 2). The structure consists of a five-stranded anti-parallel beta-sheet surrounded by alpha-helices and resembles a contact lens. Highly conserved residues are mainly located on the concave face, suggesting thereby that this side of the molecule might be involved in some biologically relevant interface(s). Although the isolated domain 2 appears to be mostly monomeric in solution, biochemical and structural data indicate a potential homodimer. The proposed dimer model can be further positioned within the quaternary arrangement of the whole eEF1 assembly.

Published
2003

28. Blind testing of routine, fully automated determination of protein structures from NMR data.

Author

Rosato, A., Aramini, J.M., Arrowsmith, C., Bagaria, A., Baker, D., Cavalli, A., Doreleijers, J., Eletsky, A., Giachetti, A., Guerry, P., Gutmanas, A., Guntert, P., He, Y., Herrmann, T., Huang, Y.J., Jaravine, V., Jonker, H.R., Kennedy, M.A., Lange, O.F., Liu, G., Malliavin, T.E., Mani, R., Mao, B., Montelione, G.T., Nilges, M., Rossi, P., Schot, G. van der, Schwalbe, H., Szyperski, T.A., Vendruscolo, M., Vernon, R., Vranken, W.F., Vries, S.D. de, Vuister, G.W., Wu, B., Yang, Y., Bonvin, A.M., Rosato, A., Aramini, J.M., Arrowsmith, C., Bagaria, A., Baker, D., Cavalli, A., Doreleijers, J., Eletsky, A., Giachetti, A., Guerry, P., Gutmanas, A., Guntert, P., He, Y., Herrmann, T., Huang, Y.J., Jaravine, V., Jonker, H.R., Kennedy, M.A., Lange, O.F., Liu, G., Malliavin, T.E., Mani, R., Mao, B., Montelione, G.T., Nilges, M., Rossi, P., Schot, G. van der, Schwalbe, H., Szyperski, T.A., Vendruscolo, M., Vernon, R., Vranken, W.F., Vries, S.D. de, Vuister, G.W., Wu, B., Yang, Y., and Bonvin, A.M.

Abstract

Item does not contain fulltext, The protocols currently used for protein structure determination by nuclear magnetic resonance (NMR) depend on the determination of a large number of upper distance limits for proton-proton pairs. Typically, this task is performed manually by an experienced researcher rather than automatically by using a specific computer program. To assess whether it is indeed possible to generate in a fully automated manner NMR structures adequate for deposition in the Protein Data Bank, we gathered 10 experimental data sets with unassigned nuclear Overhauser effect spectroscopy (NOESY) peak lists for various proteins of unknown structure, computed structures for each of them using different, fully automatic programs, and compared the results to each other and to the manually solved reference structures that were not available at the time the data were provided. This constitutes a stringent "blind" assessment similar to the CASP and CAPRI initiatives. This study demonstrates the feasibility of routine, fully automated protein structure determination by NMR.

Published
2012

29. CASD-NMR: critical assessment of automated structure determination by NMR.

Author

Rosato, A., Bagaria, A., Baker, D., Bardiaux, B., Cavalli, A., Doreleijers, J., Giachetti, A., Guerry, P., Guntert, P., Herrmann, T., Huang, Y.J., Jonker, H.R., Mao, B., Malliavin, T.E., Montelione, G.T., Nilges, M., Raman, S., Schot, G. van der, Vranken, W.F., Vuister, G.W., Bonvin, A.M., Rosato, A., Bagaria, A., Baker, D., Bardiaux, B., Cavalli, A., Doreleijers, J., Giachetti, A., Guerry, P., Guntert, P., Herrmann, T., Huang, Y.J., Jonker, H.R., Mao, B., Malliavin, T.E., Montelione, G.T., Nilges, M., Raman, S., Schot, G. van der, Vranken, W.F., Vuister, G.W., and Bonvin, A.M.

Abstract

Contains fulltext : 75259.pdf (publisher's version ) (Closed access)

Published
2009

31. RECOORD: a Recalculated COORdinates Database of 500+ proteins from PDB using restraints from the BioMagResBank

Author

NMR-spectroscopie, NMR Spectroscopy 1, Dep Scheikunde, Nederveen, A.J., Doreleijers, J.F., Vranken, W., Miller, Z., Spronk, C.A.E.M., Nabuurs, S.B., Guntert, P., Livny, M., Markley, J.L., Nilges, M., Ulrich, E.L., Kaptein, R., Bonvin, A.M.J.J., NMR-spectroscopie, NMR Spectroscopy 1, Dep Scheikunde, Nederveen, A.J., Doreleijers, J.F., Vranken, W., Miller, Z., Spronk, C.A.E.M., Nabuurs, S.B., Guntert, P., Livny, M., Markley, J.L., Nilges, M., Ulrich, E.L., Kaptein, R., and Bonvin, A.M.J.J.

Published
2005

35. Solution structure of Polytheonamide B

Author

Hamada, N., primary, Matsunaga, S., additional, Fujiwara, M., additional, Fujjita, K., additional, Hirota, H., additional, Schmucki, R., additional, Guntert, P., additional, and Fusetani, N., additional

Published
2010
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36. Structure of the Cdt1 C-terminal domain

Author

Khayrutdinov, B.I., primary, Bae, W.J., additional, Yun, Y.M., additional, Tsuyama, T., additional, Kim, J.J., additional, Hwang, E., additional, Ryu, K.-S., additional, Cheong, H.-K., additional, Cheong, C., additional, Karplus, P.A., additional, Guntert, P., additional, Tada, S., additional, Jeon, Y.H., additional, and Cho, Y., additional

Published
2009
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40. Solution structure of the second RNA recognition motif (RRM) of TIA-1

Author

Takahashi, M., primary, Kuwasako, K., additional, Abe, C., additional, Tsuda, K., additional, Inoue, M., additional, Terada, T., additional, Shirouzu, M., additional, Kobayashi, N., additional, Kigawa, T., additional, Taguchi, S., additional, Guntert, P., additional, Hayashizaki, Y., additional, Tanaka, A., additional, Muto, Y., additional, and Yokoyama, S., additional

Published
2008
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