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pro vyhledávání: '"Ulrich, E.L."'
Background: The nuclear magnetic resonance (NMR) spectroscopic data for biological macromolecules archived at the BioMagResBank (BMRB) provide a rich resource of biophysical information at atomic resolution. The NMR data archived in NMR-STAR ASCII fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______2127::28bb428fdbaccdd2502816aa981ffb60
https://pergamos.lib.uoa.gr/uoa/dl/object/uoadl:3070988
https://pergamos.lib.uoa.gr/uoa/dl/object/uoadl:3070988
Autor:
Doreleijers J.F., Vranken W.F., Schulte C., Markley J.L., Ulrich E.L., Vriend G., Vuister G.W.
Publikováno v:
UnpayWall
ORCID
Microsoft Academic Graph
NARCIS
Europe PubMed Central
PubMed Central
DANS (Data Archiving and Networked Services)
ICT FP7 Publications Database
Nucleic Acids Research, 40, D519-524
Nucleic Acids Research
ORCID
Microsoft Academic Graph
NARCIS
Europe PubMed Central
PubMed Central
DANS (Data Archiving and Networked Services)
ICT FP7 Publications Database
Nucleic Acids Research, 40, D519-524
Nucleic Acids Research
For many macromolecular NMR ensembles from the Protein Data Bank (PDB) the experiment-based restraint lists are available, while other experimental data, mainly chemical shift values, are often available from the BioMagResBank. The accuracy and preci
Autor:
Sali, A., Berman, H.M., Schwede, T., Trewhella, J., Kleywegt, G., Burley, S.K., Markley, J., Nakamura, H., Adams, P., Bonvin, A.M.J.J., Wah, C., Dal Peraro, M., Di Maio, F., Ferrin, T.E., Grünewald, K., Gutmanas, A., Henderson, R., Hummer, G., Iawsaki, K., Johnson, G., Lawson, C.L., Meiler, J., Marti-Renom, M.A., Montelione, G.T., Nilges, M., Nussinov, R., Patwardhan, A., Rappsilber, J., Read, R.J., Saibil, Helen R., Schröder, G.F., Schwieters, C., Seidel, C.A.M., Svergun, D., Topf, Maya, Ulrich, E.L., Velankar, S., Westbrook, J.D.
Structures of biomolecular systems are increasingly computed by integrative modeling that relies on varied types of experimental data and theoretical information. We describe here the proceedings and conclusions from the first wwPDB Hybrid/Integrativ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::e5c019dc3bb5464c457b3873c0a94391
https://eprints.bbk.ac.uk/id/eprint/12322/1/Sali_et_al_Structure_2015.pdf
https://eprints.bbk.ac.uk/id/eprint/12322/1/Sali_et_al_Structure_2015.pdf
Autor:
Doreleijers, J.F., Nederveen, A.J., Vranken, W., Lin, J., Bonvin, A.M.J.J., Kaptein, R., Markley, J.L., Ulrich, E.L., NMR-spectroscopie, NMR Spectroscopy 1, Dep Scheikunde
Publikováno v:
Journal of Biomolecular NMR, 32, 1. Springer Netherlands
Journal of biomolecular NMR, 32(1), 1-12. Springer Netherlands
Journal of biomolecular NMR, 32(1), 1-12. Springer Netherlands
We present two new databases of NMR-derived distance and dihedral angle restraints: the Database Of Converted Restraints (DOCR) and the Filtered Restraints Database (FRED). These databases currently correspond to 545 proteins with NMR structures depo
Autor:
Ulrich, E.L., Akutsu, H., Doreleijers, J., Harano, Y., Ioannidis, Y.E., Lin, J., Livny, M., Mading, S., Maziuk, D., Miller, Z., Nakatani, E., Schulte, C.F., Tolmie, D.E., Wenger, R.K., Yao, H., Markley, J.L.
Publikováno v:
Nucleic Acids Research, 36, D402-8
Nucleic Acids Research
Nucleic Acids Research, 36, Database issue, pp. D402-8
Nucleic Acids Research
Nucleic Acids Research, 36, Database issue, pp. D402-8
Contains fulltext : 70130.pdf (Publisher’s version ) (Open Access) The BioMagResBank (BMRB: www.bmrb.wisc.edu) is a repository for experimental and derived data gathered from nuclear magnetic resonance (NMR) spectroscopic studies of biological mole
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4653b9a2255a49811f6a594f6aaddfc
http://hdl.handle.net/2066/70130
http://hdl.handle.net/2066/70130
The BioMagResBank (BMRB: www.bmrb.wisc.edu ext-link) is a repository for experimental and derived data gathered from nuclear magnetic resonance (NMR) spectroscopic studies of biological molecules. BMRB is a partner in the Worldwide Protein Data Bank
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______2127::146f0df82aec02bfa3aaf793ddb8836c
https://pergamos.lib.uoa.gr/uoa/dl/object/uoadl:3094432
https://pergamos.lib.uoa.gr/uoa/dl/object/uoadl:3094432
Autor:
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
Publikováno v:
Proteins, 59(4), 662-672. Wiley-Liss Inc.
Proteins: Structure function and bioinformatics, 59, 662. Wiley-Liss Inc.
Proteins-Structure Function and Bioinformatics, 59, 662-72
Proteins-Structure Function and Bioinformatics, 59, 4, pp. 662-72
Proteins: Structure function and bioinformatics, 59, 662. Wiley-Liss Inc.
Proteins-Structure Function and Bioinformatics, 59, 662-72
Proteins-Structure Function and Bioinformatics, 59, 4, pp. 662-72
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 we
Autor:
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.
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 restra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______101::e693c1dc408addbc222d83406b68b394
https://dspace.library.uu.nl/handle/1874/14804
https://dspace.library.uu.nl/handle/1874/14804
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