[{"date_updated":"2021-01-12T08:16:37Z","extern":"1","type":"journal_article","article_type":"original","status":"public","_id":"8028","issue":"46","volume":25,"publication_status":"published","publication_identifier":{"issn":["0270-6474","1529-2401"]},"language":[{"iso":"eng"}],"main_file_link":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6725859/","open_access":"1"}],"intvolume":" 25","month":"11","abstract":[{"lang":"eng","text":"Transmission of signals within the brain is essential for cognitive function, but it is not clear how neural circuits support reliable and accurate signal propagation over a sufficiently large dynamic range. Two modes of propagation have been studied: synfire chains, in which synchronous activity travels through feedforward layers of a neuronal network, and the propagation of fluctuations in firing rate across these layers. In both cases, a sufficient amount of noise, which was added to previous models from an external source, had to be included to support stable propagation. Sparse, randomly connected networks of spiking model neurons can generate chaotic patterns of activity. We investigate whether this activity, which is a more realistic noise source, is sufficient to allow for signal transmission. We find that, for rate-coded signals but not for synfire chains, such networks support robust and accurate signal reproduction through up to six layers if appropriate adjustments are made in synaptic strengths. We investigate the factors affecting transmission and show that multiple signals can propagate simultaneously along different pathways. Using this feature, we show how different types of logic gates can arise within the architecture of the random network through the strengthening of specific synapses."}],"oa_version":"Published Version","pmid":1,"article_processing_charge":"No","external_id":{"pmid":["16291952"]},"author":[{"full_name":"Vogels, Tim P","orcid":"0000-0003-3295-6181","last_name":"Vogels","id":"CB6FF8D2-008F-11EA-8E08-2637E6697425","first_name":"Tim P"},{"first_name":"L. F.","last_name":"Abbott","full_name":"Abbott, L. F."}],"title":"Signal propagation and logic gating in networks of integrate-and-fire neurons","citation":{"ista":"Vogels TP, Abbott LF. 2005. Signal propagation and logic gating in networks of integrate-and-fire neurons. Journal of Neuroscience. 25(46), 10786–10795.","chicago":"Vogels, Tim P, and L. F. Abbott. “Signal Propagation and Logic Gating in Networks of Integrate-and-Fire Neurons.” Journal of Neuroscience. Society for Neuroscience, 2005. https://doi.org/10.1523/jneurosci.3508-05.2005.","apa":"Vogels, T. P., & Abbott, L. F. (2005). Signal propagation and logic gating in networks of integrate-and-fire neurons. Journal of Neuroscience. Society for Neuroscience. https://doi.org/10.1523/jneurosci.3508-05.2005","ama":"Vogels TP, Abbott LF. Signal propagation and logic gating in networks of integrate-and-fire neurons. Journal of Neuroscience. 2005;25(46):10786-10795. doi:10.1523/jneurosci.3508-05.2005","ieee":"T. P. Vogels and L. F. Abbott, “Signal propagation and logic gating in networks of integrate-and-fire neurons,” Journal of Neuroscience, vol. 25, no. 46. Society for Neuroscience, pp. 10786–10795, 2005.","short":"T.P. Vogels, L.F. Abbott, Journal of Neuroscience 25 (2005) 10786–10795.","mla":"Vogels, Tim P., and L. F. Abbott. “Signal Propagation and Logic Gating in Networks of Integrate-and-Fire Neurons.” Journal of Neuroscience, vol. 25, no. 46, Society for Neuroscience, 2005, pp. 10786–95, doi:10.1523/jneurosci.3508-05.2005."},"user_id":"D865714E-FA4E-11E9-B85B-F5C5E5697425","page":"10786-10795","date_created":"2020-06-25T13:12:33Z","date_published":"2005-11-16T00:00:00Z","doi":"10.1523/jneurosci.3508-05.2005","year":"2005","publication":"Journal of Neuroscience","day":"16","oa":1,"publisher":"Society for Neuroscience","quality_controlled":"1"},{"user_id":"D865714E-FA4E-11E9-B85B-F5C5E5697425","citation":{"ista":"Vogels TP, Rajan K, Abbott LF. 2005. Neural network dynamics. Annual Review of Neuroscience. 28(1), 357–376.","chicago":"Vogels, Tim P, Kanaka Rajan, and L.F. Abbott. “Neural Network Dynamics.” Annual Review of Neuroscience. Annual Reviews, 2005. https://doi.org/10.1146/annurev.neuro.28.061604.135637.","short":"T.P. Vogels, K. Rajan, L.F. Abbott, Annual Review of Neuroscience 28 (2005) 357–376.","ieee":"T. P. Vogels, K. Rajan, and L. F. Abbott, “Neural network dynamics,” Annual Review of Neuroscience, vol. 28, no. 1. Annual Reviews, pp. 357–376, 2005.","ama":"Vogels TP, Rajan K, Abbott LF. Neural network dynamics. Annual Review of Neuroscience. 2005;28(1):357-376. doi:10.1146/annurev.neuro.28.061604.135637","apa":"Vogels, T. P., Rajan, K., & Abbott, L. F. (2005). Neural network dynamics. Annual Review of Neuroscience. Annual Reviews. https://doi.org/10.1146/annurev.neuro.28.061604.135637","mla":"Vogels, Tim P., et al. “Neural Network Dynamics.” Annual Review of Neuroscience, vol. 28, no. 1, Annual Reviews, 2005, pp. 357–76, doi:10.1146/annurev.neuro.28.061604.135637."},"title":"Neural network dynamics","external_id":{"pmid":["16022600"]},"article_processing_charge":"No","author":[{"last_name":"Vogels","full_name":"Vogels, Tim P","orcid":"0000-0003-3295-6181","first_name":"Tim P","id":"CB6FF8D2-008F-11EA-8E08-2637E6697425"},{"first_name":"Kanaka","last_name":"Rajan","full_name":"Rajan, Kanaka"},{"full_name":"Abbott, L.F.","last_name":"Abbott","first_name":"L.F."}],"quality_controlled":"1","publisher":"Annual Reviews","publication":"Annual Review of Neuroscience","day":"21","year":"2005","date_created":"2020-06-25T13:13:11Z","date_published":"2005-07-21T00:00:00Z","doi":"10.1146/annurev.neuro.28.061604.135637","page":"357-376","_id":"8029","status":"public","type":"journal_article","article_type":"review","extern":"1","date_updated":"2021-01-12T08:16:37Z","pmid":1,"oa_version":"None","abstract":[{"text":"Neural network modeling is often concerned with stimulus-driven responses, but most of the activity in the brain is internally generated. Here, we review network models of internally generated activity, focusing on three types of network dynamics: (a) sustained responses to transient stimuli, which provide a model of working memory; (b) oscillatory network activity; and (c) chaotic activity, which models complex patterns of background spiking in cortical and other circuits. We also review propagation of stimulus-driven activity through spontaneously active networks. Exploring these aspects of neural network dynamics is critical for understanding how neural circuits produce cognitive function.","lang":"eng"}],"intvolume":" 28","month":"07","language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"issn":["0147-006X","1545-4126"]},"issue":"1","volume":28},{"publisher":"Elsevier","quality_controlled":"1","oa":1,"date_published":"2005-01-26T00:00:00Z","doi":"10.1016/j.cub.2005.01.008","date_created":"2021-06-07T10:24:30Z","page":"154-159","day":"26","publication":"Current Biology","year":"2005","title":"DNA methylation profiling identifies CG methylation clusters in Arabidopsis genes","author":[{"full_name":"Tran, Robert K.","last_name":"Tran","first_name":"Robert K."},{"first_name":"Jorja G.","full_name":"Henikoff, Jorja G.","last_name":"Henikoff"},{"full_name":"Zilberman, Daniel","orcid":"0000-0002-0123-8649","last_name":"Zilberman","id":"6973db13-dd5f-11ea-814e-b3e5455e9ed1","first_name":"Daniel"},{"first_name":"Renata F.","full_name":"Ditt, Renata F.","last_name":"Ditt"},{"first_name":"Steven E.","full_name":"Jacobsen, Steven E.","last_name":"Jacobsen"},{"last_name":"Henikoff","full_name":"Henikoff, Steven","first_name":"Steven"}],"external_id":{"pmid":["15668172 "]},"article_processing_charge":"No","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","citation":{"ista":"Tran RK, Henikoff JG, Zilberman D, Ditt RF, Jacobsen SE, Henikoff S. 2005. DNA methylation profiling identifies CG methylation clusters in Arabidopsis genes. Current Biology. 15(2), 154–159.","chicago":"Tran, Robert K., Jorja G. Henikoff, Daniel Zilberman, Renata F. Ditt, Steven E. Jacobsen, and Steven Henikoff. “DNA Methylation Profiling Identifies CG Methylation Clusters in Arabidopsis Genes.” Current Biology. Elsevier, 2005. https://doi.org/10.1016/j.cub.2005.01.008.","ama":"Tran RK, Henikoff JG, Zilberman D, Ditt RF, Jacobsen SE, Henikoff S. DNA methylation profiling identifies CG methylation clusters in Arabidopsis genes. Current Biology. 2005;15(2):154-159. doi:10.1016/j.cub.2005.01.008","apa":"Tran, R. K., Henikoff, J. G., Zilberman, D., Ditt, R. F., Jacobsen, S. E., & Henikoff, S. (2005). DNA methylation profiling identifies CG methylation clusters in Arabidopsis genes. Current Biology. Elsevier. https://doi.org/10.1016/j.cub.2005.01.008","short":"R.K. Tran, J.G. Henikoff, D. Zilberman, R.F. Ditt, S.E. Jacobsen, S. Henikoff, Current Biology 15 (2005) 154–159.","ieee":"R. K. Tran, J. G. Henikoff, D. Zilberman, R. F. Ditt, S. E. Jacobsen, and S. Henikoff, “DNA methylation profiling identifies CG methylation clusters in Arabidopsis genes,” Current Biology, vol. 15, no. 2. Elsevier, pp. 154–159, 2005.","mla":"Tran, Robert K., et al. “DNA Methylation Profiling Identifies CG Methylation Clusters in Arabidopsis Genes.” Current Biology, vol. 15, no. 2, Elsevier, 2005, pp. 154–59, doi:10.1016/j.cub.2005.01.008."},"month":"01","intvolume":" 15","scopus_import":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cub.2005.01.008"}],"oa_version":"Published Version","pmid":1,"abstract":[{"lang":"eng","text":"Cytosine DNA methylation in vertebrates is widespread, but methylation in plants is found almost exclusively at transposable elements and repetitive DNA [1]. Within regions of methylation, methylcytosines are typically found in CG, CNG, and asymmetric contexts. CG sites are maintained by a plant homolog of mammalian Dnmt1 acting on hemi-methylated DNA after replication. Methylation of CNG and asymmetric sites appears to be maintained at each cell cycle by other mechanisms. We report a new type of DNA methylation in Arabidopsis, dense CG methylation clusters found at scattered sites throughout the genome. These clusters lack non-CG methylation and are preferentially found in genes, although they are relatively deficient toward the 5′ end. CG methylation clusters are present in lines derived from different accessions and in mutants that eliminate de novo methylation, indicating that CG methylation clusters are stably maintained at specific sites. Because 5-methylcytosine is mutagenic, the appearance of CG methylation clusters over evolutionary time predicts a genome-wide deficiency of CG dinucleotides and an excess of C(A/T)G trinucleotides within transcribed regions. This is exactly what we find, implying that CG methylation clusters have contributed profoundly to plant gene evolution. We suggest that CG methylation clusters silence cryptic promoters that arise sporadically within transcription units."}],"issue":"2","volume":15,"language":[{"iso":"eng"}],"publication_identifier":{"eissn":["1879-0445"],"issn":["0960-9822"]},"publication_status":"published","status":"public","type":"journal_article","article_type":"original","_id":"9491","department":[{"_id":"DaZi"}],"extern":"1","date_updated":"2021-12-14T09:12:26Z"},{"scopus_import":"1","main_file_link":[{"url":"https://doi.org/10.1186/gb-2005-6-11-r90","open_access":"1"}],"month":"10","intvolume":" 6","abstract":[{"lang":"eng","text":"Background:\r\nDNA methylation occurs at preferred sites in eukaryotes. In Arabidopsis, DNA cytosine methylation is maintained by three subfamilies of methyltransferases with distinct substrate specificities and different modes of action. Targeting of cytosine methylation at selected loci has been found to sometimes involve histone H3 methylation and small interfering (si)RNAs. However, the relationship between different cytosine methylation pathways and their preferred targets is not known.\r\nResults:\r\nWe used a microarray-based profiling method to explore the involvement of Arabidopsis CMT3 and DRM DNA methyltransferases, a histone H3 lysine-9 methyltransferase (KYP) and an Argonaute-related siRNA silencing component (AGO4) in methylating target loci. We found that KYP targets are also CMT3 targets, suggesting that histone methylation maintains CNG methylation genome-wide. CMT3 and KYP targets show similar proximal distributions that correspond to the overall distribution of transposable elements of all types, whereas DRM targets are distributed more distally along the chromosome. We find an inverse relationship between element size and loss of methylation in ago4 and drm mutants.\r\nConclusion:\r\nWe conclude that the targets of both DNA methylation and histone H3K9 methylation pathways are transposable elements genome-wide, irrespective of element type and position. Our findings also suggest that RNA-directed DNA methylation is required to silence isolated elements that may be too small to be maintained in a silent state by a chromatin-based mechanism alone. Thus, parallel pathways would be needed to maintain silencing of transposable elements."}],"pmid":1,"oa_version":"Published Version","issue":"11","volume":6,"publication_identifier":{"eissn":["1465-6906"],"issn":["1474-760X"]},"publication_status":"published","language":[{"iso":"eng"}],"article_type":"original","type":"journal_article","status":"public","_id":"9514","department":[{"_id":"DaZi"}],"date_updated":"2021-12-14T09:09:41Z","extern":"1","quality_controlled":"1","publisher":"Springer Nature","oa":1,"date_published":"2005-10-19T00:00:00Z","doi":"10.1186/gb-2005-6-11-r90","date_created":"2021-06-07T13:12:41Z","year":"2005","day":"19","publication":"Genome Biology","article_number":"R90","author":[{"first_name":"Robert K.","last_name":"Tran","full_name":"Tran, Robert K."},{"id":"6973db13-dd5f-11ea-814e-b3e5455e9ed1","first_name":"Daniel","orcid":"0000-0002-0123-8649","full_name":"Zilberman, Daniel","last_name":"Zilberman"},{"full_name":"de Bustos, Cecilia","last_name":"de Bustos","first_name":"Cecilia"},{"first_name":"Renata F.","full_name":"Ditt, Renata F.","last_name":"Ditt"},{"first_name":"Jorja G.","full_name":"Henikoff, Jorja G.","last_name":"Henikoff"},{"first_name":"Anders M.","full_name":"Lindroth, Anders M.","last_name":"Lindroth"},{"first_name":"Jeffrey","last_name":"Delrow","full_name":"Delrow, Jeffrey"},{"full_name":"Boyle, Tom","last_name":"Boyle","first_name":"Tom"},{"last_name":"Kwong","full_name":"Kwong, Samson","first_name":"Samson"},{"last_name":"Bryson","full_name":"Bryson, Terri D.","first_name":"Terri D."},{"first_name":"Steven E.","full_name":"Jacobsen, Steven E.","last_name":"Jacobsen"},{"first_name":"Steven","last_name":"Henikoff","full_name":"Henikoff, Steven"}],"article_processing_charge":"No","external_id":{"pmid":["16277745"]},"title":"Chromatin and siRNA pathways cooperate to maintain DNA methylation of small transposable elements in Arabidopsis","citation":{"mla":"Tran, Robert K., et al. “Chromatin and SiRNA Pathways Cooperate to Maintain DNA Methylation of Small Transposable Elements in Arabidopsis.” Genome Biology, vol. 6, no. 11, R90, Springer Nature, 2005, doi:10.1186/gb-2005-6-11-r90.","ama":"Tran RK, Zilberman D, de Bustos C, et al. Chromatin and siRNA pathways cooperate to maintain DNA methylation of small transposable elements in Arabidopsis. Genome Biology. 2005;6(11). doi:10.1186/gb-2005-6-11-r90","apa":"Tran, R. K., Zilberman, D., de Bustos, C., Ditt, R. F., Henikoff, J. G., Lindroth, A. M., … Henikoff, S. (2005). Chromatin and siRNA pathways cooperate to maintain DNA methylation of small transposable elements in Arabidopsis. Genome Biology. Springer Nature. https://doi.org/10.1186/gb-2005-6-11-r90","short":"R.K. Tran, D. Zilberman, C. de Bustos, R.F. Ditt, J.G. Henikoff, A.M. Lindroth, J. Delrow, T. Boyle, S. Kwong, T.D. Bryson, S.E. Jacobsen, S. Henikoff, Genome Biology 6 (2005).","ieee":"R. K. Tran et al., “Chromatin and siRNA pathways cooperate to maintain DNA methylation of small transposable elements in Arabidopsis,” Genome Biology, vol. 6, no. 11. Springer Nature, 2005.","chicago":"Tran, Robert K., Daniel Zilberman, Cecilia de Bustos, Renata F. Ditt, Jorja G. Henikoff, Anders M. Lindroth, Jeffrey Delrow, et al. “Chromatin and SiRNA Pathways Cooperate to Maintain DNA Methylation of Small Transposable Elements in Arabidopsis.” Genome Biology. Springer Nature, 2005. https://doi.org/10.1186/gb-2005-6-11-r90.","ista":"Tran RK, Zilberman D, de Bustos C, Ditt RF, Henikoff JG, Lindroth AM, Delrow J, Boyle T, Kwong S, Bryson TD, Jacobsen SE, Henikoff S. 2005. Chromatin and siRNA pathways cooperate to maintain DNA methylation of small transposable elements in Arabidopsis. Genome Biology. 6(11), R90."},"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9"},{"publication":"Human Molecular Genetics","day":"01","year":"2005","publication_status":"published","date_created":"2018-12-11T11:48:48Z","volume":14,"date_published":"2005-11-01T00:00:00Z","doi":"10.1093/hmg/ddi350","issue":"21","page":"3191 - 3201","abstract":[{"text":"The impact of an amino acid replacement on the organism's fitness can vary from lethal to selectively neutral and even, in rare cases, beneficial. Substantial data are available on either pathogenic or acceptable replacements. However, the whole distribution of coefficients of selection against individual replacements is not known for any organism. To ascertain this distribution for human proteins, we combined data on pathogenic missense mutations, on human non-synonymous SNPs and on human-chimpanzee divergence of orthologous proteins. Fractions of amino acid replacements which reduce fitness by >10-2, 10-2-10-4, 10-4-10-5 and <10-5 are 25, 49, 14 and 12%, respectively. On average, the strength of selection against a replacement is substantially higher when chemically dissimilar amino acids are involved, and the Grantham's index of a replacement explains 35% of variance in the average logarithm of selection coefficients associated with different replacements. Still, the impact of a replacement depends on its context within the protein more than on its own nature. Reciprocal replacements are often associated with rather different selection coefficients, in particular, replacements of non-polar amino acids with polar ones are typically much more deleterious than replacements in the opposite direction. However, differences between evolutionary fluxes of reciprocal replacements are only weakly correlated with the differences between the corresponding selection coefficients.","lang":"eng"}],"intvolume":" 14","month":"11","publisher":"Oxford University Press","quality_controlled":0,"extern":1,"citation":{"chicago":"Yampolsky, Lev, Fyodor Kondrashov, and Alexey Kondrashov. “Distribution of the Strength of Selection against Amino Acid Replacements in Human Proteins.” Human Molecular Genetics. Oxford University Press, 2005. https://doi.org/10.1093/hmg/ddi350.","ista":"Yampolsky L, Kondrashov F, Kondrashov A. 2005. Distribution of the strength of selection against amino acid replacements in human proteins. Human Molecular Genetics. 14(21), 3191–3201.","mla":"Yampolsky, Lev, et al. “Distribution of the Strength of Selection against Amino Acid Replacements in Human Proteins.” Human Molecular Genetics, vol. 14, no. 21, Oxford University Press, 2005, pp. 3191–201, doi:10.1093/hmg/ddi350.","ieee":"L. Yampolsky, F. Kondrashov, and A. Kondrashov, “Distribution of the strength of selection against amino acid replacements in human proteins,” Human Molecular Genetics, vol. 14, no. 21. Oxford University Press, pp. 3191–3201, 2005.","short":"L. Yampolsky, F. Kondrashov, A. Kondrashov, Human Molecular Genetics 14 (2005) 3191–3201.","apa":"Yampolsky, L., Kondrashov, F., & Kondrashov, A. (2005). Distribution of the strength of selection against amino acid replacements in human proteins. Human Molecular Genetics. Oxford University Press. https://doi.org/10.1093/hmg/ddi350","ama":"Yampolsky L, Kondrashov F, Kondrashov A. Distribution of the strength of selection against amino acid replacements in human proteins. Human Molecular Genetics. 2005;14(21):3191-3201. doi:10.1093/hmg/ddi350"},"date_updated":"2021-01-12T08:19:13Z","title":"Distribution of the strength of selection against amino acid replacements in human proteins","publist_id":"6807","author":[{"first_name":"Lev","full_name":"Yampolsky, Lev Y","last_name":"Yampolsky"},{"last_name":"Kondrashov","full_name":"Fyodor Kondrashov","orcid":"0000-0001-8243-4694","first_name":"Fyodor","id":"44FDEF62-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Alexey","full_name":"Kondrashov, Alexey S","last_name":"Kondrashov"}],"_id":"843","status":"public","type":"journal_article"},{"month":"12","intvolume":" 33","quality_controlled":"1","publisher":"Springer Nature","oa_version":"None","abstract":[{"lang":"eng","text":"Fast multidimensional NMR with a time resolution of a few seconds provides a new tool for high throughput screening and site-resolved real-time studies of kinetic molecular processes by NMR. Recently we have demonstrated the feasibility to record protein 1H–15N correlation spectra in a few seconds of acquisition time using a new SOFAST-HMQC experiment (Schanda and Brutscher (2005) J. Am. Chem. Soc. 127, 8014). Here, we investigate in detail the performance of SOFAST-HMQC to record 1H–15N and 1H−13C correlation spectra of proteins of different size and at different magnetic field strengths. Compared to standard 1H–15N correlation experiments SOFAST-HMQC provides a significant gain in sensitivity, especially for fast repetition rates. Guidelines are provided on how to set up SOFAST-HMQC experiments for a given protein sample. In addition, an alternative pulse scheme, IPAP-SOFAST-HMQC is presented that allows application on NMR spectrometers equipped with cryogenic probes, and fast measurement of one-bond 1H–13C and 1H–15N scalar and residual dipolar coupling constants."}],"issue":"4","volume":33,"date_published":"2005-12-01T00:00:00Z","doi":"10.1007/s10858-005-4425-x","date_created":"2020-09-18T10:13:59Z","page":"199-211","day":"01","language":[{"iso":"eng"}],"publication":"Journal of Biomolecular NMR","publication_identifier":{"issn":["0925-2738","1573-5001"]},"publication_status":"published","year":"2005","status":"public","keyword":["Spectroscopy","Biochemistry"],"article_type":"original","type":"journal_article","_id":"8491","title":"SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds","author":[{"full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul"},{"full_name":"Kupče, Ēriks","last_name":"Kupče","first_name":"Ēriks"},{"full_name":"Brutscher, Bernhard","last_name":"Brutscher","first_name":"Bernhard"}],"article_processing_charge":"No","extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","citation":{"ista":"Schanda P, Kupče Ē, Brutscher B. 2005. SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds. Journal of Biomolecular NMR. 33(4), 199–211.","chicago":"Schanda, Paul, Ēriks Kupče, and Bernhard Brutscher. “SOFAST-HMQC Experiments for Recording Two-Dimensional Deteronuclear Correlation Spectra of Proteins within a Few Seconds.” Journal of Biomolecular NMR. Springer Nature, 2005. https://doi.org/10.1007/s10858-005-4425-x.","short":"P. Schanda, Ē. Kupče, B. Brutscher, Journal of Biomolecular NMR 33 (2005) 199–211.","ieee":"P. Schanda, Ē. Kupče, and B. Brutscher, “SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds,” Journal of Biomolecular NMR, vol. 33, no. 4. Springer Nature, pp. 199–211, 2005.","apa":"Schanda, P., Kupče, Ē., & Brutscher, B. (2005). SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-005-4425-x","ama":"Schanda P, Kupče Ē, Brutscher B. SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds. Journal of Biomolecular NMR. 2005;33(4):199-211. doi:10.1007/s10858-005-4425-x","mla":"Schanda, Paul, et al. “SOFAST-HMQC Experiments for Recording Two-Dimensional Deteronuclear Correlation Spectra of Proteins within a Few Seconds.” Journal of Biomolecular NMR, vol. 33, no. 4, Springer Nature, 2005, pp. 199–211, doi:10.1007/s10858-005-4425-x."},"date_updated":"2021-01-12T08:19:38Z"},{"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"status":"public","article_type":"original","type":"journal_article","_id":"8492","title":"Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds","article_processing_charge":"No","author":[{"last_name":"Schanda","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"first_name":"Bernhard","full_name":"Brutscher, Bernhard","last_name":"Brutscher"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","citation":{"ama":"Schanda P, Brutscher B. Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. Journal of the American Chemical Society. 2005;127(22):8014-8015. doi:10.1021/ja051306e","apa":"Schanda, P., & Brutscher, B. (2005). Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja051306e","ieee":"P. Schanda and B. Brutscher, “Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds,” Journal of the American Chemical Society, vol. 127, no. 22. American Chemical Society, pp. 8014–8015, 2005.","short":"P. Schanda, B. Brutscher, Journal of the American Chemical Society 127 (2005) 8014–8015.","mla":"Schanda, Paul, and Bernhard Brutscher. “Very Fast Two-Dimensional NMR Spectroscopy for Real-Time Investigation of Dynamic Events in Proteins on the Time Scale of Seconds.” Journal of the American Chemical Society, vol. 127, no. 22, American Chemical Society, 2005, pp. 8014–15, doi:10.1021/ja051306e.","ista":"Schanda P, Brutscher B. 2005. Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. Journal of the American Chemical Society. 127(22), 8014–8015.","chicago":"Schanda, Paul, and Bernhard Brutscher. “Very Fast Two-Dimensional NMR Spectroscopy for Real-Time Investigation of Dynamic Events in Proteins on the Time Scale of Seconds.” Journal of the American Chemical Society. American Chemical Society, 2005. https://doi.org/10.1021/ja051306e."},"date_updated":"2021-01-12T08:19:39Z","intvolume":" 127","month":"05","publisher":"American Chemical Society","quality_controlled":"1","oa_version":"None","abstract":[{"lang":"eng","text":"We demonstrate for different protein samples that 2D 1H−15N correlation NMR spectra can be recorded in a few seconds of acquisition time using a new band-selective optimized flip-angle short-transient heteronuclear multiple quantum coherence experiment. This has enabled us to measure fast hydrogen−deuterium exchange rate constants along the backbone of a small globular protein fragment by real-time 2D NMR."}],"date_created":"2020-09-18T10:14:05Z","issue":"22","date_published":"2005-05-14T00:00:00Z","volume":127,"doi":"10.1021/ja051306e","page":"8014-8015","language":[{"iso":"eng"}],"publication":"Journal of the American Chemical Society","day":"14","year":"2005","publication_status":"published","publication_identifier":{"issn":["0002-7863","1520-5126"]}},{"_id":"8516","status":"public","keyword":["Analysis"],"article_type":"original","type":"journal_article","extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2021-01-12T08:19:49Z","citation":{"mla":"Bourgain, Jean, and Vadim Kaloshin. “On Diffusion in High-Dimensional Hamiltonian Systems.” Journal of Functional Analysis, vol. 229, no. 1, Elsevier, 2005, pp. 1–61, doi:10.1016/j.jfa.2004.09.006.","ama":"Bourgain J, Kaloshin V. On diffusion in high-dimensional Hamiltonian systems. Journal of Functional Analysis. 2005;229(1):1-61. doi:10.1016/j.jfa.2004.09.006","apa":"Bourgain, J., & Kaloshin, V. (2005). On diffusion in high-dimensional Hamiltonian systems. Journal of Functional Analysis. Elsevier. https://doi.org/10.1016/j.jfa.2004.09.006","short":"J. Bourgain, V. Kaloshin, Journal of Functional Analysis 229 (2005) 1–61.","ieee":"J. Bourgain and V. Kaloshin, “On diffusion in high-dimensional Hamiltonian systems,” Journal of Functional Analysis, vol. 229, no. 1. Elsevier, pp. 1–61, 2005.","chicago":"Bourgain, Jean, and Vadim Kaloshin. “On Diffusion in High-Dimensional Hamiltonian Systems.” Journal of Functional Analysis. Elsevier, 2005. https://doi.org/10.1016/j.jfa.2004.09.006.","ista":"Bourgain J, Kaloshin V. 2005. On diffusion in high-dimensional Hamiltonian systems. Journal of Functional Analysis. 229(1), 1–61."},"title":"On diffusion in high-dimensional Hamiltonian systems","author":[{"first_name":"Jean","last_name":"Bourgain","full_name":"Bourgain, Jean"},{"full_name":"Kaloshin, Vadim","orcid":"0000-0002-6051-2628","last_name":"Kaloshin","first_name":"Vadim","id":"FE553552-CDE8-11E9-B324-C0EBE5697425"}],"article_processing_charge":"No","oa_version":"None","abstract":[{"text":"The purpose of this paper is to construct examples of diffusion for E-Hamiltonian perturbations\r\nof completely integrable Hamiltonian systems in 2d-dimensional phase space, with d large.\r\nIn the first part of the paper, simple and explicit examples are constructed illustrating absence\r\nof ‘long-time’ stability for size E Hamiltonian perturbations of quasi-convex integrable systems\r\nalready when the dimension 2d of phase space becomes as large as log 1/E . We first produce\r\nthe example in Gevrey class and then a real analytic one, with some additional work.\r\nIn the second part, we consider again E-Hamiltonian perturbations of completely integrable\r\nHamiltonian system in 2d-dimensional space with E-small but not too small, |E| > exp(−d), with\r\nd the number of degrees of freedom assumed large. It is shown that for a class of analytic\r\ntime-periodic perturbations, there exist linearly diffusing trajectories. The underlying idea for\r\nboth examples is similar and consists in coupling a fixed degree of freedom with a large\r\nnumber of them. The procedure and analytical details are however significantly different. As\r\nmentioned, the construction in Part I is totally elementary while Part II is more involved, relying\r\nin particular on the theory of normally hyperbolic invariant manifolds, methods of generating\r\nfunctions, Aubry–Mather theory, and Mather’s variational methods.","lang":"eng"}],"month":"12","intvolume":" 229","quality_controlled":"1","publisher":"Elsevier","day":"01","publication":"Journal of Functional Analysis","language":[{"iso":"eng"}],"publication_identifier":{"issn":["0022-1236"]},"publication_status":"published","year":"2005","volume":229,"doi":"10.1016/j.jfa.2004.09.006","date_published":"2005-12-01T00:00:00Z","issue":"1","date_created":"2020-09-18T10:49:06Z","page":"1-61"},{"citation":{"short":"F. Kondrashov, Biofizika 50 (2005) 389–395.","ieee":"F. Kondrashov, “The analysis of monomer sequences in protein and tRNA and the manifestation of the compensation of pathogenic deviations in their evolution,” Biofizika, vol. 50, no. 3. Pleiades Publishing, pp. 389–395, 2005.","ama":"Kondrashov F. The analysis of monomer sequences in protein and tRNA and the manifestation of the compensation of pathogenic deviations in their evolution. Biofizika. 2005;50(3):389-395.","apa":"Kondrashov, F. (2005). The analysis of monomer sequences in protein and tRNA and the manifestation of the compensation of pathogenic deviations in their evolution. Biofizika. Pleiades Publishing.","mla":"Kondrashov, Fyodor. “The Analysis of Monomer Sequences in Protein and TRNA and the Manifestation of the Compensation of Pathogenic Deviations in Their Evolution.” Biofizika, vol. 50, no. 3, Pleiades Publishing, 2005, pp. 389–95.","ista":"Kondrashov F. 2005. The analysis of monomer sequences in protein and tRNA and the manifestation of the compensation of pathogenic deviations in their evolution. Biofizika. 50(3), 389–395.","chicago":"Kondrashov, Fyodor. “The Analysis of Monomer Sequences in Protein and TRNA and the Manifestation of the Compensation of Pathogenic Deviations in Their Evolution.” Biofizika. Pleiades Publishing, 2005."},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publist_id":"6769","author":[{"last_name":"Kondrashov","full_name":"Kondrashov, Fyodor","orcid":"0000-0001-8243-4694","first_name":"Fyodor","id":"44FDEF62-F248-11E8-B48F-1D18A9856A87"}],"article_processing_charge":"No","external_id":{"pmid":["15977826"]},"title":"The analysis of monomer sequences in protein and tRNA and the manifestation of the compensation of pathogenic deviations in their evolution","publisher":"Pleiades Publishing","quality_controlled":"1","year":"2005","day":"01","publication":"Biofizika","page":"389 - 395","date_published":"2005-05-01T00:00:00Z","date_created":"2018-12-11T11:48:58Z","_id":"877","article_type":"original","type":"journal_article","status":"public","date_updated":"2021-01-12T08:21:01Z","extern":"1","abstract":[{"text":"Sequence analysis of protein and mitochondrially encoded tRNA genes shows that substitutions\r\nproducing pathogenic effects in humans are often found in normal, healthy individuals from other species.\r\nAnalysis of stability of protein and tRNA structures shows that the disease-causing effects of pathogenic\r\nmutations can be neutralized by other, compensatory substitutions that restore the structural stability of the\r\nmolecule. Further study of such substitutions will, hopefully, lead to new methods for curing genetic dis-\r\neases that may be based on the correction of molecule stability as a whole instead of reversing an individual\r\npathogenic mutation.","lang":"eng"}],"oa_version":"None","pmid":1,"main_file_link":[{"url":"http://pleiades.online/abstract/biophys/5/biophys0349_abstract.pdf"}],"month":"05","intvolume":" 50","publication_status":"published","language":[{"iso":"eng"}],"issue":"3","volume":50},{"extern":1,"citation":{"chicago":"Kondrashov, Fyodor. “In Search of the Limits of Evolution.” Nature Genetics. Nature Publishing Group, 2005. https://doi.org/10.1038/ng0105-9.","ista":"Kondrashov F. 2005. In search of the limits of evolution. Nature Genetics. 37(1), 9–10.","mla":"Kondrashov, Fyodor. “In Search of the Limits of Evolution.” Nature Genetics, vol. 37, no. 1, Nature Publishing Group, 2005, pp. 9–10, doi:10.1038/ng0105-9.","apa":"Kondrashov, F. (2005). In search of the limits of evolution. Nature Genetics. Nature Publishing Group. https://doi.org/10.1038/ng0105-9","ama":"Kondrashov F. In search of the limits of evolution. Nature Genetics. 2005;37(1):9-10. doi:10.1038/ng0105-9","short":"F. Kondrashov, Nature Genetics 37 (2005) 9–10.","ieee":"F. Kondrashov, “In search of the limits of evolution,” Nature Genetics, vol. 37, no. 1. Nature Publishing Group, pp. 9–10, 2005."},"date_updated":"2021-01-12T08:21:02Z","title":"In search of the limits of evolution","author":[{"full_name":"Fyodor Kondrashov","orcid":"0000-0001-8243-4694","last_name":"Kondrashov","first_name":"Fyodor","id":"44FDEF62-F248-11E8-B48F-1D18A9856A87"}],"publist_id":"6770","_id":"878","status":"public","type":"journal_article","publication":"Nature Genetics","day":"01","publication_status":"published","year":"2005","date_created":"2018-12-11T11:48:59Z","date_published":"2005-01-01T00:00:00Z","issue":"1","doi":"10.1038/ng0105-9","volume":37,"page":"9 - 10","abstract":[{"text":"Negative trade-offs are thought to be a pervasive phenomenon and to inhibit evolution at all levels. New evidence shows that at the molecular level, there may be no trade-offs preventing the emergence of an enzyme with multiple functions.\n","lang":"eng"}],"intvolume":" 37","month":"01","quality_controlled":0,"publisher":"Nature Publishing Group"}]