Lex of areas and in the parietal cortex. As well, we are aware that variations in the part of the visual field in which the stimuli are presented, as well as variations in the density and duration of dots, could have led to variations in preference, as they do in discrimination thresholds [59]. But to make the study more manageable, we instead opted for a limited number of patterns, and used these to detect preferences and to correlate preferences with the strength of activity in early visual areas. The results given here edge us closer to understanding the relationship between identifiable Sch66336 site characteristics of a kinetic visual stimulus and its aesthetic rating. Whether the approach we have used in this study can, with modifications, be used for other types of visual stimulus, in the domains of form and colour, for example, remains to be seen. For the moment, we restrict ourselves to the conclusion that characteristics of kinetic stimuli can be identified that, when part of the kinetic work, make it preferable over others lacking these characteristics, and that the preference for these stimuli correlates with their capacity to elicit a stronger response from visual areas that are strongly activated by moving visual stimuli as well as from the field A1 of mOFC.rsob.royalsocietypublishing.org Open Biol 2:6. AcknowledgementsThis work was supported by the Wellcome Trust, London. We are indebted to Dominic ffytche, Stewart Shipp and members of the Wellcome Laboratory of Neurobiology for their critical reading of this manuscript.
Complexes containing SMC proteins play central roles in regulating key chromatin transactions during mitotic chromosome formation and segregation, in DNA repair, transcription and in partitioning the replicated genome. Although bacterial and archaeal SMC complexes typically involve homodimers [1,2], their eukaryotic counterparts consist of a heterodimer (SMC2/SMC4 in condensin, SMC1/SMC3 in cohesin and SMC5/SMC6 in the SMC5/6 complex) associated with three or more non-SMC subunits [3 ?]. Eukaryotic SMC proteins have a conserved architecture, with N- and C- globular `head’ domains at either end and a globular `hinge’ in the middle. The proteins fold back on themselves to create an approximately 45 nm-long intramolecular anti-parallel Sulfatinib site coiled-coil with the hinge domain at one end and the bipartite head domain at the other [9?2]. A variety of nonSMC subunits associate with this head domain. When the N- and C-terminal head segments pair with one another they assemble an ATP-binding cassettePresent address: Department of Clinical Sciences, Division of Infection Medicine, Lund University, 221 84 Lund, Sweden. Present address: The Jackson Laboratory for Genomic Medicine, 10 Discovery Drive, Farmington, CT 06030, USA. Electronic supplementary material is available at http://dx.doi.org/10.1098/rsob.150005.2015 The Authors. Published by the Royal Society under the terms of the Creative Commons AttributionLicense http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.(ABC)-type ATPase domain [9] that is characteristic for SMC proteins. The hinge domain mediates SMC protein dimerization, can bind DNA [13?5] and can transmit structural changes along the coiled-coil region to the head domains [11,16,17]. In condensin and cohesin, a wealth of evidence demonstrates that the two SMC proteins are packed side by side, with their paired hinge regions at one end and.Lex of areas and in the parietal cortex. As well, we are aware that variations in the part of the visual field in which the stimuli are presented, as well as variations in the density and duration of dots, could have led to variations in preference, as they do in discrimination thresholds [59]. But to make the study more manageable, we instead opted for a limited number of patterns, and used these to detect preferences and to correlate preferences with the strength of activity in early visual areas. The results given here edge us closer to understanding the relationship between identifiable characteristics of a kinetic visual stimulus and its aesthetic rating. Whether the approach we have used in this study can, with modifications, be used for other types of visual stimulus, in the domains of form and colour, for example, remains to be seen. For the moment, we restrict ourselves to the conclusion that characteristics of kinetic stimuli can be identified that, when part of the kinetic work, make it preferable over others lacking these characteristics, and that the preference for these stimuli correlates with their capacity to elicit a stronger response from visual areas that are strongly activated by moving visual stimuli as well as from the field A1 of mOFC.rsob.royalsocietypublishing.org Open Biol 2:6. AcknowledgementsThis work was supported by the Wellcome Trust, London. We are indebted to Dominic ffytche, Stewart Shipp and members of the Wellcome Laboratory of Neurobiology for their critical reading of this manuscript.
Complexes containing SMC proteins play central roles in regulating key chromatin transactions during mitotic chromosome formation and segregation, in DNA repair, transcription and in partitioning the replicated genome. Although bacterial and archaeal SMC complexes typically involve homodimers [1,2], their eukaryotic counterparts consist of a heterodimer (SMC2/SMC4 in condensin, SMC1/SMC3 in cohesin and SMC5/SMC6 in the SMC5/6 complex) associated with three or more non-SMC subunits [3 ?]. Eukaryotic SMC proteins have a conserved architecture, with N- and C- globular `head’ domains at either end and a globular `hinge’ in the middle. The proteins fold back on themselves to create an approximately 45 nm-long intramolecular anti-parallel coiled-coil with the hinge domain at one end and the bipartite head domain at the other [9?2]. A variety of nonSMC subunits associate with this head domain. When the N- and C-terminal head segments pair with one another they assemble an ATP-binding cassettePresent address: Department of Clinical Sciences, Division of Infection Medicine, Lund University, 221 84 Lund, Sweden. Present address: The Jackson Laboratory for Genomic Medicine, 10 Discovery Drive, Farmington, CT 06030, USA. Electronic supplementary material is available at http://dx.doi.org/10.1098/rsob.150005.2015 The Authors. Published by the Royal Society under the terms of the Creative Commons AttributionLicense http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.(ABC)-type ATPase domain [9] that is characteristic for SMC proteins. The hinge domain mediates SMC protein dimerization, can bind DNA [13?5] and can transmit structural changes along the coiled-coil region to the head domains [11,16,17]. In condensin and cohesin, a wealth of evidence demonstrates that the two SMC proteins are packed side by side, with their paired hinge regions at one end and.