http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
The Vertical Corporate Campus: Integrating Modern Workplace Models into the High-Rise Typology
Britton, John,Hargis, Steve Council on Tall Building and Urban Habitat Korea 2016 International journal of high-rise buildings Vol.5 No.2
As the great urban migration continues to drive the growth of cities worldwide, global companies are seeking new approaches to the urban workplace and corporate campus. In light of environmental and economic imperatives to develop taller and denser central business districts, a key challenge is merging contemporary workplace concepts, which emphasize large, open floors and high levels of connectivity, with high-rise typologies with smaller floor plates set around center cores. This paper traces the evolution of the corporate campus and emerging design strategies for translating contemporary workplace models into a vertical campus typology that allows companies to realize the benefits of urban locations, while contributing to a more sustainable future.
Muts Homolog Sliding Clamps Shield the DNA from Binding Proteins
Hanne, Jeungphill,Britton, Brooke M.,Park, Jonghyun,Liu, Jiaquan,Martin-Lopez, Juana,Jones, Nathan,Schoffner, Matthew,Klajner, Piotr,Bundschuh, Ralf,Lee, Jong-Bong,Fishel, Richard Published for the Biophysical Society by the Rocke 2019 Biophysical journal Vol.116 No.3
MutS homolog sliding clamps shield the DNA from binding proteins
Hanne, Jeungphill,Britton, Brooke M.,Park, Jonghyun,Liu, Jiaquan,Martí,n-Lí,ó,pez, Juana,Jones, Nathan,Schoffner, Matthew,Klajner, Piotr,Bundschuh, Ralf,Lee, Jong-Bong,Fishel, Richar American Society for Biochemistry and Molecular Bi 2018 The Journal of biological chemistry Vol.293 No.37
<P>Sliding clamps on DNA consist of evolutionarily conserved enzymes that coordinate DNA replication, repair, and the cellular DNA damage response. MutS homolog (MSH) proteins initiate mismatch repair (MMR) by recognizing mispaired nucleotides and in the presence of ATP form stable sliding clamps that randomly diffuse along the DNA. The MSH sliding clamps subsequently load MutL homolog (MLH/PMS) proteins that form a second extremely stable sliding clamp, which together coordinate downstream MMR components with the excision-initiation site that may be hundreds to thousands of nucleotides distant from the mismatch. Specific or nonspecific binding of other proteins to the DNA between the mismatch and the distant excision-initiation site could conceivably obstruct the free diffusion of these MMR sliding clamps, inhibiting their ability to initiate repair. Here, we employed bulk biochemical analysis, single-molecule fluorescence imaging, and mathematical modeling to determine how sliding clamps might overcome such hindrances along the DNA. Using both bacterial and human MSH proteins, we found that increasing the number of MSH sliding clamps on a DNA decreased the association of the Escherichia coli transcriptional repressor LacI to its cognate promoter LacO. Our results suggest a simple mechanism whereby thermal diffusion of MSH sliding clamps along the DNA alters the association kinetics of other DNA-binding proteins over extended distances. These observations appear generally applicable to any stable sliding clamp that forms on DNA.</P>
Luan, Qinmeng,Britton, T. Benjamin,Jun, Tea-Sung Elsevier 2018 Materials science & engineering. properties, micro Vol.734 No.-
<P><B>Abstract</B></P> <P>Titanium alloys are widely used in light weight applications such as jet engine fans, where their mechanical performance under a range of loading regimes is important. Titanium alloys are mechanically anisotropic with respect to crystallographic orientation, and remarkably titanium creeps at room temperature. This means that the strain rate sensitivity (SRS) and stress relaxation performance are critical in predicting component life. In this work, we focus on systematically exploring the macroscopic SRS of Grade 1 commercially pure titanium (CP Ti) with varying grain sizes and texture using uniaxial compression. Briefly, we find that Ti samples had positive SRS and samples compressed along the sheet rolling direction (RD) (i.e. soft grains dominant) were less rate sensitive than bars compressed along the sheet normal direction (ND) (i.e. hard grains dominant). We attribute this rate sensitivity to the relative activity of slip and twinning. Within the grain size range of ~ 317 ± 7 μ m , we observe an increase in the rate sensitivity, where volume fraction of { 10 1 ̅ 2 } < 10 1 ̅ 1 > T1 tensile twins was low, and the twin width at different strain rates were similar. These observations imply that the macroscopic rate sensitivity is controlled by the ensemble behaviour of local deformation processes: the amount of slips accumulated at grain boundaries affects the SRS, which is grain size and texture dependent. We hope that this experimental study motivates mechanistic modelling studies using crystal plasticity, including strain rate sensitivity and twinning, to predict the performance of titanium alloys.</P>
The sensitivity of respondent‐driven sampling
Lu, Xin,Bengtsson, Linus,Britton, Tom,Camitz, Martin,Kim, Beom Jun,Thorson, Anna,Liljeros, Fredrik Blackwell Publishing Ltd 2012 JOURNAL OF THE ROYAL STATISTICAL SOCIETY SERIES A- Vol.175 No.1
<P><B>Summary. </B> Researchers in many scientific fields make inferences from individuals to larger groups. For many groups, however, there is no list of members from which to draw a random sample. Respondent‐driven sampling (RDS) is a relatively new sampling methodology that circumvents this difficulty by using the social networks of the groups under study. The RDS method has been shown to provide unbiased estimates of population proportions given certain conditions. The method is now widely used in human immunodeficiency virus related studies among high risk populations globally. We test the RDS methodology by simulating RDS studies on the social networks of a large Lesbian, gay, bisexual and transgender Web community. The robustness of the RDS method is tested by violating, one by one, the conditions under which the method provides unbiased estimates. Simulations indicate that the bias is large if networks are directed or respondents choose to invite people on the basis of characteristics that are correlated with the study outcomes. The bias and variance increase if participants invite close as opposed to more distant friends whereas sampling in denser networks sharply reduces variance. However, the RDS method shows strong resistance to sampling without replacement, low response rates and certain errors in the participants’ reporting of their network sizes, as well as the selection criteria of seeds. The effects of network structure and the number of seeds and coupons are also discussed.</P>
Cascading MutS and MutL sliding clamps control DNA diffusion to activate mismatch repair
Liu, Jiaquan,Hanne, Jeungphill,Britton, Brooke M.,Bennett, Jared,Kim, Daehyung,Lee, Jong-Bong,Fishel, Richard Nature Publishing Group, a division of Macmillan P 2016 Nature Vol.539 No.7630
<P>Mismatched nucleotides arise from polymerase misincorporation errors, recombination between heteroallelic parents and chemical or physical DNA damage(1). Highly conserved MutS (MSH) and MutL (MLH/PMS) homologues initiate mismatch repair and, in higher eukaryotes, act as DNA damage sensors that can trigger apoptosis(2). Defects in human mismatch repair genes cause Lynch syndrome or hereditary non-polyposis colorectal cancer and 10-40% of related sporadic tumours(3). However, the collaborative mechanics of MSH and MLH/PMS proteins have not been resolved in any organism. We visualized Escherichia coli (Ec) ensemble mismatch repair and confirmed that EcMutS mismatch recognition results in the formation of stable ATP-bound sliding clamps that randomly diffuse along the DNA with intermittent backbone contact. The EcMutS sliding clamps act as a platform to recruit EcMutL onto the mismatched DNA, forming an EcMutS-EcMutL search complex that then closely follows the DNA backbone. ATP binding by EcMutL establishes a second long-lived DNA clamp that oscillates between the principal EcMutS-EcMutL search complex and unrestricted EcMutS and EcMutL sliding clamps. The EcMutH endonuclease that targets mismatch repair excision only binds clamped EcMutL, increasing its DNA association kinetics by more than 1,000-fold. The assembly of an EcMutS-EcMutL-EcMutH search complex illustrates how sequential stable sliding clamps can modulate one-dimensional diffusion mechanics along the DNA to direct mismatch repair.</P>