The Experts below are selected from a list of 15723 Experts worldwide ranked by ideXlab platform
Elizabeth Parks - One of the best experts on this subject based on the ideXlab platform.
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engaging the discourse of international language recognition through iso 639 3 signed language Change requests
Critical Inquiry in Language Studies, 2015Co-Authors: Elizabeth ParksAbstract:Linguistic ideologies that are left unquestioned and unexplored, especially as reflected and produced in marginalized language communities, can contribute to inequality made real in decisions about languages and the people who use them. One of the primary bodies of knowledge guiding international language policy is the International Organization for Standardization (ISO) 639-3 Registry of Languages. I explore the impact of international language recognition through a Critical Discourse Analysis of proposed Registry Change requests related to a specific type of minority language: signed language. I describe key social actors involved in the international discourse of signed language recognition, types of knowledge used to promote distinct signed languages, naming strategies for those distinct entities, and ways that these processes are creating current social reality for signed language users around the world. Ultimately, I argue for deeper exploration of intersecting “deaf” and “sign language” identities,...
Chaok Seok - One of the best experts on this subject based on the ideXlab platform.
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How Does a Registry Change in Dynein’s Coiled-Coil Stalk Drive Binding of Dynein to Microtubules?
Biochemistry, 2011Co-Authors: Jung-hyun Choi, Hahnbeom Park, Chaok SeokAbstract:Dynein is a motor protein that transports cellular cargo along the microtubule (MT) by consuming ATP. Dynein’s microtubule-binding domain (MTBD) is separated from the ATP-binding core by a ∼15 nm stalk that consists of two α-helices forming an antiparallel coiled coil. It was previously suggested that the coiled-coil stalk creates a Registry shift to modulate its binding affinity for MT. A crystal structure of the low-affinity form of MTBD was determined, but that of the high-affinity form with the Registry shift is not yet available. In this study, we obtained an all-atom model structure for the high-affinity form of MTBD bound to MT by an anisotropic network model, protein–protein docking, and molecular dynamics simulations. We observe that the magnitude of the coiled-coil helix sliding is dramatically reduced near the two prolines that form the stalk–MTBD boundary and subsequently transformed to cyclic movements of MTBD helices, leading to formation of a new salt bridge with MT at the binding interface...
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how does a Registry Change in dynein s coiled coil stalk drive binding of dynein to microtubules
Biochemistry, 2011Co-Authors: Jung-hyun Choi, Hahnbeom Park, Chaok SeokAbstract:Dynein is a motor protein that transports cellular cargo along the microtubule (MT) by consuming ATP. Dynein’s microtubule-binding domain (MTBD) is separated from the ATP-binding core by a ∼15 nm stalk that consists of two α-helices forming an antiparallel coiled coil. It was previously suggested that the coiled-coil stalk creates a Registry shift to modulate its binding affinity for MT. A crystal structure of the low-affinity form of MTBD was determined, but that of the high-affinity form with the Registry shift is not yet available. In this study, we obtained an all-atom model structure for the high-affinity form of MTBD bound to MT by an anisotropic network model, protein–protein docking, and molecular dynamics simulations. We observe that the magnitude of the coiled-coil helix sliding is dramatically reduced near the two prolines that form the stalk–MTBD boundary and subsequently transformed to cyclic movements of MTBD helices, leading to formation of a new salt bridge with MT at the binding interface...
Jung-hyun Choi - One of the best experts on this subject based on the ideXlab platform.
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How Does a Registry Change in Dynein’s Coiled-Coil Stalk Drive Binding of Dynein to Microtubules?
Biochemistry, 2011Co-Authors: Jung-hyun Choi, Hahnbeom Park, Chaok SeokAbstract:Dynein is a motor protein that transports cellular cargo along the microtubule (MT) by consuming ATP. Dynein’s microtubule-binding domain (MTBD) is separated from the ATP-binding core by a ∼15 nm stalk that consists of two α-helices forming an antiparallel coiled coil. It was previously suggested that the coiled-coil stalk creates a Registry shift to modulate its binding affinity for MT. A crystal structure of the low-affinity form of MTBD was determined, but that of the high-affinity form with the Registry shift is not yet available. In this study, we obtained an all-atom model structure for the high-affinity form of MTBD bound to MT by an anisotropic network model, protein–protein docking, and molecular dynamics simulations. We observe that the magnitude of the coiled-coil helix sliding is dramatically reduced near the two prolines that form the stalk–MTBD boundary and subsequently transformed to cyclic movements of MTBD helices, leading to formation of a new salt bridge with MT at the binding interface...
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how does a Registry Change in dynein s coiled coil stalk drive binding of dynein to microtubules
Biochemistry, 2011Co-Authors: Jung-hyun Choi, Hahnbeom Park, Chaok SeokAbstract:Dynein is a motor protein that transports cellular cargo along the microtubule (MT) by consuming ATP. Dynein’s microtubule-binding domain (MTBD) is separated from the ATP-binding core by a ∼15 nm stalk that consists of two α-helices forming an antiparallel coiled coil. It was previously suggested that the coiled-coil stalk creates a Registry shift to modulate its binding affinity for MT. A crystal structure of the low-affinity form of MTBD was determined, but that of the high-affinity form with the Registry shift is not yet available. In this study, we obtained an all-atom model structure for the high-affinity form of MTBD bound to MT by an anisotropic network model, protein–protein docking, and molecular dynamics simulations. We observe that the magnitude of the coiled-coil helix sliding is dramatically reduced near the two prolines that form the stalk–MTBD boundary and subsequently transformed to cyclic movements of MTBD helices, leading to formation of a new salt bridge with MT at the binding interface...
Hahnbeom Park - One of the best experts on this subject based on the ideXlab platform.
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How Does a Registry Change in Dynein’s Coiled-Coil Stalk Drive Binding of Dynein to Microtubules?
Biochemistry, 2011Co-Authors: Jung-hyun Choi, Hahnbeom Park, Chaok SeokAbstract:Dynein is a motor protein that transports cellular cargo along the microtubule (MT) by consuming ATP. Dynein’s microtubule-binding domain (MTBD) is separated from the ATP-binding core by a ∼15 nm stalk that consists of two α-helices forming an antiparallel coiled coil. It was previously suggested that the coiled-coil stalk creates a Registry shift to modulate its binding affinity for MT. A crystal structure of the low-affinity form of MTBD was determined, but that of the high-affinity form with the Registry shift is not yet available. In this study, we obtained an all-atom model structure for the high-affinity form of MTBD bound to MT by an anisotropic network model, protein–protein docking, and molecular dynamics simulations. We observe that the magnitude of the coiled-coil helix sliding is dramatically reduced near the two prolines that form the stalk–MTBD boundary and subsequently transformed to cyclic movements of MTBD helices, leading to formation of a new salt bridge with MT at the binding interface...
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how does a Registry Change in dynein s coiled coil stalk drive binding of dynein to microtubules
Biochemistry, 2011Co-Authors: Jung-hyun Choi, Hahnbeom Park, Chaok SeokAbstract:Dynein is a motor protein that transports cellular cargo along the microtubule (MT) by consuming ATP. Dynein’s microtubule-binding domain (MTBD) is separated from the ATP-binding core by a ∼15 nm stalk that consists of two α-helices forming an antiparallel coiled coil. It was previously suggested that the coiled-coil stalk creates a Registry shift to modulate its binding affinity for MT. A crystal structure of the low-affinity form of MTBD was determined, but that of the high-affinity form with the Registry shift is not yet available. In this study, we obtained an all-atom model structure for the high-affinity form of MTBD bound to MT by an anisotropic network model, protein–protein docking, and molecular dynamics simulations. We observe that the magnitude of the coiled-coil helix sliding is dramatically reduced near the two prolines that form the stalk–MTBD boundary and subsequently transformed to cyclic movements of MTBD helices, leading to formation of a new salt bridge with MT at the binding interface...
Paul W Wales - One of the best experts on this subject based on the ideXlab platform.
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Change of outcomes in pediatric intestinal failure use of time series analysis to assess the evolution of an intestinal rehabilitation program
Journal of The American College of Surgeons, 2016Co-Authors: Carol Oliveira, Nicole De Silva, Sanja Stanojevic, Yaron Avitzur, Ahmed M Bayoumi, Wendy J Ungar, Jeffrey S Hoch, Paul W WalesAbstract:Background The clinical picture of pediatric intestinal failure has Changed over the past 15 years, while effectiveness evolving treatment options remains unclear. This study explored evolution in care and quantified independent effects of new treatment options. Study Design Consecutive patients (n = 196) with neonatal or infantile intestinal failure, born between July 1996 and December 2011, were derived from an intestinal rehabilitation program (IRP) patient Registry. Change over time was analyzed using multivariable Box-Jenkins method-based autoregressive integrative moving average models (ARIMA), robust linear regression, and nonparametric trend analysis. Four systematically introduced treatment options (IRP, serial transverse enteroplasty, omega-3 lipid emulsions, and ethanol locks) were evaluated. Analyses were adjusted for patient characteristics and disease severity. The primary outcome was disease-specific mortality from liver failure and sepsis. Secondary outcomes included parenteral nutrition weaning, transplantations, catheter complications, and liver disease. Results Patient characteristics remained unChanged over time, except for decreasing small bowel length (−0.5%/quarter; 95% CI −0.85, −0.16) and ICU admission time (−0.6 days/quarter; 95% CI −1.03, −0.18). Disease-specific mortality diminished significantly over time (−0.02 deaths/quarter; 95% CI −0.03, −0.01) by IRP and omega-3 lipids introduction (−0.6 deaths/quarter each, 95% CI −1.23, −0.02 and −0.77, −0.45, respectively). Serial transverse enteroplasty and ethanol locks had no significant impact. Parenteral nutrition weaning and transplantations remained unChanged, while catheter sepsis and complication rates decreased by 0.3 episodes/1,000 catheter-days each (95% CI −0.43, −0.2 and −0.45, −0.24, respectively). Conclusions Introduction of IRP and omega-3 lipids independently decreased disease-specific mortality. For the first time, time series analysis was applied to evaluate effectiveness of treatment options in intestinal rehabilitation.