cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.5281/zenodo.1342541
title: Human Family With Sequence Similarity 83 Member B (Fam83B); A Target Enabling Package

description: FAM83A-H are newly identified oncogenes characterised by a conserved DUF1669 domain. FAM83B can substitute for RAS to promote malignant transformation. Ablation of FAM83B or mutation of Lys230 inhibits malignant phenotypes, implicating FAM83B as potential therapeutic target. As part of this TEP, we solved the first crystal structures from the FAM83 family, including FAM83A and FAM83B. The structures of the DUF1669 domain reveal a phospholipase D-like fold lacking conservation of key catalytic residues. We deorphanise the FAM83 DUF1669 domain as a critical docking scaffold for binding of casein kinase 1 isoforms. Finally, using XChem fragment screening we report chemical fragments that bind to Lys230 in the central pocket of the DUF1669 and form starting points for potential drug development.
description: Further versions of this document will contain experimental data about the FAM83 TEP.
DOI: 10.5281/zenodo.1344502
title: Human Receptor-Interacting Serine/Threonine-Protein Kinase 2 (Ripk2); A Target Enabling Package

description: RIPK2 inflammatory signalling downstream from the bacteria-sensing receptors NOD1 and NOD2 is associated with auto-immune and inflammatory conditions. RIPK2 inhibition has shown promise in disease models of inflammatory bowel disease and multiple sclerosis. In this TEP, we reveal a lack of correlation between inhibitor efficacy in cells and their potency using in vitro kinase assays. We show that RIPK2 kinase activity is in fact dispensable for NOD2 inflammatory signalling and that RIPK2 inhibitors function instead by antagonizing XIAP-binding and ubiquitination of RIPK2. We characterise the molecular basis for this effect. We also solved the first crystal structure of the RIPK2 kinase domain and applied a range of biochemical and cellular assays to profile type I and type II RIPK2 kinase inhibitors. Overall, our study illustrates how to target the ATP-binding pocket in RIPK2 to interfere with the RIPK2-XIAP interaction for modulation of NOD signalling.
description: Future versions of this document will contain experimental data for the RIPK2 TEP.
DOI: 10.5281/zenodo.1344544
title: Human Family With Sequence Similarity 83 Member B (Fam83B); A Target Enabling Package

description: FAM83A-H are newly identified oncogenes characterised by a conserved DUF1669 domain. FAM83B can substitute for RAS to promote malignant transformation. Ablation of FAM83B or mutation of Lys230 inhibits malignant phenotypes, implicating FAM83B as potential therapeutic target. As part of this TEP, we solved the first crystal structures from the FAM83 family, including FAM83A and FAM83B. The structures of the DUF1669 domain reveal a phospholipase D-like fold lacking conservation of key catalytic residues. We deorphanise the FAM83 DUF1669 domain as a critical docking scaffold for binding of casein kinase 1 isoforms. Finally, using XChem fragment screening we report chemical fragments that bind to Lys230 in the central pocket of the DUF1669 and form starting points for potential drug development.
DOI: 10.5517/ccdc.csd.cc1qcp92
title: CCDC 1590154: Experimental Crystal Structure Determination

description: Related Article: Yekai Huang,  Yanan Li,  Jianan Sun,  Jindong Li,  Zhenggen Zha,  and Zhiyong Wang|2018|J.Org.Chem.|83|8464|doi:10.1021/acs.joc.8b01057
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc1z722c
title: CCDC 1824042: Experimental Crystal Structure Determination

description: Related Article: Buddhadeb Mondal,  Rajendra Maity,  and Subhas Chandra Pan|2018|J.Org.Chem.|83|8645|doi:10.1021/acs.joc.8b00781
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc1zbx4c
title: CCDC 1827733: Experimental Crystal Structure Determination

description: Related Article: Xin-Gang Wang, Yuke Li, Lu-Lu Zhang, Bo-Sheng Zhang, Qiang Wang, Jun-Wei Ma, Yong-Min Liang|2018|Chem.Commun.|54|9541|doi:10.1039/C8CC05067H
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc1zf0gw
title: CCDC 1829758: Experimental Crystal Structure Determination

description: Related Article: Pavel A. Sakharov,  Mikhail S. Novikov,  and Alexander F. Khlebnikov|2018|J.Org.Chem.|83|8304|doi:10.1021/acs.joc.8b01004
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc1zfp58
title: CCDC 1830400: Experimental Crystal Structure Determination

description: Related Article: Xia Song,  Cai Gao,  Bin Li,  Xinying Zhang,  and Xuesen Fan|2018|J.Org.Chem.|83|8509|doi:10.1021/acs.joc.8b01098
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc1zgpmr
title: CCDC 1831375: Experimental Crystal Structure Determination

description: Related Article: Narendra Kumar Vaishanv,  Ashis Kumar Gupta,  Ruchir Kant,  and Kishor Mohanan|2018|J.Org.Chem.|83|8759|doi:10.1021/acs.joc.8b01074
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.17632/2vd7mpx94m.1
title: Test Problems' Data Sets

description: This data sets were generated as the test problems for evaluating the performance of the proposed mixed-integer programming model as well as the Genetic Algorithm hybridized with variable neighborhood search. The first, second and third columns show the problem number, the station number and the stations' demands in bins, respectively.
DOI: 10.17632/56w858dr9j.1
title: Acceptance and Gamification Models of the Agon Framework, an Acceptance Requirements Framework Based on Gamification

description: We have been interested in developing a generic framework for modelling, analyzing and fulfilling acceptance requirements for software systems through gamification [Piras, 2016, 2017]. Our objective is to support the systematic design of engaging software that meets acceptance requirements. To meet our objective we conducted a wide review of the literature to select the most important, effective and representative user acceptance models [Ajzen, 1991, Compeau et al., 1999, Davis, 1986, Davis et al., 1992, Moore and Benbasat, 1991, Sheppard et al., 1988, Taylor and Todd, 1995, Thompson et al., 1991, Venkatesh and Davis, 2000, Venkatesh et al., 2003]. We have integrated elements of existing models to create an Acceptance Model based on goal modeling techniques [Chung et al., 2012, Horkoff et al., 2017, Li et al., 2013, Mylopoulos et al., 1992]. This model gives a generic characterization of the problem space for acceptance requirements. We have also developed a Gamification Model [Piras, 2016, 2017] that defines a design space for gamified solutions to acceptance requirements, also through a literature review. This model includes gamification concepts such as point systems (i.e., experience, redeemable, skill, karma, reputation and training points), badges, leader-boards, levels, paths, gamified training (i.e., suggestions, tricks, tours, tutorials, training paths), gamified market (i.e., rewards and market policies of redeeming, making gifts, purchasing), game roles, powers, unlockable powers, gamified community [Deterding et al., 2011, Hamari, 2015, Schell, 2014, Zichermann and Cunningham, 2011], etc., and the alternative choices a designer has when designing a gamified solution [Deterding et al., 2011, Hamari, 2015, Schell, 2014, Zichermann and Cunningham, 2011]. Our framework, named Agon5, recognizes the importance of understanding game mechanics and dynamics by applying well-known gamification patterns and guidelines Schell [2014], Zichermann and Cunningham [2011] in producing an effective gamified design. In order to obtain more details and the description of such models, the Agon Framework and its method, "Acceptance Requirements Analysis Based on Gamification", please read the following published papers: - L. Piras, E. Paja, P. Giorgini and J. Mylopoulos, “Goal Models for Acceptance Requirements Analysis and Gamification Design”, in 36th International Conference on Conceptual Modeling (ER), Springer, Valencia (Spain), 2017. - L. Piras, E. Paja, R. Cuel, D. Ponte, P. Giorgini and J. Mylopoulos, “Gamification Solutions for Software Acceptance: A Comparative Study of Requirements Engineering and Organizational Behavior Techniques”, in 11th IEEE International Conference on Research Challenges in Information Science (RCIS), IEEE, Brighton (UK), 2017. - L. Piras, P. Giorgini, and J. Mylopoulos, “Acceptance Requirements and their Gamification Solutions”, in 24th IEEE International Requirements Engineering Conference (RE), IEEE, Beijing, 2016.
DOI: 10.17632/9srzngjb9v.1
title: Data for: Reshaping gut microbiota mitigates lead-led memory impairment through a novel H3K27me3-based mechanism in female rats
DOI: 10.17632/scz4c488x5.3
title: Data sets and their analysis for: Modeling stochastic optimal portfolio of partitioned projects financed by loan within a flexible time horizon

description: Our model is examined based on an extensive data set. The values of model parameters are generated randomly using discrete uniform distribution.
DOI: 10.5255/ukda-sn-7555-3
title: Opinions and Lifestyle Survey, Transport Issues Module, February - April 2013
DOI: 10.5255/ukda-sn-7571-4
title: Opinions and Lifestyle Survey, Electric Vehicles Module, February 2014 and February 2015
DOI: 10.5255/ukda-sn-7572-3
title: Opinions and Lifestyle Survey, Internet Access Module, January, February and March, 2014
DOI: 10.5517/ccdc.csd.cc1zgyky
title: CCDC 1831621: Experimental Crystal Structure Determination

description: Related Article: Narendra Kumar Vaishanv,  Ashis Kumar Gupta,  Ruchir Kant,  and Kishor Mohanan|2018|J.Org.Chem.|83|8759|doi:10.1021/acs.joc.8b01074
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc1zhgb8
title: CCDC 1832110: Experimental Crystal Structure Determination

description: Related Article: Sergey V. Zaytsev,  Konstantin L. Ivanov,  Dmitry A. Skvortsov,  Stanislav I. Bezzubov,  Mikhail Ya. Melnikov,  and Ekaterina M. Budynina|2018|J.Org.Chem.|83|8695|doi:10.1021/acs.joc.8b00922
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc1zk4zn
title: CCDC 1833742: Experimental Crystal Structure Determination

description: Related Article: Annaram Thirupathi,  Manojkumar Janni,  and Saravanan Peruncheralathan|2018|J.Org.Chem.|83|8668|doi:10.1021/acs.joc.8b00816
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc1zk50q
title: CCDC 1833743: Experimental Crystal Structure Determination

description: Related Article: Annaram Thirupathi,  Manojkumar Janni,  and Saravanan Peruncheralathan|2018|J.Org.Chem.|83|8668|doi:10.1021/acs.joc.8b00816
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc1zlckh
title: CCDC 1834907: Experimental Crystal Structure Determination

description: Related Article: Jian Li,  Shuhua Bai,  Yang Li,  Zhengbing Wang,  Xiaoyu Huo,  and Li Liu|2018|J.Org.Chem.|83|8780|doi:10.1021/acs.joc.8b01120
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc1zlclj
title: CCDC 1834908: Experimental Crystal Structure Determination

description: Related Article: Jian Li,  Shuhua Bai,  Yang Li,  Zhengbing Wang,  Xiaoyu Huo,  and Li Liu|2018|J.Org.Chem.|83|8780|doi:10.1021/acs.joc.8b01120
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc1zlcmk
title: CCDC 1834909: Experimental Crystal Structure Determination

description: Related Article: Jian Li,  Shuhua Bai,  Yang Li,  Zhengbing Wang,  Xiaoyu Huo,  and Li Liu|2018|J.Org.Chem.|83|8780|doi:10.1021/acs.joc.8b01120
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc1zmy5q
title: CCDC 1836414: Experimental Crystal Structure Determination

description: Related Article: Muhammad Yousaf, Ximena Zarate, Eduardo Schott, Alan J. Lough, Bryan D. Koivisto|2018|RSC Advances|8|28533|doi:10.1039/C8RA03384F
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc1zmy6r
title: CCDC 1836415: Experimental Crystal Structure Determination

description: Related Article: Muhammad Yousaf, Ximena Zarate, Eduardo Schott, Alan J. Lough, Bryan D. Koivisto|2018|RSC Advances|8|28533|doi:10.1039/C8RA03384F
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.17632/7gzbgs4bsr.1
title: Relationships of adiponectin to regional adiposity, insulin sensitivity, serum lipids and inflammatory markers in sedentary and endurance-trained Japanese young women

description: The raw data required to reproduce the findings of “Relationships of adiponectin to regional adiposity, insulin sensitivity, serum lipids and inflammatory markers in sedentary and endurance-trained Japanese young women”
DOI: 10.17632/mbrgjzbz5n.1
title: Road kill vertebrates southcentral Kansas 1980's

description: This study measured the frequency of vertebrates killed by vehicle collisions along stretch of two-lane highway in Kansas between 1985-1987. These data are the basis for a paper published in Transactions of Kansas Academy of Science, 2018, 121: 69-83. Data in columns record year, month and date (A, B, C), name of individual animal and group assigned (D and E), the location tenth mile section from specific intersections and segment number (F and G), adjacent land-use (agriculture, pasture, residential, woodland) on north, south or both sides (H, I and J), culvert (none, small or large) on one side or both (K and L), tree (none, one or more, hedgerow) on both sides of road (M and N), house (none, one or more than one) on both sides of road (O and P), intersection present or not (Q), water (R) and barn (S). The methodology led to high accuracy in number of animals found, a particular high mortality frequency for box turtles, snakes, rabbits and small rodents. The data stored here can be used for examining trends in wildlife road mortality at broader scales or overtime.
DOI: 10.17632/nkk3wcdnky.1
title: Fatigue of a polycrystalline nickel based superalloy: numerical simulation and physical experiment

description: Thermo-mechanical fatigue of a polycrystalline nickel based superalloy was studied by numerical simulation and physical experiment in order to understand effects of temperature, applied stress, and processing residual stress on microstructure degeneration and mechanical deterioration of key components in aircraft engine.
DOI: 10.5255/ukda-sn-7460-3
title: Opinions and Lifestyle Survey, Public Perceptions of Tax Compliance Module, May 2012 - March 2013
DOI: 10.5255/ukda-sn-7494-3
title: Opinions and Lifestyle Survey, Court Fees Module, April and May 2013
DOI: 10.5255/ukda-sn-7498-3
title: Opinions and Lifestyle Survey, Disability Monitoring Module, July, August, September, November and December, 2012
DOI: 10.5255/ukda-sn-7524-3
title: Opinions and Lifestyle Survey, Well-Being Module, May - December, 2013 and January and February 2014
DOI: 10.5255/ukda-sn-7554-3
title: Opinions and Lifestyle Survey, Charitable Giving Module, August and November 2012 and February 2013
DOI: 10.5281/zenodo.1344545
title: Human Receptor-Interacting Serine/Threonine-Protein Kinase 2 (Ripk2); A Target Enabling Package

description: RIPK2 inflammatory signalling downstream from the bacteria-sensing receptors NOD1 and NOD2 is associated with auto-immune and inflammatory conditions. RIPK2 inhibition has shown promise in disease models of inflammatory bowel disease and multiple sclerosis. In this TEP, we reveal a lack of correlation between inhibitor efficacy in cells and their potency using in vitro kinase assays. We show that RIPK2 kinase activity is in fact dispensable for NOD2 inflammatory signalling and that RIPK2 inhibitors function instead by antagonizing XIAP-binding and ubiquitination of RIPK2. We characterise the molecular basis for this effect. We also solved the first crystal structure of the RIPK2 kinase domain and applied a range of biochemical and cellular assays to profile type I and type II RIPK2 kinase inhibitors. Overall, our study illustrates how to target the ATP-binding pocket in RIPK2 to interfere with the RIPK2-XIAP interaction for modulation of NOD signalling.
DOI: 10.5517/ccdc.csd.cc1zfs39
title: CCDC 1830491: Experimental Crystal Structure Determination

description: Related Article: Pauline Chaumont,  Jérome Baudoux,  Jacques Maddaluno,  Jacques Rouden,  and Anne Harrison-Marchand|2018|J.Org.Chem.|83|8081|doi:10.1021/acs.joc.8b00901
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc1znkx3
title: CCDC 1837026: Experimental Crystal Structure Determination

description: Related Article: Alexandre Pinto,  Miriam Piccichè,  Rosa Griera,  Elies Molins,  Joan Bosch,  and Mercedes Amat|2018|J.Org.Chem.|83|8364|doi:10.1021/acs.joc.8b00983
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc1zp31t
title: CCDC 1837526: Experimental Crystal Structure Determination

description: Related Article: Jun-Cheng Su,  Shan Wang,  Wen Cheng,  Xiao-Jun Huang,  Man-Mei Li,  Ren-Wang Jiang,  Yao-Lan Li,  Lei Wang,  Wen-Cai Ye,  and Ying Wang|2018|J.Org.Chem.|83|8522|doi:10.1021/acs.joc.8b01050
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc1zp32v
title: CCDC 1837527: Experimental Crystal Structure Determination

description: Related Article: Jun-Cheng Su,  Shan Wang,  Wen Cheng,  Xiao-Jun Huang,  Man-Mei Li,  Ren-Wang Jiang,  Yao-Lan Li,  Lei Wang,  Wen-Cai Ye,  and Ying Wang|2018|J.Org.Chem.|83|8522|doi:10.1021/acs.joc.8b01050
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.