المؤلفون: Jin Zheng, Arne Moeller, Wei-Ping Gai, Bente Pakkenberg, Cristine Betzer, Tomasz Brudek, Louise Berkhoudt Lassen, Anders Olsen, Glenda M. Halliday, YuHong Fu, Lasse Reimer, Marisa Brini, Tong Chen, Tito Calì, Rikke Hahn Kofoed, Emil Gregersen, Susana Aznar, Poul Henning Jensen, Jens Peter Andersen

المصدر: Betzer, C, Lassen, L B, Olsen, A, Kofoed, R H, Reimer, L, Gregersen, E, Zheng, J, Calì, T, Gai, W-P, Chen, T, Moeller, A, Brini, M, Fu, Y, Halliday, G, Brudek, T, Aznar, S, Pakkenberg, B, Andersen, J P & Jensen, P H 2018, ' Alpha-synuclein aggregates activate calcium pump SERCA leading to calcium dysregulation ', EMBO Reports, vol. 19, no. 5, e44617 . https://doi.org/10.15252/embr.201744617Test
EMBO Reports
Betzer, C, Lassen, L B, Olsen, A, Kofoed, R H, Reimer, L, Gregersen, E, Zheng, J, Calì, T, Gai, W P, Chen, T, Moeller, A, Brini, M, Fu, Y, Halliday, G, Brudek, T, Aznar, S, Pakkenberg, B, Andersen, J P & Jensen, P H 2018, ' Alpha-synuclein aggregates activate calcium pump SERCA leading to calcium dysregulation ', EMBO Reports, vol. 19, no. 5, e44617 . https://doi.org/10.15252/embr.201744617Test

مصطلحات موضوعية: 0301 basic medicine, Male, Indoles, alpha-synuclein, Protein aggregation, Endoplasmic Reticulum, Biochemistry, chemistry.chemical_compound, Mice, Cytosol, Molecular Biology of Disease, Membrane & Intracellular Transport, Cells, Cultured, aggregation, Brain, Parkinson Disease, Articles, Cell biology, endoplasmic reticulum, alpha‐synuclein, alpha-Synuclein, cardiovascular system, Cyclopiazonic acid, SERCA, alpha-synuclein,calcium pumps,aggregates, endoplasmic reticulum, parkinson disease, Calcium pump, chemistry.chemical_element, Calcium, Article, Cell Line, Sarcoplasmic Reticulum Calcium-Transporting ATPases, 03 medical and health sciences, Protein Aggregates, calcium pumps, mental disorders, Genetics, Animals, Humans, Caenorhabditis elegans, Molecular Biology, Alpha-synuclein, calcium, Endoplasmic reticulum, Rats, nervous system diseases, 030104 developmental biology, chemistry, nervous system, aggregates, Lewy Bodies, Neuroscience

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aeb501568bf4b3599696a7861c0caaecTest
https://pure.au.dk/portal/da/publications/alphasynuclein-aggregates-activate-calcium-pump-serca-leading-to-calcium-dysregulationTest(3827620f-4fb6-4218-ad64-763d0cc36eed).html

المؤلفون: Peder Madsen, Dovile Januliene, Arne Moeller, Dorthe Strandbygaard, Maria Hansen, Jacob Andersen, Claus Munck Petersen, Jeppe Achton Nielsen, Esben M. Quistgaard, Søren Thirup

المصدر: Januliene, D, Andersen, J L, Nielsen, J A, Quistgaard, E M, Hansen, M, Strandbygaard, D, Moeller, A, Petersen, C M, Madsen, P & Thirup, S S 2017, ' Acidic Environment Induces Dimerization and Ligand Binding Site Collapse in the Vps10p Domain of Sortilin ', Structure, vol. 25, no. 12, 12, pp. 1809-1819.e3 . https://doi.org/10.1016/j.str.2017.09.015Test

مصطلحات موضوعية: 0301 basic medicine, Conformational change, crystal structure, Endosome, Plasma protein binding, CHO Cells, Molecular Dynamics Simulation, Endocytosis, Ligands, ligand release, 03 medical and health sciences, Cricetulus, conformational change, Structural Biology, Cricetinae, Animals, Humans, endocytosis, Vps10p domain, Binding site, Molecular Biology, Histidine, Binding Sites, dimerization, Chemistry, sortilin, Hydrogen-Ion Concentration, histidine, Ligand (biochemistry), Molecular Docking Simulation, Adaptor Proteins, Vesicular Transport, 030104 developmental biology, HEK293 Cells, Ectodomain, Biochemistry, Biophysics, Protein Multimerization, sorting, Protein Binding

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccef5a9c5118886b6ad510d7115b456eTest
https://pure.au.dk/portal/da/publications/acidic-environment-induces-dimerization-and-ligand-binding-site-collapse-in-the-vps10p-domain-of-sortilinTest(3a1347ab-8f7b-491c-973b-3a7dcbe9b918).html

المؤلفون: Michael Fried, Bridget Carragher, Chunxia Zhao, Arne Moeller, Elizabeth M. Wilson-Kubalek, Sidney W. Whiteheart

المصدر: Journal of Structural Biology. 177:335-343

مصطلحات موضوعية: Models, Molecular, Surface Properties, CHO Cells, Plasma protein binding, Random hexamer, Article, Structural Biology, Adenine nucleotide, Cricetinae, Animals, Protein Structure, Quaternary, N-Ethylmaleimide-Sensitive Proteins, SNARE complex disassembly, Adenine Nucleotides, Chemistry, Lipid bilayer fusion, AAA proteins, Protein Structure, Tertiary, Microscopy, Electron, Crystallography, Amino Acid Substitution, Biophysics, Soluble NSF attachment protein, SNARE Proteins, Ultracentrifugation, Protein Binding

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9829b536065ab1bfd2d972573258d606Test
https://doi.org/10.1016/j.jsb.2011.12.018Test

المؤلفون: Jürgen Markl, Sabrina Keller, Bernhard Lieb, Nadja Hellmann, Ralf Dürr, V. Moeller, Arne Moeller, Ladan Sarraf-Zadeh, Stefanie Heinz

المصدر: Moeller, V, Dürr, R, Sarraf-Zadeh, L, Keller, S, Heinz, S, Hellmann, N, Möller, A, Lieb, B & Markl, J 2011, ' Recombinant functional multidomain hemoglobin from the gastropod Biomphalaria glabrata ', IUBMB Life, vol. 63, no. 5, pp. 323-8 . https://doi.org/10.1002/iub.453Test

مصطلحات موضوعية: Protein subunit, Clinical Biochemistry, Cooperativity, medicine.disease_cause, Biochemistry, law.invention, Hemoglobins, chemistry.chemical_compound, law, Genetics, medicine, Animals, Humans, Biomphalaria glabrata, Protein Structure, Quaternary, Molecular Biology, Escherichia coli, Peptide sequence, Heme, Biomphalaria, biology, Schistosoma mansoni, Cell Biology, biology.organism_classification, Recombinant Proteins, Oxygen, Protein Subunits, chemistry, Recombinant DNA, Oxygen binding

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8911e72e9a5dc3053220edcaee1b5467Test
https://doi.org/10.1002/iub.453Test

المؤلفون: Frank Depoix, Ulrich Meissner, Arne Moeller, Jürgen Markl, Christos Gatsogiannis

المصدر: Gatsogiannis, C, Möller, A, Depoix, F, Meissner, U & Markl, J 2007, ' Nautilus pompilius hemocyanin : 9 A cryo-EM structure and molecular model reveal the subunit pathway and the interfaces between the 70 functional units ', Journal of Molecular Biology, vol. 374, no. 2, pp. 465-86 . https://doi.org/10.1016/j.jmb.2007.09.036Test

مصطلحات موضوعية: Models, Molecular, Molecular model, Protein Conformation, medicine.medical_treatment, Protein subunit, Molecular Sequence Data, Octopodiformes, Allosteric regulation, Biology, Hemocyanin, Turn (biochemistry), Protein structure, Structural Biology, Image Processing, Computer-Assisted, medicine, Animals, Amino Acid Sequence, Molecular Biology, Binding Sites, Sequence Homology, Amino Acid, Cryoelectron Microscopy, Protein primary structure, Crystallography, Hemocyanins, Biophysics, Nautilus, Protein quaternary structure

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::932357e9e148af65c03f1c0a9debb045Test
https://doi.org/10.1016/j.jmb.2007.09.036Test

المؤلفون: Patrick R. Griffin, Raymond C. Stevens, Hualiang Jiang, Ming-Wei Wang, Beili Wu, Fai Y. Siu, Chong Wang, Clinton S. Potter, Linlin Yang, Bridget Carragher, Huaiyu Yang, Chris de Graaf, Arne Moeller, Venkatasubramanian Dharmarajan, Graham M. West, Steffen Reedtz-Runge, Hu Zhou, Dehua Yang, Bruce D. Pascal, Gaojie Song

المساهمون: Medicinal chemistry, AIMMS

المصدر: Yang, L, Yang, D, de Graaf, C, Moeller, A, West, G M, Dharmarajan, V, Wang, C, Siu, F Y, Song, G, Reedtz-Runge, S, Pascal, B D, Wu, B, Potter, C S, Zhou, H, Griffin, P R, Carragher, B, Yang, H, Wang, M W, Stevens, R C & Jiang, H 2015, ' Conformational states of the full-length glucagon receptor ', Nature Communications, vol. 6, 7859, pp. 1-13 . https://doi.org/10.1038/ncomms8859Test
Nature Communications
Nature Communications, 6:7859, 1-13. Nature Publishing Group

مصطلحات موضوعية: General Physics and Astronomy, Plasma protein binding, Molecular Dynamics Simulation, Ligands, General Biochemistry, Genetics and Molecular Biology, Article, Protein Structure, Secondary, Molecular dynamics, Protein structure, Tandem Mass Spectrometry, Receptors, Glucagon, Sf9 Cells, Animals, Humans, Disulfides, Receptor, Multidisciplinary, Chemistry, Deuterium Exchange Measurement, General Chemistry, Glucagon, 3. Good health, Protein Structure, Tertiary, Microscopy, Electron, Biochemistry, Structural biology, Biophysics, Hydrogen–deuterium exchange, Glucagon receptor, Chromatography, Liquid, Protein Binding

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59458c006cd1f5769e01967b98761887Test
https://research.vu.nl/en/publications/e936c4c7-d5a0-4bba-9d6f-686641bc2531Test

المؤلفون: Arne Moeller, Scott C. Rosenberg, Tiffany Y Su, Kevin D. Corbett, Qiaozhen Ye, Jeffrey A. Speir

المصدر: eLife, Vol 4 (2015)
eLife, vol 4, iss 4
eLife

مصطلحات موضوعية: Models, Molecular, Mad2, Cell division, Gene Expression, Sequence Homology, Cell Cycle Proteins, Crystallography, X-Ray, Biochemistry, HORMA domain protein, Spindle pole body, Models, biophysics, Mad2 Proteins, structural biology, Biology (General), N-Ethylmaleimide-Sensitive Proteins, Phylogeny, Adenosine Triphosphatases, Genetics, Crystallography, Escherichia coli Proteins, General Neuroscience, Adaptor Proteins, Nuclear Proteins, Endopeptidase Clp, General Medicine, Biophysics and Structural Biology, Recombinant Proteins, Cell biology, Amino Acid, Spindle checkpoint, C. elegans, Medicine, AAA+ ATPase, Insight, Protein Binding, Protein Structure, QH301-705.5, 1.1 Normal biological development and functioning, Science, Molecular Sequence Data, Spindle Apparatus, Biology, General Biochemistry, Genetics and Molecular Biology, spindle assembly checkpoint, Underpinning research, Escherichia coli, Animals, Humans, biochemistry, Amino Acid Sequence, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Cell Cycle Protein, mouse, Adaptor Proteins, Signal Transducing, Sequence Homology, Amino Acid, General Immunology and Microbiology, Cohesin, Signal Transducing, Molecular, Protein Structure, Tertiary, Spindle apparatus, Checkpoint Proteins, X-Ray, M Phase Cell Cycle Checkpoints, ATPases Associated with Diverse Cellular Activities, Generic health relevance, Biochemistry and Cell Biology, Carrier Proteins, Sequence Alignment, Tertiary, Molecular Chaperones

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e7c3446c228e07c1c512ff79843f42cTest
https://elifesciences.org/articles/07367Test

المؤلفون: Bridget Carragher, Arne Moeller, Houchao Tao, Sung Chang Lee, Ina L. Urbatsch, Qinghai Zhang, Clinton S. Potter, Geoffrey Chang, Jeffrey A. Speir

مصطلحات موضوعية: Models, Molecular, Protein Conformation, Membrane lipids, ATP-binding cassette transporter, Plasma protein binding, Biology, Article, Drug pharmacokinetics, Membrane Lipids, Mice, Protein structure, Bacterial Proteins, Structural Biology, Homologous chromosome, Animals, Nucleotide, ATP Binding Cassette Transporter, Subfamily B, Member 1, Molecular Biology, chemistry.chemical_classification, Nucleotides, Protein Stability, High protein, Microscopy, Electron, Biochemistry, chemistry, Structural Homology, Protein, ATP-Binding Cassette Transporters, Protein Binding

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09d4a94be5e8b0e2e090dac754fc6cd9Test
https://europepmc.org/articles/PMC4351144Test/

المؤلفون: Sébastien Boutet, Lydia N. Caro, Graham M. West, Stella Lisova, Vsevolod Katritch, Anton Barty, Qingping Xu, Xiaoyong Zhi, H. Eric Xu, Bridget Carragher, Jörg Standfuss, Kay Diederichs, Arne Moeller, Oleksandr Yefanov, Nadia A. Zatsepin, Chelsie E. Conrad, Wayne L. Hubbell, John C. H. Spence, Garth J. Williams, Yanyong Kang, Yuhui Dong, Nicole Howe, Daniel James, Christopher Kupitz, Dingjie Wang, Xin Gu, Thomas A. White, Zhong Zheng, Jiyuan Ke, Martin Caffrey, Xiang Gao, Marc Messerschmidt, Raimund Fromme, Chenghai Zhang, Raymond C. Stevens, Vsevolod V. Gurevich, Yi Jiang, Ned Van Eps, Regina J. Lee, Sergey A. Vishnivetskiy, Henry N. Chapman, Uwe Weierstall, Jun Li, Kelly Suino-Powell, X. Edward Zhou, M. H. Eileen Tan, Vadim Cherezov, Haiguang Liu, Petra Fromme, Hualiang Jiang, Parker W. de Waal, Yuanzheng He, Jesse Coe, Kuntal Pal, Dianfan Li, Clinton S. Potter, Bruce D. Pascal, Shatabdi Roy-Chowdhury, Minjia Tan, Wei Liu, Huaiyu Yang, Jinming Ma, Andrii Ishchenko, Ingo Grotjohann, Meitian Wang, Oliver P. Ernst, Gye Won Han, Yingming Zhao, Shibom Basu, Karsten Melcher, Patrick R. Griffin, Cornelius Gati

المصدر: Scientific Data
Nature
Nature, vol 523, iss 7562

مصطلحات موضوعية: Models, Molecular, Rhodopsin, Data Descriptor, genetic structures, General Science & Technology, 1.1 Normal biological development and functioning, Plasma protein binding, Crystallography, X-Ray, Mice, Underpinning research, Models, ddc:570, Arrestin, Animals, Humans, Disulfides, G protein-coupled receptor, Multidisciplinary, Crystallography, Binding Sites, biology, Chemistry, Lasers, X-Rays, Palaeontology, Molecular, Reproducibility of Results, eye diseases, Research data, Transmembrane domain, X-ray crystallography, G protein-coupled receptors, Structural biology, Multiprotein Complexes, Helix, biology.protein, Biophysics, X-Ray, Arrestin beta 1, Generic health relevance, sense organs, X-ray tomography, Protein Binding, Signal Transduction

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::412e7c7cbc3c5bcc023c998fa5ba0861Test
https://pubmed.ncbi.nlm.nih.gov/27272251Test

المؤلفون: Jürgen Markl, Arne Moeller, Andreas G. Martin, Frank Depoix, Judith Rheinbay, Wolfgang Gebauer

المصدر: Markl, J, Möller, A, Martin, A G, Rheinbay, J, Gebauer, W & Depoix, F 2009, ' 10-A cryoEM structure and molecular model of the Myriapod (Scutigera) 6x6mer hemocyanin : understanding a giant oxygen transport protein ', Journal of Molecular Biology, vol. 392, no. 2, pp. 362-80 . https://doi.org/10.1016/j.jmb.2009.06.082Test

مصطلحات موضوعية: Models, Molecular, Molecular model, medicine.medical_treatment, Protein subunit, Molecular Sequence Data, Protein Data Bank (RCSB PDB), Hemocyanin, chemistry.chemical_compound, Structural Biology, medicine, Animals, Carboxylate, Amino Acid Sequence, Protein Structure, Quaternary, Molecular Biology, Histidine, biology, Cryoelectron Microscopy, Oxygen transport, Spirostreptus, biology.organism_classification, Oxygen, Crystallography, chemistry, Hemocyanins, Protein Multimerization, Carrier Proteins, Sequence Alignment

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5dca030328a0676dc78bff8a389c5d4Test
https://pure.au.dk/portal/da/publications/10a-cryoem-structure-and-molecular-model-of-the-myriapod-scutigera-6x6mer-hemocyaninTest(52538af2-e050-44f7-ac12-82cfa84d59be).html