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1دورية أكاديمية
المؤلفون: Khanal, Pushpa, Boskovic, Zoran, Lahti, Lauri, Ghimire, Aruna, Minkeviciene, Rimante, Opazo, Patricio, Hotulainen, Pirta
المساهمون: Neuroscience Center, Helsinki Institute of Life Science HiLIFE, STEMM - Stem Cells and Metabolism Research Program, Medicum
مصطلحات موضوعية: BAR domains, Actin cytoskeleton, Dendritic spines, Spine initiation, 3112 Neurosciences
وصف الملف: application/pdf
العلاقة: Khanal , P , Boskovic , Z , Lahti , L , Ghimire , A , Minkeviciene , R , Opazo , P & Hotulainen , P 2023 , ' Gas7 Is a Novel Dendritic Spine Initiation Factor ' , eNeuro , vol. 10 , no. 4 , ENEURO.0344-22.2023 . https://doi.org/10.1523/ENEURO.0344-22.2023Test; ORCID: /0000-0003-1017-1172/work/135801919; ORCID: /0000-0002-0063-4236/work/135803468; 0bf6a12c-7916-4d54-a42c-a3fd2c10b17f; http://hdl.handle.net/10138/358042Test; 000973675200004
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2دورية أكاديمية
المؤلفون: Larsen, Andreas Haahr
المصدر: Larsen , A H 2022 , ' Molecular Dynamics Simulations of Curved Lipid Membranes ' , International Journal of Molecular Sciences , vol. 23 , no. 15 , 8098 . https://doi.org/10.3390/ijms23158098Test
مصطلحات موضوعية: molecular dynamics (MD), lipid membrane, membrane curvature, vesicle, free energy of binding, BAR DOMAINS, AMPHIPATHIC HELICES, FORCE-FIELD, CURVATURE, PROTEINS, SHAPE, MECHANISM, MODEL
وصف الملف: application/pdf
الإتاحة: https://doi.org/10.3390/ijms23158098Test
https://curis.ku.dk/portal/da/publications/molecular-dynamics-simulations-of-curved-lipid-membranesTest(cd59ba91-8737-4ae9-9270-53abf2967ea2).html
https://curis.ku.dk/ws/files/317046031/Molecular.pdfTest -
3دورية أكاديمية
المؤلفون: Luka Mesarec, Mitja Drab, Samo Penič, Veronika Kralj-Iglič, Aleš Iglič
المصدر: International Journal of Molecular Sciences; Volume 22; Issue 5; Pages: 2348
مصطلحات موضوعية: cytoskeleton, membrane skeleton, cell shape, orientational ordering, actin filaments, active force, BAR domains, anisotropic shape of molecules, NMIIA motor domains, membrane budding
جغرافية الموضوع: agris
وصف الملف: application/pdf
العلاقة: Biochemistry; https://dx.doi.org/10.3390/ijms22052348Test
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المؤلفون: Pushpa Khanal, Zoran Boskovic, Lauri Lahti, Aruna Ghimire, Rimante Minkeviciene, Patricio Opazo, Pirta Hotulainen
المساهمون: Minerva Foundation Institute for Medical Research Helsinki, University of Queensland, Department of Computer Science, Aalto-yliopisto, Aalto University, Neuroscience Center, Helsinki Institute of Life Science HiLIFE, STEMM - Stem Cells and Metabolism Research Program, Medicum
مصطلحات موضوعية: Spine initiation, actin cytoskeleton, BAR domains, General Neuroscience, Actin cytoskeleton, 3112 Neurosciences, spine initiation, General Medicine, dendritic spines, Dendritic spines
وصف الملف: application/pdf
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4f8081d8bf4452ff202c79d07347ad7Test
https://aaltodoc.aalto.fi/handle/123456789/120822Test -
5دورية أكاديمية
المؤلفون: Bassereau, Patricia, Jin, Rui, Baumgart, Tobias, Deserno, Markus, Dimova, Rumiana, Frolov, Vadim, Bashkirov, Pavel V., Grubmüller, Helmut, Jahn, Reinhard, Risselada, H. Jelger, Johannes, Ludger, Kozlov, Michael M., Lipowsky, Reinhard, Pucadyil, Thomas J., Zeno, Wade F., Stachowiak, Jeanne C., Stamou, Dimitrios, Breuer, Artù, Lauritsen, Line, Simon, Camille, Sykes, Cécile, Voth, Gregory A., Weikl, Thomas R.
مصطلحات موضوعية: biomembrane, curavture, remodeling, clathrin-mediated endocytosis, domain-containing proteins, membrane curvature, lipid-membranes, amphipathic helix, fluid membranes, bar domains, independent carriers, generating proteins, elastic properties
العلاقة: http://iopscience.iop.org/article/10.1088/1361-6463/aacb98/metaTest; Journalof Physics D-Applied physics 51(34) : (2018) // Article ID 343001; http://hdl.handle.net/10810/29751Test
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المؤلفون: Samo Penič, Aleš Iglič, Luka Mesarec, Veronika Kralj-Iglič, Mitja Drab
المصدر: International journal of molecular sciences, vol. 22, no. 5, 2348, 2021.
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 22, Iss 2348, p 2348 (2021)
Volume 22
Issue 5مصطلحات موضوعية: 0301 basic medicine, Models, Molecular, Erythrocytes, aktivna sila, 02 engineering and technology, lcsh:Chemistry, BAR domene, udc:577, Cytoskeleton, orientacijski red, lcsh:QH301-705.5, Spectroscopy, active force, orientational ordering, Vesicle, membrane skeleton, cytoskeleton, General Medicine, Membrane budding, 021001 nanoscience & nanotechnology, Computer Science Applications, Membrane, oblika celic, 0210 nano-technology, Monte Carlo Method, anizotropna oblika molekul, motorne domene NMIIA, Materials science, brstenje membran, aktinski filamenti, Models, Biological, Catalysis, Article, cell shape, Inorganic Chemistry, 03 medical and health sciences, Membrane Microdomains, Humans, Computer Simulation, Physical and Theoretical Chemistry, Molecular Biology, membranski skelet, Actin, membrane budding, Organic Chemistry, Erythrocyte Membrane, Biological membrane, Actin cytoskeleton, NMIIA motor domains, Elasticity, 030104 developmental biology, anisotropic shape of molecules, lcsh:Biology (General), lcsh:QD1-999, BAR domains, Amphiphysin, actin filaments, Biophysics, citoskelet
وصف الملف: application/pdf; text/url
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06a69c835825907b859b4be5b5376b04Test
https://hdl.handle.net/20.500.12556/RUL-135022Test -
7دورية أكاديمية
المؤلفون: Lomize, Andrei L., Todd, Spencer C., Pogozheva, Irina D.
مصطلحات موضوعية: ion channels, membrane curvature, TOM complex, transporters, web server, membrane proteins, annexins, ATP synthase, BAR domains, Biological Chemistry, Health Sciences
وصف الملف: application/pdf
العلاقة: Lomize, Andrei L.; Todd, Spencer C.; Pogozheva, Irina D. (2022). "Spatial arrangement of proteins in planar and curved membranes by PPM 3.0." Protein Science 31(1): 209-220.; https://hdl.handle.net/2027.42/171626Test; Protein Science; Wang W, Chen X, Zhang L, et al. Atomic structure of human TOM core complex. Cell Discov. 2020; 6: 67.; Carlson B, Soderling SH. Mechanisms of cellular protrusions branch out. Dev Cell. 2009; 17: 307 – 309.; Boye TL, Jeppesen JC, Maeda K, et al. Annexins induce curvature on free‐edge membranes displaying distinct morphologies. Sci Rep. 2018; 8: 10309.; Davies KM, Anselmi C, Wittig I, Faraldo‐Gómez JD, Kühlbrandt W. Structure of the yeast F 1 F 0 ‐ATP synthase dimer and its role in shaping the mitochondrial cristae. Proc Natl Acad Sci U S A. 2012; 109: 13602 – 13607.; Guo H, Bueler SA, Rubinstein JL. Atomic model for the dimeric F 0 region of mitochondrial ATP synthase. Science. 2017; 358: 936 – 940.; Daum B, Nicastro D, Austin J 2nd, McIntosh JR, Kühlbrandt W. Arrangement of photosystem II and ATP synthase in chloroplast membranes of spinach and pea. Plant Cell. 2010; 22: 1299 – 1312.; Guo YR, MacKinnon R. Structure‐based membrane dome mechanism for Piezo mechanosensitivity. Elife. 2017; 6: e33660.; Saotome K, Murthy SE, Kefauver JM, Whitwam T, Patapoutian A, Ward AB. Structure of the mechanically activated ion channel Piezo1. Nature. 2018; 554: 481 – 486.; Wang L, Zhou H, Zhang M, et al. Structure and mechanogating of the mammalian tactile channel Piezo2. Nature. 2019; 573: 225 – 229.; Tucker K, Park E. Cryo‐EM structure of the mitochondrial protein‐import channel TOM complex at near‐atomic resolution. Nat Struct Mol Biol. 2019; 26: 1158 – 1166.; Wang Y, Nguyen NX, She J, et al. Structural mechanism of EMRE‐dependent gating of the human mitochondrial calcium uniporter. Cell. 2019; 177: 1252 – 1261.; Wang Y, Han Y, She J, et al. Structural insights into the Ca(2+)‐dependent gating of the human mitochondrial calcium uniporter. Elife. 2020; 9: e60513.; Zhuo W, Zhou H, Guo R, et al. Structure of intact human MCU supercomplex with the auxiliary MICU subunits. Protein Cell. 2021; 12: 220 – 229.; Fan M, Zhang J, Tsai C‐W, et al. Structure and mechanism of the mitochondrial Ca(2+) uniporter holocomplex. Nature. 2020; 582: 129 – 133.; De La Fuente S, Fernandez‐Sanz C, Vail C, et al. Strategic positioning and biased activity of the mitochondrial calcium uniporter in cardiac muscle. J Biol Chem. 2016; 291: 23343 – 23362.; Yang X, Wang Q, Cao E. Structure of the human cation‐chloride cotransporter nkcc1 determined by single‐particle electron cryo‐microscopy. Nat Commun. 2020; 11: 1016.; Tascón I, Sousa JS, Corey RA, et al. Structural basis of proton‐coupled potassium transport in the KUP family. Nat Commun. 2020; 11: 626.; Agip AA, Blaza JN, Bridges HR, et al. Cryo‐EM structures of complex I from mouse heart mitochondria in two biochemically defined states. Nat Struct Mol Biol. 2018; 25: 548 – 556.; Huang Z, Shen L, Wang W, et al. Structure of photosystem I‐LHCI‐LHCII from the green alga Chlamydomonas Reinhardtii in state 2. Nat Commun. 2021; 12: 1100.; Chen M, Perez‐Boerema A, Zhang L, et al. Distinct structural modulation of photosystem I and lipid environment stabilizes its tetrameric assembly. Nature Plants. 2020; 6: 314 – 320.; Pi X, Zhao S, Wang W, et al. The pigment‐protein network of a diatom photosystem II‐light‐harvesting antenna supercomplex. Science. 2019; 365: eaax4406.; Wang Z, Fan G, Hryc CF, et al. An allosteric transport mechanism for the AcrAB‐TolC multidrug efflux pump. Elife. 2017; 6: e24905.; Glavier M, Puvanendran D, Salvador D, et al. Antibiotic export by MexB multidrug efflux transporter is allosterically controlled by a MexA‐OprM chaperone‐like complex. Nat Commun. 2020; 11: 4948.; Fitzpatrick AWP, Llabrés S, Neuberger A, et al. Structure of the MacAB‐TolC ABC‐type tripartite multidrug efflux pump. Nat Microbiol. 2017; 2: 17070.; Syrjanen J, Michalski K, Kawate T, Furukawa H. On the molecular nature of large‐pore channels. J Mol Biol. 2021; 433: 166994.; Pogozheva ID, Tristram‐Nagle S, Mosberg HI, Lomize AL. Structural adaptations of proteins to different biological membranes. Biochim Biophys Acta. 2013; 1828: 2592 – 2608.; Campelo F, McMahon HT, Kozlov MM. The hydrophobic insertion mechanism of membrane curvature generation by proteins. Biophys J. 2008; 95: 2325 – 2339.; Bausewein T, Mills DJ, Langer JD, Nitschke B, Nussberger S, Kühlbrandt W. Cryo‐EM structure of the TOM core complex from neurospora crassa. Cell. 2017; 170: 693 – 700.; Burley SK, Berman HM, Kleywegt GJ, Markley JL, Nakamura H, Velankar S. Protein Data Bank (PDB): The single global macromolecular structure archive. Methods Mol Biol. 2017; 1607: 627 – 641.; Lawson CL, Baker ML, Best C, et al. EMDataBank.org: Unified data resource for CryoEM. Nucleic Acids Res. 2011; 39: D456 – D464.; Lomize AL, Pogozheva ID, Lomize MA, Mosberg HI. Positioning of proteins in membranes: A computational approach. Protein Sci. 2006; 15: 1318 – 1333.; Lomize MA, Pogozheva ID, Joo H, Mosberg HI, Lomize AL. OPM database and PPM web server: Resources for positioning of proteins in membranes. Nucleic Acids Res. 2012; 40: D370 – D376.; Nugent T, Jones DT. Membrane protein orientation and refinement using a knowledge‐based statistical potential. BMC Bioinform. 2013; 14: 276.; Araiso Y, Tsutsumi A, Qiu J, et al. Structure of the mitochondrial import gate reveals distinct preprotein paths. Nature. 2019; 575: 395 – 401.; Senes A, Chadi DC, Law PB, Walters RF, Nanda V, Degrado WF. E(z), a depth‐dependent potential for assessing the energies of insertion of amino acid side‐chains into membranes: Derivation and applications to determining the orientation of transmembrane and interfacial helices. J Mol Biol. 2007; 366: 436 – 448.; Schramm CA, Hannigan BT, Donald JE, et al. Knowledge‐based potential for positioning membrane‐associated structures and assessing residue‐specific energetic contributions. Structure. 2012; 20: 924 – 935.; Hsieh D, Davis A, Nanda V. A knowledge‐based potential highlights unique features of membrane alpha‐helical and beta‐barrel protein insertion and folding. Protein Sci. 2012; 21: 50 – 62.; Tusnady GE, Dosztanyi Z, Simon I. Transmembrane proteins in the Protein Data Bank: Identification and classification. Bioinformatics. 2004; 20: 2964 – 2972.; Tusnady GE, Dosztanyi Z, Simon I. TMDET: Web server for detecting transmembrane regions of proteins by using their 3d coordinates. Bioinformatics. 2005; 21: 1276 – 1277.; Postic G, Ghouzam Y, Guiraud V, Gelly J‐C. Membrane positioning for high‐ and low‐resolution protein structures through a binary classification approach. Prot Eng Des Sel. 2015; 29: 87 – 92.; Dutagaci B, Feig M. Determination of hydrophobic lengths of membrane proteins with the HDGB implicit membrane model. J Chem Inf Model. 2017; 57: 3032 – 3042.; Kozma D, Simon I, Tusnady GE. PDBTM: Protein Data Bank of transmembrane proteins after 8 years. Nucleic Acids Res. 2013; 41: D524 – D529.; Sehnal D, Bittrich S, Deshpande M, et al. Mol* viewer: Modern web app for 3D visualization and analysis of large biomolecular structures. Nucleic Acids Res. 2021; 49: W431 – W437.; Jarsch IK, Daste F, Gallop JL. Membrane curvature in cell biology: An integration of molecular mechanisms. J Cell Biol. 2016; 214: 375 – 387.; Stansfeld PJ, Goose JE, Caffrey M, et al. MemProtMD: Automated insertion of membrane protein structures into explicit lipid membranes. Structure. 2015; 23: 1350 – 1361.; Newport TD, Sansom MSP, Stansfeld PJ. The MemProtMD database: A resource for membrane‐embedded protein structures and their lipid interactions. Nucleic Acids Res. 2019; 47: D390 – d397.; Yin Y, Arkhipov A, Schulten K. Simulations of membrane tubulation by lattices of amphiphysin N‐BAR domains. Structure. 2009; 17: 882 – 892.; Lomize AL, Pogozheva ID, Mosberg HI. Anisotropic solvent model of the lipid bilayer. 2. Energetics of insertion of small molecules, peptides, and proteins in membranes. J Chem Inf Model. 2011; 51: 930 – 946.; Lomize AL, Schnitzer KA, Todd SC, Pogozheva ID. Thermodynamics‐based molecular modeling of α‐helices in membranes and micelles. J Chem Inf Model. 2021; 61: 2884 – 2896.; Suetsugu S. The proposed functions of membrane curvatures mediated by the BAR domain superfamily proteins. J Biochem. 2010; 148: 1 – 12.; Suetsugu S, Toyooka K, Senju Y. Subcellular membrane curvature mediated by the BAR domain superfamily proteins. Sem Cell Dev Biol. 2010; 21: 340 – 349.; Lemmon M. Membrane recognition by phospholipid‐binding domains. Nat Rev Mol Cell Biol. 2008; 9: 99 – 111.; Gallop JL, Jao CC, Kent HM, et al. Mechanism of endophilin N‐BAR domain‐mediated membrane curvature. EMBO J. 2006; 25: 2898 – 2910.; Liu S, Xiong X, Zhao X, Yang X, Wang H. F‐BAR family proteins, emerging regulators for cell membrane dynamic changes‐from structure to human diseases. J Hematol Oncol. 2015; 8: 47.
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8دورية أكاديمية
مصطلحات موضوعية: BAR DOMAINS,LIPID MEMBRANES,MEMBRANE DYNAMICS
وصف الملف: text/html
الإتاحة: http://cyberleninka.ru/article/n/the-role-ofTest-bar-domain-proteins-in-the-regulation-of-membrane-dynamics
http://cyberleninka.ru/article_covers/16967695.pngTest -
9مراجعة
المؤلفون: Johnson, David H, Kou, Orianna H, Bouzos, Nicoletta, Zeno, Wade F
المصدر: Trends Biochem Sci ; ISSN:0968-0004 ; Volume:49 ; Issue:5
مصطلحات موضوعية: BAR domains, clathrin, intrinsically disordered proteins, membrane bending, membrane curvature sensing, α-synuclein
العلاقة: https://doi.org/10.1016/j.tibs.2024.02.005Test; https://pubmed.ncbi.nlm.nih.gov/38508884Test; https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11069444Test/
الإتاحة: https://doi.org/10.1016/j.tibs.2024.02.005Test
https://pubmed.ncbi.nlm.nih.gov/38508884Test
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11069444Test/ -
10مراجعة
المؤلفون: Senju, Yosuke, Lappalainen, Pekka
المساهمون: Institute of Biotechnology, Pekka Lappalainen / Principal Investigator
مصطلحات موضوعية: CLATHRIN-COATED PITS, PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE, MEMBRANE CURVATURE, PLASMA-MEMBRANE, N-WASP, BAR DOMAINS, PHOSPHOINOSITIDES, CYTOSKELETON, ADHESION, POLYMERIZATION, Biochemistry, cell and molecular biology
وصف الملف: application/pdf
العلاقة: The studies focusing on protein-lipid interplay in the laboratory of PL are supported by Human Frontiers Science Program Organization (RGP0005/2016) and academy of Finland Centre of Excellence (272130). We apologize that many studies on regulation of the actin cytoskeleton dynamics by phosphoinositides could not be cited due to space limitations. Minna Poukkula (University of Helsinki) is acknowledged for excellent comments on the manuscript.; Senju , Y & Lappalainen , P 2019 , ' Regulation of actin dynamics by PI(4,5)P-2 in cell migration and endocytosis ' , Current Opinion in Cell Biology , vol. 56 , pp. 7-13 . https://doi.org/10.1016/j.ceb.2018.08.003Test; ORCID: /0000-0002-9606-3270/work/68616193; http://hdl.handle.net/10138/321962Test; 24822f48-5796-4801-a071-c65df566c60e; 000457629800003