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1دورية أكاديمية
المؤلفون: Tse, Christin, Fletcher, Terace M., Hansen, Jeffrey C.
المصدر: Proceedings of the National Academy of Sciences of the United States of America, 1998 Oct . 95(21), 12169-12173.
الوصول الحر: https://www.jstor.org/stable/46031Test
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2دورية أكاديمية
المؤلفون: T. Gorkovets K., G. Armeev A., K. Shaitan V., A. Shaytan K., Т. Горковец К., Г. Армеев А., К. Шайтан В., А. Шайтан К.
المساهمون: Работа выполнена с использованием оборудования Центра коллективного пользования сверхвысокопроизводительными вычислительными ресурсами МГУ имени М.В. Ломоносова 26 при финансовой поддержке Российского научного фонда (проект №14-24-00031, соглашение №14-24-00031-п).
المصدر: Vestnik Moskovskogo universiteta. Seriya 16. Biologiya; Том 73, № 2 (2018); 99-105 ; Вестник Московского университета. Серия 16. Биология; Том 73, № 2 (2018); 99-105 ; 0137-0952
مصطلحات موضوعية: chromatosome, nucleosome, chromatin, linker histone, linker DNA, DNA flexibility, homology modeling, хроматосома, нуклеосома, хроматин, линкерный гистон, линкерная ДНК, гибкость ДНК, моделирование по гомологии
وصف الملف: application/pdf
العلاقة: https://vestnik-bio-msu.elpub.ru/jour/article/view/584/430Test; Luger K., Mäder A.W., Richmond R.K., Sargent D.F., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 A resolution // Nature. 1997. Vol. 389. N 6648. P. 251–260.; Simpson R.T. Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histones // Biochemistry. 1978. Vol. 17. N 25. P. 5524–5531.; Lyubitelev A.V., Nikitin D.V., Shaytan A.K., Studitsky V.M., Kirpichnikov M.P. Structure and functions of linker histones // Biochemistry (Mosc.). 2016. Vol. 81. N 3. P. 213–223.; El Kennani S., Adrait A., Shaytan A.K., Khochbin S., Bruley C., Panchenko A.R., Landsman D., Pflieger D., Govin J. MS_HistoneDB, a manually curated resource for proteomic analysis of human and mouse histones // Epigenetics Chromatin. 2017. Vol. 10:2.; Syed S.H., Goutte-Gattat D., Becker N., Meyer S., Shukla M.S., Hayes J.J., Everaers R., Angelov D., Bednar J., Dimitrov S. Single-base resolution mapping of H1-nucleosome interactions and 3D organization of the nucleosome // Proc. Natl. Acad. Sci. U. S. A. 2010. Vol. 107. N 21. P. 9620–9625.; Ramakrishnan V., Finch J.T., Graziano V., Lee P.L., Sweet R.M. Crystal structure of globular domain of histone H5 and its implications for nucleosome binding // Nature. 1993. Vol. 362. N 6417. P. 219–223.; Brown D.T., Izard T., Misteli T. Mapping the interaction surface of linker histone H1(0) with the nucleosome of native chromatin in vivo // Nat. Struct. Mol. Biol. 2006. Vol. 13. N 3. P. 250–255.; Pruss D., Bartholomew B., Persinger J., Hayes J., Arents G., Moudrianakis E.N., Wolffe A.P. An asymmetric model for the nucleosome: a binding site for linker histones inside the DNA gyres // Science. 1996. Vol. 274. N 5287. P. 614–617.; Zhou Y.B., Gerchman S.E., Ramakrishnan V., Travers A., Muyldermans S. Position and orientation of the globular domain of linker histone H5 on the nucleosome // Nature. 1998. Vol. 395. N 6700. P. 402–405.; Bednar J., Garcia-Saez I., Boopathi R. et al. Structure and dynamics of a 197 bp nucleosome in complex with linker histone H1 // Mol. Cell. 2017. Vol. 66. N 3. P. 384–397; Zhou B.-R., Feng H., Kato H., Dai L., Yang Y., Zhou Y., Bai Y. Structural insights into the histone H1-nucleosome complex // Proc. Natl. Acad. Sci. U. S. A. 2013. Vol. 110. N 48. P. 19390–19395.; Zhou B.-R., Jiang J., Feng H., Ghirlando R., Xiao T.S., Bai Y. Structural mechanisms of nucleosome recognition by linker histones // Mol. Cell. 2015. Vol. 59. N 4. P. 628–638.; Zhou B.-R., Feng H., Ghirlando R., Li S., Schwieters C.D., Bai Y. A Small number of residues can determine if linker histones are bound on or off dyad in the chromatosome // J. Mol. Biol. 2016. Vol. 428. N 20. P. 3948–3959.; Cui F., Zhurkin V.B. Distinctive sequence patterns in metazoan and yeast nucleosomes: implications for linker histone binding to AT-rich and methylated DNA // Nucleic Acids Res. 2009. Vol. 37. N 9. P. 2818–2829.; Öztürk M.A., Pachov G.V., Wade R.C., Cojocaru V. Conformational selection and dynamic adaptation upon linker histone binding to the nucleosome // Nucleic Acids Res. 2016. Vol. 44. N 14. P. 6599–6613.; Pachov G.V., Gabdoulline R.R., Wade R.C. On the structure and dynamics of the complex of the nucleosome and the linker histone // Nucleic Acids Res. 2011. Vol. 39. N 12. P. 5255–5263.; Song F., Chen P., Sun D., Wang M., Dong L., Liang D., Xu R.-M., Zhu P., Li G. Cryo-EM study of the chromatin fiber reveals a double helix twisted by tetranucleosomal units // Science. 2014. Vol. 344. N 6182. P. 376–380.; Rohs R., Jin X., West S.M., Joshi R., Honig B., Mann R.S. Origins of specificity in protein-DNA recognition // Annu. Rev. Biochem. 2010. Vol. 79. P. 233–269.; Edgar R.C. MUSCLE: multiple sequence alignment with high accuracy and high throughput // Nucleic Acids Res. 2004. Vol. 32. N 5. P. 1792–1797.; Cock P.A., Antao T., Chang J.T., Chapman B.A., Cox C.J., Dalke A., Friedberg I., Hamelryck T., Kauff F., Wilczynski B., de Hoon M.J.L. Biopython: freely available Python tools for computational molecular biology and bioinformatics // Bioinformatics 2009. Vol. 25. N 11. Р. 1422–1423.; Webb B., Sali A. Comparative protein structure modeling using MODELLER // Curr. Protoc. Bioinformatics. 2016. Vol. 54. P. 5.6.1–5.6.37.; Martí-Renom M.A., Stuart A.C., Fiser A., Sánchez R., Melo F., Sali A. Comparative protein structure modeling of genes and genomes // Annu. Rev. Biophys. Biomol. Struct. 2000. Vol. 29. P. 291–325.; Pettersen E.F., Goddard T.D., Huang C.C., Couch G.S., Greenblatt D.M., Meng E.C., Ferrin T.E. UCSF Chimera — a visualization system for exploratory research and analysis // J. Comput. Chem. 2004. Vol. 25. N 13. P. 1605–1612.; Lu X., Olson W.K. 3DNA: a software package for the analysis, rebuilding and visualization of three-dimensional nucleic acid structures // Nucleic Acids Res. 2003. Vol. 31. N 17. P. 5108–5121.; Olson W.K., Gorin A.A., Lu X.-J., Hock L.M., Zhurkin V.B. DNA sequence-dependent deformability deduced from protein–DNA crystal complexes // Proc. Natl. Acad. Sci. U. S. A. 1998. Vol. 95. N 19. P. 11163–11168.; Воеводин В., Жуматий С., Соболев С., Антонов А., Брызгалов П., Никитенко Д., Стефанов К., Воеводин В. Практика суперкомпьютера “Ломоносов” // Открытые системы. СУБД. 2012. № 7 (183). С. 36–39.; https://vestnik-bio-msu.elpub.ru/jour/article/view/584Test
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3دورية أكاديمية
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4
المؤلفون: Allison Ballandras-Colas, Goedele N. Maertens, Peter Cherepanov, Alan Engelman, Erik Serrao
المصدر: Retrovirology
مصطلحات موضوعية: Virus Integration, Integration sites, MAMMARY-TUMOR VIRUS, Integrase, Cell Line, chemistry.chemical_compound, Retrovirus, Mammary tumor virus, Virology, NUCLEOTIDE-SEQUENCE, DNA flexibility, Nucleosome, Humans, BET proteins, FOAMY VIRUS, Genetics, Science & Technology, biology, Integrases, HUMAN ENDOGENOUS RETROVIRUS, Research, T-CELL LEUKEMIA, DNA, IN-VITRO, Provirus, biology.organism_classification, 3. Good health, Chromatin, Nucleosomes, Infectious Diseases, chemistry, Dinucleotide steps, HUMAN-IMMUNODEFICIENCY-VIRUS, TRANSCRIPTION START SITES, biology.protein, HIV-1, INTEGRATION SITE SELECTION, Spumavirus, TYPE-1 PREINTEGRATION COMPLEXES, Life Sciences & Biomedicine
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e003cdfa937534aa863fd17da46803d5Test
http://hdl.handle.net/10044/1/27803Test -
5
المؤلفون: Filomena Mazzei, Daniele Santoni, Francesco Pedone
المصدر: Biophysical Chemistry. 112:77-88
مصطلحات موضوعية: Molecular Sequence Data, Biophysics, Fluorescence Polarization, Rigidity (psychology), Biochemistry, DNA sequencing, chemistry.chemical_compound, Modulation (music), Animals, dna flexibility, fluorescence polarization anisotropy, nucleosomes, tetranucleotides, Nucleosome, Torsion constant, Anisotropy, Base Sequence, Chemistry, Organic Chemistry, DNA, Models, Theoretical, Nucleosomes, Crystallography, Cattle, Stress, Mechanical, Sequence Analysis, Mathematics, Fluorescence anisotropy
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aaa9f7ee1c7d70b07f49aa9ec722417eTest
https://doi.org/10.1016/j.bpc.2004.07.005Test -
6
المصدر: Scopus-Elsevier
مصطلحات موضوعية: Biophysics, Stacking, Thermodynamics, dual role of dna curvature on thermodynamic stability of nucleosome, dual role of dna flexibility on thermodynamic stability of nucleosome, mechanical statistical model, mucleosome thermodynamic stability, Quantitative Biology::Subcellular Processes, chemistry.chemical_compound, Computational chemistry, Nucleosome, Fourier series, Canonical ensemble, Statistical ensemble, Quantitative Biology::Biomolecules, Base Sequence, Chemistry, Elastic energy, DNA, Models, Theoretical, Quantitative Biology::Genomics, Elasticity, Nucleosomes, Nucleic Acid Conformation, Chemical stability, Research Article
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f32d77ab47739d53175dd447fcc641d6Test
https://doi.org/10.1016/s0006-3495Test(00)76319-3 -
7دورية أكاديمية
المؤلفون: PEDONE, Francesco, Filomena Mazzei, Daniele Santoni
المساهمون: Pedone, Francesco, Filomena, Mazzei, Daniele, Santoni
مصطلحات موضوعية: dna flexibility, fluorescence polarization anisotropy, nucleosome, tetranucleotides
العلاقة: info:eu-repo/semantics/altIdentifier/pmid/15501578; info:eu-repo/semantics/altIdentifier/wos/WOS:000224852300009; volume:112; issue:1; firstpage:77; lastpage:88; numberofpages:12; journal:BIOPHYSICAL CHEMISTRY; http://hdl.handle.net/11573/364096Test; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-6344222989; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000224852300009&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396aTest; http://www.scopus.com/inward/record.url?eid=2-s2.0-6344222989&partnerID=65&md5=b9666bc46b9504b85d472bd6b3aa8498Test
الإتاحة: https://doi.org/10.1016/j.bpc.2004.07.005Test
http://hdl.handle.net/11573/364096Test
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000224852300009&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396aTest
http://www.scopus.com/inward/record.url?eid=2-s2.0-6344222989&partnerID=65&md5=b9666bc46b9504b85d472bd6b3aa8498Test -
8
المصدر: Biophysical chemistry. 124(2)
مصطلحات موضوعية: Nucleosome organization, telomeric chromatin, Molecular Sequence Data, Biophysics, nucleosomal arrays, Solenoid (DNA), Microscopy, Atomic Force, Biochemistry, Models, Biological, DNA sequencing, chemistry.chemical_compound, Nucleosome, Humans, A-DNA, atomic force microscopy, Base Sequence, 601 strong nucleosome positioning sequence, theoretical modeling, Organic Chemistry, sequence-dependent nucleosome positioning, Telomere, telomeres, Linker DNA, Chromatin, Nucleosomes, dna flexibility, Crystallography, chemistry, afm imaging of telomeric chromatin, DNA
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5331791a95079eb39f58e312e3ad5430Test
https://pubmed.ncbi.nlm.nih.gov/16824667Test -
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المصدر: Biophysical chemistry. 107(1)
مصطلحات موضوعية: Bent molecular geometry, Molecular Sequence Data, Biophysics, Crithidia fasciculata, Biochemistry, Stability (probability), DNA sequencing, chemistry.chemical_compound, DNA flexibility, Nucleosome, Animals, nucleosome stability, Genetics, biology, Base Sequence, Models, Genetic, Organic Chemistry, DNA, Protozoan, biology.organism_classification, Linker DNA, Nucleosomes, theoretical model for prediciting nucleosome stability, DNA curvature, chemistry, Kinetoplast, Nucleic Acid Conformation, Thermodynamics, DNA
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a32b60c8839279d1ffb7020057ba9c7Test
https://pubmed.ncbi.nlm.nih.gov/14871596Test -
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المؤلفون: Claudio Anselmi, Anita Scipioni, P. De Santis, Raffaella Paparcone, Maria Savino
مصطلحات موضوعية: dna circularization, Dna curvature, dna curvature, Biophysics, Stacking, Thermodynamics, writhe transitions, Microscopy, Atomic Force, Biochemistry, Nucleosome, nucleosome stability, Writhe, Sequence, Chemistry, Organic Chemistry, DNA, Elasticity (physics), electrophoretic retardation, Quantitative Biology::Genomics, Elasticity, Nucleosomes, dna flexibility, Models, Chemical, Nucleic Acid Conformation, Chemical stability, Deformation (engineering), Algorithms
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d674c4c8268dcc544b1b74023110c95eTest
http://hdl.handle.net/11573/249464Test