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Білки (Ukrainian Wikipedia)

Analysis of information sources in references of the Wikipedia article "Білки" in Ukrainian language version.

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51nih.gov
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archive.org

business.site

website-designer-2149.business.site

cam.ac.uk

www-jackson.ch.cam.ac.uk

cell.com

cnshb.ru

  • Белки. Химическая энциклопедия. Москва: Советская энциклопедия. 1988.

doi.org

ebi.ac.uk

expasy.org

howard.edu

med.howard.edu

jbc.org

  • Sumner, JB (1926). The Isolation and Crystallization of the Enzyme Urease. Preliminary Paper (PDF). J Biol Chem. 69: 435—41. Архів оригіналу (PDF) за 29 вересня 2007. Процитовано 14 січня 2008.

lifelib.info

molcells.org

nih.gov

pubmed.ncbi.nlm.nih.gov

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  • Kendrew J, Bodo G, Dintzis H, Parrish R, Wyckoff H, Phillips D (1958). A three-dimensional model of the myoglobin molecule obtained by x-ray analysis. Nature. 181 (4610): 662—6. PMID 13517261.
  • Fulton A, Isaacs W (1991). Titin, а huge, elastic sarcomeric protein with а probable role in morphogenesis. Bioessays. 13 (4): 157—61. PMID 1859393.
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  • Welker M, von Döhren H (2006). Cyanobacterial peptides — nature's own combinatorial biosynthesis. FEMS Microbiol Rev. 30 (4): 530—563. PMID 16774586.
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  • Ellis RJ, van der Vies SM (1991). Molecular chaperones. Annu. Rev. Biochem. 60: 321—47. doi:10.1146/annurev.bi.60.070191.001541. PMID 1679318.
  • Sun Y, MacRae TH. (2005). The small heat shock proteins and their role in human disease. FEBS J. 60: 2613—27. PMID 15943797.
  • Yannay-Cohen N, Razin E. (2000). Translation and transcription: the dual functionality of LysRS in mast cells. Mol Cells. 22: 127—32. PMID 17085962. Архів оригіналу за 18 червня 2008. Процитовано 8 лютого 2008.
  • Wortinger M, Sackett MJ, Brun YV (2000). CtrA mediates a DNA replication checkpoint that prevents cell division in Caulobacter crescentus. EMBO J. 19 (17): 4503—4512. PMID 10970844.
  • Bairoch A. (2000). The ENZYME database in 2000 (PDF). Nucleic Acids Res. 28: 304—305. PMID 10592255. Архів оригіналу (PDF) за 1 червня 2011. Процитовано 16 січня 2008.
  • Radzicka A, Wolfenden R. (1995). A proficient enzyme. Science. 6 (267): 90—931. PMID 7809611.
  • Erickson HP (2007). Evolution of the cytoskeleton. Bioessays. 29 (7): 668—677. PMID 17563102.
  • Wolberg AS (2007). Thrombin generation and fibrin clot structure. Blood Rev. 21 (3): 131—142. PMID 17208341.
  • J. Li, D.R. Barreda, Y.-A. Zhang, H. Boshra, A.E. Gelman, S. LaPatra, L. Tort & J.O. Sunyer (2006). B lymphocytes from early vertebrates have potent phagocytic and microbicidal abilities. Nature Immunology. 7: 1116—1124. PMID 16980980.
  • Повещенко А.Ф., Абрамов В.В., Козлов В.В. (2007). Цитокины — факторы нейроэндоктринной регуляции. Успехи Физиологических Наук. 38 (3): 40—46. PMID 17977230.
  • Dupré DJ, Hébert TE (2006). Biosynthesis and trafficking of seven transmembrane receptor signalling complexes. Cell Signal. 10: 1549—1559. PMID 16677801.
  • Hinnebusch AG (2005). Translational regulation of GCN4 and the general amino acid control of yeast. Annu Rev Microbiol. 59: 407—450. PMID 16153175.
  • Anderson P, Kedersha N (2006). RNA granules. Cell Biol. 172 (6): 803—808. PMID 16520386.
  • Wittenberg JB (2007). On optima: the case of myoglobin-facilitated oxygen diffusion. Gene. 398 (1-2): 156—161. PMID 17573206.
  • Frelin C, Vigne P, Lazdunski M. (1981). The specificity of the sodium channel for monovalent cations. Eur J Biochem. 119 (2): 437—442. PMID 6273156.
  • Schroer, Trina A (2004). Dynactin. Annual Review of Cell and Developmental Biology. 20: 759—779. PMID 15473859.
  • Scholey JM, Brust-Mascher I, Mogilner A. (2003). Cell division. Nature. 422 (6933): 741—745. PMID 12700768.
  • Vermeulen KC, Stienen GJ, Schmid CF. (2002). Cooperative behavior of molecular motors. Muscle Res Cell Motil. 23 (1): 71—79. PMID 12363288.
  • Guo P, Lee TJ. (2007). Viral nanomotors for packaging of dsDNA and dsRNA. Mol Microbiol. 64 (4): 886—903. PMID 17501915.
  • Wilken J, Kent SB (1998). Chemical protein synthesis. Curr Opin Biotechnol. 9 (4): 412—426. PMID 9720266.
  • Dawson PE, Kent SB (2000). Synthesis of native proteins by chemical ligation. Annu Rev Biochem. 69: 923—960. PMID 10966479.
  • Ingles-Prieto A., Ibarra-Molero B., Delgado-Delgado A. та ін. (2013). Conservation of Protein Structure over Four Billion Years (PDF). Structure. 21 (9): 1690—1697. doi:10.1016/j.str.2013.06.020. PMID 23932589.
  • Piston DW, Kremers GJ. (2007). Fluorescent protein FRET: the good, the bad and the ugly. Trends Biochem Sci. 32 (9): 407—414. PMID 17764955.
  • Haustein E, Schwille P. (2007). Fluorescence correlation spectroscopy: novel variations of an established technique. Annu Rev Biophys Biomol Struct. 36: 151—169. PMID 17477838.
  • Hormeño S, Arias-Gonzalez JR. (2006). Exploring mechanochemical processes in the cell with optical tweezers. Biol Cell. 98 (12): 679—695. PMID 17105446.
  • Zlatanova J, Leuba SH. (2003). Magnetic tweezers: a sensitive tool to study DNA and chromatin at the single-molecule level. Biochem Cell Biol. 81 (3): 151—159. PMID 12897848.
  • Müller DJ, Sapra KT, Scheuring S, Kedrov A, Frederix PL, Fotiadis D, Engel A. (2006). Single-molecule studies of membrane proteins. Curr Opin Struct Biol. 16 (4): 489—495. PMID 16797964.
  • Hinterdorfer P, Dufrêne YF. (2006). Detection and localization of single molecular recognition events using atomic force microscopy. Nat Methods. 3 (5): 347—355. PMID 16628204.
  • Greenleaf WJ, Woodside MT, Block SM. (2007). High-resolution, single-molecule measurements of biomolecular motion. Annu Rev Biophys Biomol Struct. 36: 171—190. PMID 17328679.
  • G. Oster and H. Wang (2000). Reverse engineering a protein: The mechanochemistry of ATP synthase. Biochemica et Biophysica Acta (Bioenergetics). 1458: 482—510. PMID 10838060.
  • Xing, J., J-C. Liao, G. Oster (2005). Making ATP. PNAS. 102 (46): 16539—16546. PMID 16217018.
  • Kruse K, Howard M, Margolin W. (2007). An experimentalist's guide to computational modelling of the Min system. Mol Microbiol. 63 (5): 1279—1284. PMID 17302810.
  • Zhang Y, Skolnick J (2005). The protein structure prediction problem could be solved using the current PDB library. Proc Natl Acad Sci USA. 102 (4): 1029—1034. PMID 15653774.
  • Kuhlman B, Dantas G, Ireton GC, Varani G, Stoddard BL, Baker D (2003). Design of a novel globular protein fold with atomic-level accuracy. Science. 302 (5649): 1364—1368. PMID 14631033.
  • Herges T, Wenzel W (2005). In silico folding of a three helix protein and characterization of its free-energy landscape in an all-atom force field. Phys Rev Let. 94 (1): 018101. PMID 15698135.
  • Hoffmann M, Wanko M, Strodel P, Konig PH, Frauenheim T, Schulten K, Thiel W, Tajkhorshid E, Elstner M (2006). Color tuning in rhodopsins: the mechanism for the spectral shift between bacteriorhodopsin and sensory rhodopsin II. J Am Chem Soc. 128 (33): 10808—10818. PMID 16910676.
  • Shaun M Lippow, and Bruce Tidor (2007). Progress in computational protein design. Curr Opin Biotechnol. 18 (4): 305—11. PMID 17644370.
  • Loren L. Looger, Mary A. Dwyer, James J. Smith and Homme W. Hellinga (2003). Computational design of receptor and sensor proteins with novel functions. Nature. 423: 185—190. doi:10.1038/nature01556. PMID 12736688.
  • Bassil I. Dahiyat and Stephen L. Mayo. De Novo Protein Design: Fully Automated Sequence Selection. Science. PMID 9367772.
  • Eijsink VG, Gåseidnes S, Borchert TV, van den Burg B. (2005). Directed evolution of enzyme stability. Biomol Eng. 22 (1-3): 21—30. PMID 15857780.
  • Tamerler C, Sarikaya M. (2007). Molecular biomimetics: utilizing nature's molecular ways in practical engineering. Acta Biomater. 3 (3:pages = 289—299). PMID 17257913.
  • Thomas Scheibel (2005). Protein fibers as performance proteins: new technologies and applications. Curr Opin Biotechnol. 16 (4): 427—433. doi:10.1016/j.copbio.2005.05.005. PMID 15950453.

ncbi.nlm.nih.gov

ovh.org

isoelectric.ovh.org

qmul.ac.uk

chem.qmul.ac.uk

sciencemag.org

  • Mohammad Movassaghi and Eric N. Jacobsen (2002). The Simplest Enzyme. Science. 298 (5600): 1904—1905. Архів оригіналу за 17 жовтня 2007. Процитовано 15 січня 2008.

uiuc.edu

ks.uiuc.edu

  • Theoretical and Computational Biophysics group, Univ. of Illinois an Urbana-Champain. The Nuclear Pore Complex. Архів оригіналу за 20 червня 2013. Процитовано 15 січня 2008.

warbletoncouncil.org

uk.warbletoncouncil.org

web.archive.org

  • Sumner, JB (1926). The Isolation and Crystallization of the Enzyme Urease. Preliminary Paper (PDF). J Biol Chem. 69: 435—41. Архів оригіналу (PDF) за 29 вересня 2007. Процитовано 14 січня 2008.
  • Mohammad Movassaghi and Eric N. Jacobsen (2002). The Simplest Enzyme. Science. 298 (5600): 1904—1905. Архів оригіналу за 17 жовтня 2007. Процитовано 15 січня 2008.
  • S.E. Jackson (Aug 1998). How do small single-domain proteins fold? (PDF). Fold. Des. 3: R81—R91. ISSN 1359-0278. Архів оригіналу (PDF) за 1 квітня 2011. Процитовано 7 січня 2011.
  • Functional categories of proteins. NCBI. Архів оригіналу за 4 липня 2008. Процитовано 1 березня 2008.
  • Yannay-Cohen N, Razin E. (2000). Translation and transcription: the dual functionality of LysRS in mast cells. Mol Cells. 22: 127—32. PMID 17085962. Архів оригіналу за 18 червня 2008. Процитовано 8 лютого 2008.
  • Bairoch A. (2000). The ENZYME database in 2000 (PDF). Nucleic Acids Res. 28: 304—305. PMID 10592255. Архів оригіналу (PDF) за 1 червня 2011. Процитовано 16 січня 2008.
  • Cowie R.J. and Stanton G.B. Axoplasmic Transport and Neuronal Responses to Injury. Howard University College of Medicine. Архів оригіналу за 20 червня 2010. Процитовано 25 січня 2007.
  • Білок віком у 4 мільярди років // Збруч, 10.08.2013. Архів оригіналу за 8 листопада 2013. Процитовано 16 серпня 2013.

webcitation.org

wikipedia.org

en.wikipedia.org

worldcat.org

zbruc.eu