Неділько Будіса (Ukrainian Wikipedia)

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

refsWebsite
Global rank Ukrainian rank
4th place
5th place
2nd place
4th place
1st place
1st place
18th place
74th place
7,479th place
low place
low place
low place
43rd place
134th place
1,624th place
1,659th place
low place
low place
8,208th place
6,309th place
low place
low place
low place
7,056th place
1,293rd place
539th place
5th place
9th place
low place
low place

biofuture-wettbewerb.de

cipsm.de

deepdyve.com

doi.org

doi.org

  • Budisa, Nediljko (2005). The book at the Wiley Online Library. doi:10.1002/3527607188. ISBN 9783527312436.
  • Budisa, N. (2004). Prolegomena to future efforts on genetic code engineering by expanding its amino acid repertoire. Angewandte Chemie International Edition. 43: 3387—3428. doi:10.1002/anie.20030064 (неактивний 2019-05-18).{{cite journal}}: Обслуговування CS1: Сторінки із неактивним DOI станом на травень 2019 (посилання)
  • Lepthien, S.; Merkel, L.; Budisa, N. (2010). In Vivo Double and Triple Labeling of Proteins Using Synthetic Amino Acids. Angewandte Chemie International Edition. 49 (32): 5446—5450. doi:10.1002/anie.201000439. PMID 20575122.
  • Bohlke, N.; Budisa, N. (2014). Sense codon emancipation for proteome-wide incorporation of noncanonical amino acids: rare isoleucine codon AUA as a target for genetic code expansion. FEMS Microbiology Letters. 351 (2): 133—44. doi:10.1111/1574-6968.12371. PMC 4237120. PMID 24433543.
  • Völler, J.-S.; Budisa, N. (2017). Coupling genetic code expansion and metabolic engineering for synthetic cells. Current Opinion in Biotechnology. 48: 1—7. doi:10.1016/j.copbio.2017.02.002. PMID 28237511.
  • Exner, M. P.; Kuenzl, S.; Schwagerus, S.; To, T.; Ouyang, Z.; Hoesl, M. G.; Lensen, M. C.; Hackenberger, C. P. R.; Panke, S. (2017). Design of an S-Allylcysteine in situ production and incorporation system based on a novel pyrrolysyl-tRNA synthetase variant. ChemBioChem. 18 (1): 85—90. doi:10.1002/cbic.201600537. PMID 27862817.
  • Lepthien, S.; Hoesl, M. G.; Merkel, L.; Budisa, N. (2008). Azatryptophans endow proteins with intrinsic blue fluorescence. Proc. Natl. Acad. Sci. USA. 105 (42): 16095—16100. Bibcode:2008PNAS..10516095L. doi:10.1073/pnas.0802804105. PMC 2571030. PMID 18854410.
  • Baumann, T.; Hauf, M.; Schildhauer, F.; Eberl, K.; Durkin, P. M.; Deniz, E.; Löffler, J. G.; Acevedo-Rocha, C. G.; Jaric, J. (2019). Site‐Resolved Observation of Vibrational Energy Transfer Using a Genetically Encoded Ultrafast Heater. Angewandte Chemie International Edition. 58 (9): 2527—2903. doi:10.1002/anie.201812995. PMID 30589180.
  • Agostini, F.; Völler, J-S.; Koksch, B.; Acevedo-Rocha, C. G.; Kubyshkin, V.; Budisa, N. (2017). Biocatalysis with Unnatural Amino Acids: Enzymology Meets Xenobiology. Angewandte Chemie International Edition. 56 (33): 9680—9703. doi:10.1002/anie.201610129. PMID 28085996.
  • Budisa, N.; Steipe, B.; Demange, P.; Eckerskorn, C.; Kellermann, J.; Huber, R. (1995). High level biosynthetic substitution of methionine in proteins by its analogues 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli. Eur. J. Biochem. 230 (2): 788—796. doi:10.1111/j.1432-1033.1995.0788h.x. PMID 7607253.
  • Seifert, M. H.; Ksiazek, D.; Smialowski, P.; Azim, M. K.; Budisa, N.; Holak, T. A. (2002). Slow Conformational Exchange Processes in Green Fluorescent Protein Variants evidenced by NMR Spectroscopy. J. Am. Chem. Soc. 124 (27): 7932—7942. doi:10.1021/ja0257725. PMID 12095337.
  • Budisa, N.; Minks, C.; Medrano, F. J.; Lutz, J.; Huber, R.; Moroder, L. (1998). Residue specific bioincorporation of non-natural biologically active amino acids into proteins as possible drug carriers. Structure and stability of per-thiaproline mutant or annexin V. Proc. Natl. Acad. Sci. USA. 95 (2): 455—459. doi:10.1073/pnas.95.2.455. PMC 18441. PMID 9435213.
  • Budisa, N. (2013). Expanded genetic code for the engineering of ribosomally synthetized and post-translationally modified peptide natural products (RiPPs). Current Opinion in Biotechnology. 24 (4): 591—598. doi:10.1016/j.copbio.2013.02.026. PMID 23537814.
  • Hauf, M.; Richter, F.; Schneider, T.; Faidt, T.; Martins, B. M.; Baumann, T.; Durkin, P.; Dobbek, H.; Jacobs, K. (2017). Photoactivatable mussel-based underwater adhesive proteins by an expanded genetic code. ChemBioChem. 18 (18): 1819—1823. doi:10.1002/cbic.201700327. PMID 28650092.
  • Wolschner, C.; Giese, A.; Kretzschmar, H.; Huber, R.; Moroder, L.; Budisa, N. (2009). Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein. Proc. Natl. Acad. Sci. USA. 106 (19): 7756—7761. Bibcode:2009PNAS..106.7756W. doi:10.1073/pnas.0902688106. PMC 2674404. PMID 19416900.
  • Steiner, T.; Hess, P.; Bae, J. H.; Moroder, L.; Budisa, N. (2008). Synthetic Biology of Proteins: Tuning GFP´s Folding and Stability with Fluoroproline. PLOS ONE. 3 (2): e1680. Bibcode:2008PLoSO...3.1680S. doi:10.1371/journal.pone.0001680. PMC 2243022. PMID 18301757.{{cite journal}}: Обслуговування CS1: Сторінки із непозначеним DOI з безкоштовним доступом (посилання)
  • Doerfel, L. K.; Wohlgemuth, I.; Kubyshkin, V.; Starosta, A. L.; Wilson, D. N.; Budisa, N. (2015). Entropic Contribution of Elongation Factor P to Proline Positioning at the Catalytic Center of the Ribosome. J. Am. Chem. Soc. 137 (40): 12997—13006. doi:10.1021/jacs.5b07427. PMID 26384033.
  • Kubyshkin, V.; Grage, S. L.; Bürck, J.; Ulrich, A. S.; Budisa, N. (2018). Transmembrane Polyproline Helix. J. Phys. Chem. Lett. 9 (9): 2170—2174. doi:10.1021/acs.jpclett.8b00829. PMID 29638132.
  • Kubyshkin, V.; Budisa, N. (2019). Anticipating alien cells with alternative genetic codes: away from the alanine world!. Current Opinion in Biotechnology. 60: 242—249. doi:10.1016/j.copbio.2019.05.006. PMID 31279217.
  • Kubyshkin, V.; Acevedo-Rocha, C. G.; Budisa, N. (2017). On universal coding events in protein biogenesis. Biosystems. 164: 16—25. doi:10.1016/j.biosystems.2017.10.004. PMID 29030023.
  • Hoesl, M. G.; Oehm, S.; Durkin, P.; Darmon, E.; Peil, L.; Aerni, H.-R.; Rappsilber, J.; Rinehart, J.; Leach, D. (2015). Chemical evolution of a bacterial proteome. Angewandte Chemie International Edition. 54 (34): 10030—10034. doi:10.1002/anie.201502868. PMC 4782924. PMID 26136259. NIHMSID: NIHMS711205
  • Kubyshkin, V.; Budisa, N. (2017). Synthetic alienation of microbial organisms by using genetic code engineering: Why and how?. Biotechnology Journal. 12 (8): 1600097. doi:10.1002/biot.201600097. PMID 28671771.
  • Diwo, C.; Budisa, N. (2019). Alternative Biochemistries for Alien Life: Basic Concepts and Requirements for the Design of a Robust Biocontainment System in Genetic Isolation. Genes. 10 (1): 17. doi:10.3390/genes10010017. PMID 30597824.{{cite journal}}: Обслуговування CS1: Сторінки із непозначеним DOI з безкоштовним доступом (посилання)
  • Acevedo-Rocha, C. G.; Budisa, N. (2011). On the Road towards Chemically Modified Organisms Endowed with a Genetic Firewall. Angewandte Chemie International Edition. 50 (31): 6960—6962. doi:10.1002/anie.201103010. PMID 21710510.
  • Schmidt, M.; Pei, L.; Budisa, N. (2018). Xenobiology: State-of-the-art, Ethics and Philosophy of new-to-nature organisms. Т. 162. с. 301—315. doi:10.1007/10_2016_14. ISBN 978-3-319-55317-7. ISSN 0724-6145. PMID 28567486.

dx.doi.org

harvard.edu

ui.adsabs.harvard.edu

mpg.de

biochem.mpg.de

nih.gov

pubmed.ncbi.nlm.nih.gov

ncbi.nlm.nih.gov

orcid.org

pub.orcid.org

pnas.org

tu-berlin.de

biocat.tu-berlin.de

igem.biocat.tu-berlin.de

unicat.tu-berlin.de

umanitoba.ca

sci.umanitoba.ca

unisyscat.de

web.archive.org

wikidata.org

worldcat.org