Протеин (Serbian Wikipedia)

Analysis of information sources in references of the Wikipedia article "Протеин" in Serbian language version.

refsWebsite

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9nih.gov

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9doi.org

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2upenn.edu

702^nd place

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2nature.com

234^th place

287^th place

2web.archive.org

1^st place

2sciencemag.org

857^th place

569^th place

2whfreeman.com

low place

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1jbc.org

4,455^th place

2,178^th place

1books.google.com

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1archive.org

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1garlandscience.com

low place

1,011^th place

1oxfordjournals.org

1,389^th place

438^th place

1ebi.ac.uk

5,849^th place

3,688^th place

1acs.org

1,248^th place

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1psu.edu

207^th place

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1aps.org

1,503^rd place

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acs.org

pubs.acs.org

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—18. doi:10.1021/ja062082i.

aps.org

prl.aps.org

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. doi:10.1103/PhysRevLett.94.018101.

archive.org

Fulton A, Isaacs W (1991). „Titin, a huge, elastic sarcomeric protein with a probable role in morphogenesis”. Bioessays. 13 (4): 157—61. PMID 1859393. doi:10.1002/bies.950130403.

books.google.com

Dobson, CM (2000). „The nature and significance of protein folding”. Ур.: Pain, RH. Mechanisms of Protein Folding (2 изд.). New York, NY: Oxford University Press. ISBN 978-0-19-963788-1.

doi.org

Muirhead H, Perutz M (1963). „Structure of haemoglobin. A three-dimensional fourier synthesis of reduced human haemoglobin at 5.5 A resolution”. Nature. 199 (4894): 633—8. PMID 14074546. doi:10.1038/199633a0.
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. doi:10.1038/181662a0.
Fulton A, Isaacs W (1991). „Titin, a huge, elastic sarcomeric protein with a probable role in morphogenesis”. Bioessays. 13 (4): 157—61. PMID 1859393. doi:10.1002/bies.950130403.
Schwarzer D, Cole P (2005). „Protein semisynthesis and expressed protein ligation: chasing a protein's tail”. Curr Opin Chem Biol. 9 (6): 561—9. PMID 1859393. doi:10.1016/j.cbpa.2005.09.018.
Radzicka A, Wolfenden R (1995). „A proficient enzyme”. Science. 267 (6): 90—931. PMID 7809611. doi:10.1126/science.7809611.
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—18. doi:10.1021/ja062082i.
Zagrovic B, Snow CD, Shirts MR, Pande VS (2002). „Simulation of folding of a small alpha-helical protein in atomistic detail using worldwide-distributed computing”. J Mol Biol. 323 (5): 927—37. doi:10.1016/S0022-2836(02)00997-X.
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. doi:10.1103/PhysRevLett.94.018101.
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—8. doi:10.1126/science.1089427.

ebi.ac.uk

„The Catalytic Site Atlas at The European Bioinformatics Institute”. Архивирано из оригинала 03. 08. 2013. г. Приступљено 05. 07. 2010.

garlandscience.com

Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.

jbc.org

Sumner, JB (1926). „The Isolation and Crystallization of the Enzyme Urease. Preliminary Paper” (PDF). J Biol Chem. 69: 435—41.

nature.com

Muirhead H, Perutz M (1963). „Structure of haemoglobin. A three-dimensional fourier synthesis of reduced human haemoglobin at 5.5 A resolution”. Nature. 199 (4894): 633—8. PMID 14074546. doi:10.1038/199633a0.
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. doi:10.1038/181662a0.

nih.gov

ncbi.nlm.nih.gov

Muirhead H, Perutz M (1963). „Structure of haemoglobin. A three-dimensional fourier synthesis of reduced human haemoglobin at 5.5 A resolution”. Nature. 199 (4894): 633—8. PMID 14074546. doi:10.1038/199633a0.
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. doi:10.1038/181662a0.
Fulton A, Isaacs W (1991). „Titin, a huge, elastic sarcomeric protein with a probable role in morphogenesis”. Bioessays. 13 (4): 157—61. PMID 1859393. doi:10.1002/bies.950130403.
Bruckdorfer T, Marder O, Albericio F (2004). „From production of peptides in milligram amounts for research to multi-tons quantities for drugs of the future”. Curr Pharm Biotechnol. 5 (1): 29—43. PMID 14965208.
Schwarzer D, Cole P (2005). „Protein semisynthesis and expressed protein ligation: chasing a protein's tail”. Curr Opin Chem Biol. 9 (6): 561—9. PMID 1859393. doi:10.1016/j.cbpa.2005.09.018.
Gonen T, Cheng Y, Sliz P, Hiroaki Y, Fujiyoshi Y, Harrison SC, Walz T (2005). „Lipid-protein interactions in double-layered two-dimensional AQP0 crystals”. Nature. 438 (7068): 633—8. PMID 16319884.
Walian P, Cross TA, Jap BK (2004). „Structural genomics of membrane proteins”. Genome Biol. 5 (4): 215.
Bairoch, A. (2000). „The ENZYME database in 2000”. Nucleic Acids Res. 28: 304—305. PMID 10592255.
Radzicka A, Wolfenden R (1995). „A proficient enzyme”. Science. 267 (6): 90—931. PMID 7809611. doi:10.1126/science.7809611.

oxfordjournals.org

nar.oxfordjournals.org

Bairoch, A. (2000). „The ENZYME database in 2000”. Nucleic Acids Res. 28: 304—305. PMID 10592255.

psu.edu

citeseerx.ist.psu.edu

Zagrovic B, Snow CD, Shirts MR, Pande VS (2002). „Simulation of folding of a small alpha-helical protein in atomistic detail using worldwide-distributed computing”. J Mol Biol. 323 (5): 927—37. doi:10.1016/S0022-2836(02)00997-X.

sciencemag.org

Radzicka A, Wolfenden R (1995). „A proficient enzyme”. Science. 267 (6): 90—931. PMID 7809611. doi:10.1126/science.7809611.
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—8. doi:10.1126/science.1089427.

upenn.edu

chem.upenn.edu

Donald Voet; Judith G. Voet (2005). „Chapter 7. Covalent structure of proteins and nucleic acids”. Biochemistry (3 изд.). Wiley. ISBN 9780471193500.
Donald Voet; Judith G. Voet (2005). „Chapter 8. Three-Dimensional structures of proteins”. Biochemistry (3 изд.). Wiley. ISBN 9780471193500.

web.archive.org

Lodish H, Berk A, Matsudaira P, Kaiser CA, Krieger M, Scott MP, Zipurksy SL, Darnell J (2004). Molecular Cell Biology (5 изд.). New York, NY.: WH Freeman and Company. Архивирано из оригинала 17. 07. 2011. г. Приступљено 05. 07. 2010.
„The Catalytic Site Atlas at The European Bioinformatics Institute”. Архивирано из оригинала 03. 08. 2013. г. Приступљено 05. 07. 2010.

whfreeman.com

David L. Nelson; Michael M. Cox (2005). Principles of Biochemistry (IV изд.). New York: W. H. Freeman. ISBN 0-7167-4339-6.

bcs.whfreeman.com

Lodish H, Berk A, Matsudaira P, Kaiser CA, Krieger M, Scott MP, Zipurksy SL, Darnell J (2004). Molecular Cell Biology (5 изд.). New York, NY.: WH Freeman and Company. Архивирано из оригинала 17. 07. 2011. г. Приступљено 05. 07. 2010.