二次構造 (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "二次構造" in Japanese language version.

refsWebsite

Global rank Japanese rank

31nih.gov

4^th place

24^th place

24doi.org

2^nd place

6^th place

1amazon.co.jp

554^th place

50^th place

1curtin.edu.au

low place

1ucdavis.edu

1,873^rd place

4,672^nd place

1worldcat.org

5^th place

19^th place

1monash.edu.au

8,084^th place

low place

1swmed.edu

low place

amazon.co.jp (Global: 554^th place; Japanese: 50^th place)

Linderstrøm-Lang KU (1952). Lane Medical Lectures: Proteins and Enzymes. Stanford University Press. pp. 115. ASIN B0007J31SC

curtin.edu.au (Global: low place; Japanese: low place)

biomed.curtin.edu.au

Steven Bottomley (2004年). “Interactive Protein Structure Tutorial”. 2011年1月9日閲覧。

doi.org (Global: 2^nd place; Japanese: 6^th place)

“Kaj Ulrik Linderstrøm-Lang (1896–1959)”. Protein Sci. 6 (5): 1092–100. (1997). doi:10.1002/pro.5560060516. PMC 2143695. PMID 9144781. "He had already introduced the concepts of the primary, secondary, and tertiary structure of proteins in the third Lane Lecture (Linderstram-Lang, 1952)"
“Secondary structure and rigidity in model proteins”. Soft Matter 9 (40): 9548–56. (October 2013). doi:10.1039/C3SM50807B. PMID 26029761.
“Rigidity, secondary structure, and the universality of the boson peak in proteins”. Biophysical Journal 106 (12): 2667–74. (June 2014). doi:10.1016/j.bpj.2014.05.009. PMC 4070067. PMID 24940784.
“Coherent neutron scattering and collective dynamics in the protein, GFP”. Biophys. J. 105 (9): 2182–87. (2013). doi:10.1016/j.bpj.2013.09.029. PMC 3824694. PMID 24209864.
“Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features”. Biopolymers 22 (12): 2577–637. (Dec 1983). doi:10.1002/bip.360221211. PMID 6667333.
“Identification of structural motifs from protein coordinate data: secondary structure and first-level supersecondary structure”. Proteins 3 (2): 71–84. (1988). doi:10.1002/prot.340030202. PMID 3399495.
“Knowledge-based protein secondary structure assignment”. Proteins 23 (4): 566–79. (Dec 1995). doi:10.1002/prot.340230412. PMID 8749853.
Calligari, Paolo A.; Kneller, Gerald R. (2012-12-01). “ScrewFit: combining localization and description of protein secondary structure” (英語). Acta Crystallographica Section D 68 (12): 1690–1693. doi:10.1107/s0907444912039029. ISSN 0907-4449.
“Minimum message length inference of secondary structure from protein coordinate data”. Bioinformatics 28 (12): i97–i105. (Jun 2012). doi:10.1093/bioinformatics/bts223. PMC 3371855. PMID 22689785.
“Spectroscopic methods for analysis of protein secondary structure”. Anal. Biochem. 277 (2): 167–76. (2000). doi:10.1006/abio.1999.4320. PMID 10625503.
“Rapid protein fold determination using unassigned NMR data”. Proc. Natl. Acad. Sci. U.S.A. 100 (26): 15404–09. (2003). doi:10.1073/pnas.2434121100. PMC 307580. PMID 14668443.
“Prediction of protein conformation”. Biochemistry 13 (2): 222–45. (Jan 1974). doi:10.1021/bi00699a002. PMID 4358940.
“Empirical predictions of protein conformation”. Annu. Rev. Biochem. 47: 251–76. (1978). doi:10.1146/annurev.bi.47.070178.001343. PMID 354496.
“Prediction of the secondary structure of proteins from their amino acid sequence”. Adv. Enzymol. Relat. Areas Mol. Biol. 47: 45–148. (1978). doi:10.1002/9780470122921.ch2. PMID 364941.
“Integrating protein secondary structure prediction and multiple sequence alignment”. Current Protein & Peptide Science 5 (4): 249–66. (Aug 2004). doi:10.2174/1389203043379675. PMID 15320732.
“Protein secondary structure prediction”. Methods Mol. Biol. 609: 327–48. (2010). doi:10.1007/978-1-60327-241-4_19. PMID 20221928.
“SAM-T08, HMM-based protein structure prediction”. Nucleic Acids Res. 37 (Web Server issue): W492–97. (2009). doi:10.1093/nar/gkp403. PMC 2703928. PMID 19483096.
“Porter: a new, accurate server for protein secondary structure prediction”. Bioinformatics 21 (8): 1719–20. (2005). doi:10.1093/bioinformatics/bti203. PMID 15585524.
“PredictProtein—an open resource for online prediction of protein structural and functional features”. Nucleic Acids Res. 42 (Web Server issue): W337–43. (2014). doi:10.1093/nar/gku366. PMC 4086098. PMID 24799431.
“Combining prediction of secondary structure and solvent accessibility in proteins”. Proteins 59 (3): 467–75. (2005). doi:10.1002/prot.20441. PMID 15768403.
“The effect of long-range interactions on the secondary structure formation of proteins”. Protein Science 14 (8): 1955–963. (Aug 2005). doi:10.1110/ps.051479505. PMC 2279307. PMID 15987894.
“Structural classification of thioredoxin-like fold proteins”. Proteins 58 (2): 376–88. (2005). doi:10.1002/prot.20329. PMID 15558583. "Since the fold definition should include only the core secondary structural elements that are present in the majority of homologs, we define the thioredoxin-like fold as a two-layer / sandwich with the βαββαβ secondary-structure pattern."
“Alpha helices are more robust to mutations than beta strands”. PLoS Computational Biology 12 (12): 1–16. (2016). doi:10.1371/journal.pcbi.1005242. PMID 27935949.
“Global analysis of protein folding using massively parallel design, synthesis, and testing”. Science 357 (6347): 168–175. (2017). doi:10.1126/science.aan0693. PMID 28706065.

monash.edu.au (Global: 8,084^th place; Japanese: low place)

lcb.infotech.monash.edu.au

Arun Konagurthu. “SST: Protein Secondary structural assignment using Minimum Message Length inference”. Laboratory of Computational Biology, Monash University. 2018年1月4日閲覧。

nih.gov (Global: 4^th place; Japanese: 24^th place)

pubmed.ncbi.nlm.nih.gov

“Kaj Ulrik Linderstrøm-Lang (1896–1959)”. Protein Sci. 6 (5): 1092–100. (1997). doi:10.1002/pro.5560060516. PMC 2143695. PMID 9144781. "He had already introduced the concepts of the primary, secondary, and tertiary structure of proteins in the third Lane Lecture (Linderstram-Lang, 1952)"
“Secondary structure and rigidity in model proteins”. Soft Matter 9 (40): 9548–56. (October 2013). doi:10.1039/C3SM50807B. PMID 26029761.
“Rigidity, secondary structure, and the universality of the boson peak in proteins”. Biophysical Journal 106 (12): 2667–74. (June 2014). doi:10.1016/j.bpj.2014.05.009. PMC 4070067. PMID 24940784.
“Coherent neutron scattering and collective dynamics in the protein, GFP”. Biophys. J. 105 (9): 2182–87. (2013). doi:10.1016/j.bpj.2013.09.029. PMC 3824694. PMID 24209864.
“Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features”. Biopolymers 22 (12): 2577–637. (Dec 1983). doi:10.1002/bip.360221211. PMID 6667333.
“Identification of structural motifs from protein coordinate data: secondary structure and first-level supersecondary structure”. Proteins 3 (2): 71–84. (1988). doi:10.1002/prot.340030202. PMID 3399495.
“Knowledge-based protein secondary structure assignment”. Proteins 23 (4): 566–79. (Dec 1995). doi:10.1002/prot.340230412. PMID 8749853.
“Minimum message length inference of secondary structure from protein coordinate data”. Bioinformatics 28 (12): i97–i105. (Jun 2012). doi:10.1093/bioinformatics/bts223. PMC 3371855. PMID 22689785.
“Spectroscopic methods for analysis of protein secondary structure”. Anal. Biochem. 277 (2): 167–76. (2000). doi:10.1006/abio.1999.4320. PMID 10625503.
“Rapid protein fold determination using unassigned NMR data”. Proc. Natl. Acad. Sci. U.S.A. 100 (26): 15404–09. (2003). doi:10.1073/pnas.2434121100. PMC 307580. PMID 14668443.
“Prediction of protein conformation”. Biochemistry 13 (2): 222–45. (Jan 1974). doi:10.1021/bi00699a002. PMID 4358940.
“Empirical predictions of protein conformation”. Annu. Rev. Biochem. 47: 251–76. (1978). doi:10.1146/annurev.bi.47.070178.001343. PMID 354496.
“Prediction of the secondary structure of proteins from their amino acid sequence”. Adv. Enzymol. Relat. Areas Mol. Biol. 47: 45–148. (1978). doi:10.1002/9780470122921.ch2. PMID 364941.
“Integrating protein secondary structure prediction and multiple sequence alignment”. Current Protein & Peptide Science 5 (4): 249–66. (Aug 2004). doi:10.2174/1389203043379675. PMID 15320732.
“Protein secondary structure prediction”. Methods Mol. Biol. 609: 327–48. (2010). doi:10.1007/978-1-60327-241-4_19. PMID 20221928.
“SAM-T08, HMM-based protein structure prediction”. Nucleic Acids Res. 37 (Web Server issue): W492–97. (2009). doi:10.1093/nar/gkp403. PMC 2703928. PMID 19483096.
“Porter: a new, accurate server for protein secondary structure prediction”. Bioinformatics 21 (8): 1719–20. (2005). doi:10.1093/bioinformatics/bti203. PMID 15585524.
“PredictProtein—an open resource for online prediction of protein structural and functional features”. Nucleic Acids Res. 42 (Web Server issue): W337–43. (2014). doi:10.1093/nar/gku366. PMC 4086098. PMID 24799431.
“Combining prediction of secondary structure and solvent accessibility in proteins”. Proteins 59 (3): 467–75. (2005). doi:10.1002/prot.20441. PMID 15768403.
“The effect of long-range interactions on the secondary structure formation of proteins”. Protein Science 14 (8): 1955–963. (Aug 2005). doi:10.1110/ps.051479505. PMC 2279307. PMID 15987894.
“Structural classification of thioredoxin-like fold proteins”. Proteins 58 (2): 376–88. (2005). doi:10.1002/prot.20329. PMID 15558583. "Since the fold definition should include only the core secondary structural elements that are present in the majority of homologs, we define the thioredoxin-like fold as a two-layer / sandwich with the βαββαβ secondary-structure pattern."
“Alpha helices are more robust to mutations than beta strands”. PLoS Computational Biology 12 (12): 1–16. (2016). doi:10.1371/journal.pcbi.1005242. PMID 27935949.
“Global analysis of protein folding using massively parallel design, synthesis, and testing”. Science 357 (6347): 168–175. (2017). doi:10.1126/science.aan0693. PMID 28706065.

pmc.ncbi.nlm.nih.gov

“Kaj Ulrik Linderstrøm-Lang (1896–1959)”. Protein Sci. 6 (5): 1092–100. (1997). doi:10.1002/pro.5560060516. PMC 2143695. PMID 9144781. "He had already introduced the concepts of the primary, secondary, and tertiary structure of proteins in the third Lane Lecture (Linderstram-Lang, 1952)"
“Rigidity, secondary structure, and the universality of the boson peak in proteins”. Biophysical Journal 106 (12): 2667–74. (June 2014). doi:10.1016/j.bpj.2014.05.009. PMC 4070067. PMID 24940784.
“Coherent neutron scattering and collective dynamics in the protein, GFP”. Biophys. J. 105 (9): 2182–87. (2013). doi:10.1016/j.bpj.2013.09.029. PMC 3824694. PMID 24209864.
“Minimum message length inference of secondary structure from protein coordinate data”. Bioinformatics 28 (12): i97–i105. (Jun 2012). doi:10.1093/bioinformatics/bts223. PMC 3371855. PMID 22689785.
“Rapid protein fold determination using unassigned NMR data”. Proc. Natl. Acad. Sci. U.S.A. 100 (26): 15404–09. (2003). doi:10.1073/pnas.2434121100. PMC 307580. PMID 14668443.
“SAM-T08, HMM-based protein structure prediction”. Nucleic Acids Res. 37 (Web Server issue): W492–97. (2009). doi:10.1093/nar/gkp403. PMC 2703928. PMID 19483096.
“PredictProtein—an open resource for online prediction of protein structural and functional features”. Nucleic Acids Res. 42 (Web Server issue): W337–43. (2014). doi:10.1093/nar/gku366. PMC 4086098. PMID 24799431.
“The effect of long-range interactions on the secondary structure formation of proteins”. Protein Science 14 (8): 1955–963. (Aug 2005). doi:10.1110/ps.051479505. PMC 2279307. PMID 15987894.

swmed.edu (Global: low place; Japanese: low place)

prodata.swmed.edu

“Structural classification of thioredoxin-like fold proteins”. Proteins 58 (2): 376–88. (2005). doi:10.1002/prot.20329. PMID 15558583. "Since the fold definition should include only the core secondary structural elements that are present in the majority of homologs, we define the thioredoxin-like fold as a two-layer / sandwich with the βαββαβ secondary-structure pattern."

ucdavis.edu (Global: 1,873^rd place; Japanese: 4,672^nd place)

nook.cs.ucdavis.edu

“Knowledge-based protein secondary structure assignment”. Proteins 23 (4): 566–79. (Dec 1995). doi:10.1002/prot.340230412. PMID 8749853.

worldcat.org (Global: 5^th place; Japanese: 19^th place)

search.worldcat.org

Calligari, Paolo A.; Kneller, Gerald R. (2012-12-01). “ScrewFit: combining localization and description of protein secondary structure” (英語). Acta Crystallographica Section D 68 (12): 1690–1693. doi:10.1107/s0907444912039029. ISSN 0907-4449.

二次構造 (Japanese Wikipedia)

amazon.co.jp (Global: 554th place; Japanese: 50th place)

curtin.edu.au (Global: low place; Japanese: low place)

biomed.curtin.edu.au

doi.org (Global: 2nd place; Japanese: 6th place)

monash.edu.au (Global: 8,084th place; Japanese: low place)

lcb.infotech.monash.edu.au

nih.gov (Global: 4th place; Japanese: 24th place)

pubmed.ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

swmed.edu (Global: low place; Japanese: low place)

prodata.swmed.edu

ucdavis.edu (Global: 1,873rd place; Japanese: 4,672nd place)

nook.cs.ucdavis.edu

worldcat.org (Global: 5th place; Japanese: 19th place)

search.worldcat.org

amazon.co.jp (Global: 554^th place; Japanese: 50^th place)

doi.org (Global: 2^nd place; Japanese: 6^th place)

monash.edu.au (Global: 8,084^th place; Japanese: low place)

nih.gov (Global: 4^th place; Japanese: 24^th place)

ucdavis.edu (Global: 1,873^rd place; Japanese: 4,672^nd place)

worldcat.org (Global: 5^th place; Japanese: 19^th place)