புரதம் மடிப்படைதல் (Tamil Wikipedia)

Analysis of information sources in references of the Wikipedia article "புரதம் மடிப்படைதல்" in Tamil language version.

refsWebsite

Global rank Tamil rank

16nih.gov

4^th place

5^th place

15doi.org

2^nd place

4^th place

4wikipedia.org

low place

2archive.org

6^th place

8^th place

2fasebj.org

low place

6,587^th place

2pnas.org

1,293^rd place

347^th place

1nature.com

234^th place

115^th place

1sciencemag.org

857^th place

228^th place

1wiley.com

222^nd place

219^th place

1jbmb.or.kr

low place

1toolserver.org

low place

352^nd place

1wisc.edu

1,045^th place

408^th place

1biomednet.com

low place

1ucl.ac.uk

1,306^th place

805^th place

1biomolecular-modeling.com

low place

archive.org (Global: 6^th place; Tamil: 8^th place)

Anfinsen, C. (1972). "The formation and stabilization of protein structure". Biochem. J. 128 (4): 737–49. பப்மெட்:4565129. https://archive.org/details/sim_biochemical-journal_1972-07_128_4/page/737.
Kim, P. S., Baldwin, R. L. (1990). "Intermediates in the folding reactions of small proteins". Annu. Rev. Biochem. 59: 631–60. doi:10.1146/annurev.bi.59.070190.003215. பப்மெட்:2197986. https://archive.org/details/sim_annual-review-of-biochemistry_1990_59/page/631.

biomednet.com (Global: low place; Tamil: low place)

Jackson S. E. (August 1998). "How do small single-domain proteins fold?" (^{[தொடர்பிழந்த இணைப்பு]}). Fold Des 3 (4): R81–91. doi:10.1016/S1359-0278(98)00033-9. பப்மெட்:9710577. http://biomednet.com/elecref/13590278003R0081.

biomolecular-modeling.com (Global: low place; Tamil: low place)

"Protein folding" (by Molecular Dynamics).

doi.org (Global: 2^nd place; Tamil: 4^th place)

dx.doi.org

Dennis J. Selkoe (2003). "Folding proteins in fatal ways". Nature 426: pp. 900–904. doi:10.1038/nature02264. பப்மெட்:14685251. http://www.nature.com/nature/journal/v426/n6968/full/nature02264.html.
van den Berg, B., Wain, R., Dobson, C. M., Ellis R. J. (August 2000). "Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell". EMBO J. 19 (15): 3870–5. doi:10.1093/emboj/19.15.3870. பப்மெட்:10921869.
Rose, G., Fleming, P., Banavar, J., Maritan, A. (2006). "A backbone-based theory of protein folding". Proc. Natl. Acad. Sci. U.S.A. 103 (45): 16623–33. doi:10.1073/pnas.0606843103. பப்மெட்:17075053.
Deechongkit, S., Nguyen, H., Dawson, P. E., Gruebele, M., Kelly, J. W. (2004). "Context Dependent Contributions of Backbone H-Bonding to β-Sheet Folding Energetics". Nature 403 (45): 101–5. doi:10.1073/pnas.0606843103. பப்மெட்:17075053.
Anfinsen CB. (20 July 1973). "Principles that Govern the Folding of Protein Chains". Science. 181 (4096): 223-230. doi:10.1126/science.181.4096.223. http://www.sciencemag.org/cgi/pdf_extract/181/4096/223. பார்த்த நாள்: 21 ஜூலை 2010.
Venkataramanan Soundararajan, Rahul Raman, S. Raguram, V. Sasisekharan, Ram Sasisekharan (2010). "Atomic Interaction Networks in the Core of Protein Domains and Their Native Folds". PLoS ONE 5 (2): e9391. doi:10.1371/journal.pone.0009391.
Alexander, P. A., He Y., Chen, Y., Orban, J., Bryan, P. N. (2007). "The design and characterization of two proteins with 88% sequence identity but different structure and function". Proc Natl Acad Sci U S A. 104 (29): 11963–8. doi:10.1073/pnas.0700922104. பப்மெட்:17609385.
Takai, K., Nakamura, K., Toki, T., Tsunogai, U., Miyazaki, M., Miyazaki, J., Hirayama, H., Nakagawa, S., Nunoura, T., Horikoshi, K. (2008). "Cell proliferation at 122 °C and isotopically heavy CH4 production by a hyperthermophilic methanogen under high-pressure cultivation". Proc Natl Acad Sci USA 105: 10949–54. doi:10.1073/pnas.0712334105.
எஆசு:10.1146/annurev.biochem.75.101304.123901
This citation will be automatically completed in the next few minutes. You can jump the queue or expand by hand
Kim, P. S., Baldwin, R. L. (1990). "Intermediates in the folding reactions of small proteins". Annu. Rev. Biochem. 59: 631–60. doi:10.1146/annurev.bi.59.070190.003215. பப்மெட்:2197986. https://archive.org/details/sim_annual-review-of-biochemistry_1990_59/page/631.
Jackson S. E. (August 1998). "How do small single-domain proteins fold?" (^{[தொடர்பிழந்த இணைப்பு]}). Fold Des 3 (4): R81–91. doi:10.1016/S1359-0278(98)00033-9. பப்மெட்:9710577. http://biomednet.com/elecref/13590278003R0081.
Kubelka, J., Hofrichter, J., Eaton, W. A. (February 2004). "The protein folding 'speed limit'". Curr. Opin. Struct. Biol. 14 (1): 76–88. doi:10.1016/j.sbi.2004.01.013. பப்மெட்:15102453.
Sharma, V., Kaila, V. R. I., and Annila, A. (2009). "Protein folding as an evolutionary process". Physica A 388 (6): 851–862. doi:10.1016/j.physa.2008.12.004.
Bu, Z; Cook, J; Callaway, D. J. E. (2001). "Dynamic regimes and correlated structural dynamics in native and denatured alpha-lactalbuminC". J Mol Biol 312 (4): 865–873. doi:10.1006/jmbi.2001.5006. பப்மெட்:11575938.
Kmiecik, S., and Kolinski, A. (2007). "Characterization of protein-folding pathways by reduced-space modeling". Proc. Natl. Acad. Sci. U.S.A. 104 (30): 12330–5. doi:10.1073/pnas.0702265104. பப்மெட்:17636132.

fasebj.org (Global: low place; Tamil: 6,587^th place)

Pace, C., Shirley, B., McNutt, M., Gajiwala, K. (1 January 1996). "Forces contributing to the conformational stability of proteins". FASEB J. 10 (1): 75–83. பப்மெட்:8566551. http://www.fasebj.org/cgi/reprint/10/1/75.
Shortle, D. (1 January 1996). "The denatured state (the other half of the folding equation) and its role in protein stability". FASEB J. 10 (1): 27–34. பப்மெட்:8566543. http://www.fasebj.org/cgi/reprint/10/1/27.

jbmb.or.kr (Global: low place; Tamil: low place)

Lee, S., Tsai, F. (2005). "Molecular chaperones in protein quality control". J. Biochem. Mol. Biol. 38 (3): 259–65. பப்மெட்:15943899. http://www.jbmb.or.kr/fulltext/jbmb/view.php?vol=38&page=259. பார்த்த நாள்: 2010-07-21.

nature.com (Global: 234^th place; Tamil: 115^th place)

Dennis J. Selkoe (2003). "Folding proteins in fatal ways". Nature 426: pp. 900–904. doi:10.1038/nature02264. பப்மெட்:14685251. http://www.nature.com/nature/journal/v426/n6968/full/nature02264.html.

nih.gov (Global: 4^th place; Tamil: 5^th place)

ncbi.nlm.nih.gov

Anfinsen, C. (1972). "The formation and stabilization of protein structure". Biochem. J. 128 (4): 737–49. பப்மெட்:4565129. https://archive.org/details/sim_biochemical-journal_1972-07_128_4/page/737.
Dennis J. Selkoe (2003). "Folding proteins in fatal ways". Nature 426: pp. 900–904. doi:10.1038/nature02264. பப்மெட்:14685251. http://www.nature.com/nature/journal/v426/n6968/full/nature02264.html.
van den Berg, B., Wain, R., Dobson, C. M., Ellis R. J. (August 2000). "Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell". EMBO J. 19 (15): 3870–5. doi:10.1093/emboj/19.15.3870. பப்மெட்:10921869.
Pace, C., Shirley, B., McNutt, M., Gajiwala, K. (1 January 1996). "Forces contributing to the conformational stability of proteins". FASEB J. 10 (1): 75–83. பப்மெட்:8566551. http://www.fasebj.org/cgi/reprint/10/1/75.
Rose, G., Fleming, P., Banavar, J., Maritan, A. (2006). "A backbone-based theory of protein folding". Proc. Natl. Acad. Sci. U.S.A. 103 (45): 16623–33. doi:10.1073/pnas.0606843103. பப்மெட்:17075053.
Deechongkit, S., Nguyen, H., Dawson, P. E., Gruebele, M., Kelly, J. W. (2004). "Context Dependent Contributions of Backbone H-Bonding to β-Sheet Folding Energetics". Nature 403 (45): 101–5. doi:10.1073/pnas.0606843103. பப்மெட்:17075053.
Lee, S., Tsai, F. (2005). "Molecular chaperones in protein quality control". J. Biochem. Mol. Biol. 38 (3): 259–65. பப்மெட்:15943899. http://www.jbmb.or.kr/fulltext/jbmb/view.php?vol=38&page=259. பார்த்த நாள்: 2010-07-21.
Alexander, P. A., He Y., Chen, Y., Orban, J., Bryan, P. N. (2007). "The design and characterization of two proteins with 88% sequence identity but different structure and function". Proc Natl Acad Sci U S A. 104 (29): 11963–8. doi:10.1073/pnas.0700922104. பப்மெட்:17609385.
Shortle, D. (1 January 1996). "The denatured state (the other half of the folding equation) and its role in protein stability". FASEB J. 10 (1): 27–34. பப்மெட்:8566543. http://www.fasebj.org/cgi/reprint/10/1/27.
Kim, P. S., Baldwin, R. L. (1990). "Intermediates in the folding reactions of small proteins". Annu. Rev. Biochem. 59: 631–60. doi:10.1146/annurev.bi.59.070190.003215. பப்மெட்:2197986. https://archive.org/details/sim_annual-review-of-biochemistry_1990_59/page/631.
Jackson S. E. (August 1998). "How do small single-domain proteins fold?" (^{[தொடர்பிழந்த இணைப்பு]}). Fold Des 3 (4): R81–91. doi:10.1016/S1359-0278(98)00033-9. பப்மெட்:9710577. http://biomednet.com/elecref/13590278003R0081.
Kubelka, J., Hofrichter, J., Eaton, W. A. (February 2004). "The protein folding 'speed limit'". Curr. Opin. Struct. Biol. 14 (1): 76–88. doi:10.1016/j.sbi.2004.01.013. பப்மெட்:15102453.
Bu, Z; Cook, J; Callaway, D. J. E. (2001). "Dynamic regimes and correlated structural dynamics in native and denatured alpha-lactalbuminC". J Mol Biol 312 (4): 865–873. doi:10.1006/jmbi.2001.5006. பப்மெட்:11575938.
Kmiecik, S., and Kolinski, A. (2007). "Characterization of protein-folding pathways by reduced-space modeling". Proc. Natl. Acad. Sci. U.S.A. 104 (30): 12330–5. doi:10.1073/pnas.0702265104. பப்மெட்:17636132.

pubmedcentral.nih.gov

van den Berg, B., Wain, R., Dobson, C. M., Ellis R. J. (August 2000). "Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell". EMBO J. 19 (15): 3870–5. doi:10.1093/emboj/19.15.3870. பப்மெட்:10921869.
Alexander, P. A., He Y., Chen, Y., Orban, J., Bryan, P. N. (2007). "The design and characterization of two proteins with 88% sequence identity but different structure and function". Proc Natl Acad Sci U S A. 104 (29): 11963–8. doi:10.1073/pnas.0700922104. பப்மெட்:17609385.

pnas.org (Global: 1,293^rd place; Tamil: 347^th place)

Mirny, L. A., Abkevich, V. I. & Shakhnovich, E. I. (28 Apr 1998). "How evolution makes proteins fold quickly.". Proc Natl Acad Sci U S A. 95 (9): 4976-4981. http://www.pnas.org/content/95/9/4976.abstract. ^{[தொடர்பிழந்த இணைப்பு]}
S Rackovsky. (15 Jan 1993). "On the nature of the protein folding code.". Proc Natl Acad Sci U S A. 90 (2): 644-648. http://www.pnas.org/content/90/2/644.abstract. ^{[தொடர்பிழந்த இணைப்பு]}

sciencemag.org (Global: 857^th place; Tamil: 228^th place)

Anfinsen CB. (20 July 1973). "Principles that Govern the Folding of Protein Chains". Science. 181 (4096): 223-230. doi:10.1126/science.181.4096.223. http://www.sciencemag.org/cgi/pdf_extract/181/4096/223. பார்த்த நாள்: 21 ஜூலை 2010.

toolserver.org (Global: low place; Tamil: 352^nd place)

எஆசு:10.1146/annurev.biochem.75.101304.123901
This citation will be automatically completed in the next few minutes. You can jump the queue or expand by hand

ucl.ac.uk (Global: 1,306^th place; Tamil: 805^th place)

cs.ucl.ac.uk

"Fragment-based Protein Folding Simulations".

wikipedia.org (Global: low place; Tamil: low place)

en.wikipedia.org

Mirny, L. A., Abkevich, V. I. & Shakhnovich, E. I. (28 Apr 1998). "How evolution makes proteins fold quickly.". Proc Natl Acad Sci U S A. 95 (9): 4976-4981. http://www.pnas.org/content/95/9/4976.abstract. ^{[தொடர்பிழந்த இணைப்பு]}
S Rackovsky. (15 Jan 1993). "On the nature of the protein folding code.". Proc Natl Acad Sci U S A. 90 (2): 644-648. http://www.pnas.org/content/90/2/644.abstract. ^{[தொடர்பிழந்த இணைப்பு]}
Jackson S. E. (August 1998). "How do small single-domain proteins fold?" (^{[தொடர்பிழந்த இணைப்பு]}). Fold Des 3 (4): R81–91. doi:10.1016/S1359-0278(98)00033-9. பப்மெட்:9710577. http://biomednet.com/elecref/13590278003R0081.

ta.wikipedia.org

எஆசு:10.1146/annurev.biochem.75.101304.123901
This citation will be automatically completed in the next few minutes. You can jump the queue or expand by hand

wiley.com (Global: 222^nd place; Tamil: 219^th place)

www3.interscience.wiley.com

Govindarajan S, Recabarren R, Goldstein RA. (17 Sep 1999). "Estimating the total number of protein folds.". Proteins. 35 (4): 408-414. http://www3.interscience.wiley.com/journal/65000323/abstract. பார்த்த நாள்: 21 ஜூலை 2010.

wisc.edu (Global: 1,045^th place; Tamil: 408^th place)

biochem.wisc.edu

C. Levinthal (1968). "Are there pathways for protein folding?". J. Chim. Phys. 65: 44–5. http://www.biochem.wisc.edu/courses/biochem704/Reading/Levinthal1968.pdf. பார்த்த நாள்: 2010-07-21.

புரதம் மடிப்படைதல் (Tamil Wikipedia)

archive.org (Global: 6th place; Tamil: 8th place)

biomednet.com (Global: low place; Tamil: low place)

biomolecular-modeling.com (Global: low place; Tamil: low place)

doi.org (Global: 2nd place; Tamil: 4th place)

dx.doi.org

fasebj.org (Global: low place; Tamil: 6,587th place)

jbmb.or.kr (Global: low place; Tamil: low place)

nature.com (Global: 234th place; Tamil: 115th place)

nih.gov (Global: 4th place; Tamil: 5th place)

ncbi.nlm.nih.gov

pubmedcentral.nih.gov

pnas.org (Global: 1,293rd place; Tamil: 347th place)

sciencemag.org (Global: 857th place; Tamil: 228th place)

toolserver.org (Global: low place; Tamil: 352nd place)

ucl.ac.uk (Global: 1,306th place; Tamil: 805th place)

cs.ucl.ac.uk

wikipedia.org (Global: low place; Tamil: low place)

en.wikipedia.org

ta.wikipedia.org

wiley.com (Global: 222nd place; Tamil: 219th place)

www3.interscience.wiley.com

wisc.edu (Global: 1,045th place; Tamil: 408th place)

biochem.wisc.edu

archive.org (Global: 6^th place; Tamil: 8^th place)

doi.org (Global: 2^nd place; Tamil: 4^th place)

fasebj.org (Global: low place; Tamil: 6,587^th place)

nature.com (Global: 234^th place; Tamil: 115^th place)

nih.gov (Global: 4^th place; Tamil: 5^th place)

pnas.org (Global: 1,293^rd place; Tamil: 347^th place)

sciencemag.org (Global: 857^th place; Tamil: 228^th place)

toolserver.org (Global: low place; Tamil: 352^nd place)

ucl.ac.uk (Global: 1,306^th place; Tamil: 805^th place)

wiley.com (Global: 222^nd place; Tamil: 219^th place)

wisc.edu (Global: 1,045^th place; Tamil: 408^th place)