 Protein Structure, Secondary
"Protein Structure, Secondary" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
| Descriptor ID |
D017433
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| MeSH Number(s) |
G02.111.570.790.709.600
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| Concept/Terms |
Protein Structure, Secondary- Protein Structure, Secondary
- Secondary Protein Structure
- Protein Structures, Secondary
- Secondary Protein Structures
- Structure, Secondary Protein
- Structures, Secondary Protein
beta-Sheet Conformation, Protein- beta-Sheet Conformation, Protein
- Conformation, Protein beta-Sheet
- Conformations, Protein beta-Sheet
- Protein beta-Sheet Conformation
- Protein beta-Sheet Conformations
- beta Sheet Conformation, Protein
- beta-Sheet Conformations, Protein
- Protein Conformation, beta-Sheet
- Conformation, beta-Sheet Protein
- Conformations, beta-Sheet Protein
- Protein Conformation, beta Sheet
- Protein Conformations, beta-Sheet
- beta-Sheet Protein Conformation
- beta-Sheet Protein Conformations
Protein Conformation, beta-Strand- Protein Conformation, beta-Strand
- Conformation, beta-Strand Protein
- Conformations, beta-Strand Protein
- Protein Conformation, beta Strand
- Protein Conformations, beta-Strand
- beta-Strand Protein Conformation
- beta-Strand Protein Conformations
- beta-Strand Conformation, Protein
- Conformation, Protein beta-Strand
- Conformations, Protein beta-Strand
- Protein beta-Strand Conformation
- Protein beta-Strand Conformations
- beta Strand Conformation, Protein
- beta-Strand Conformations, Protein
alpha-Helical Conformation, Protein- alpha-Helical Conformation, Protein
- Conformation, Protein alpha-Helical
- Conformations, Protein alpha-Helical
- Protein alpha-Helical Conformation
- Protein alpha-Helical Conformations
- alpha Helical Conformation, Protein
- alpha-Helical Conformations, Protein
- Protein Conformation, alpha-Helical
- Conformation, alpha-Helical Protein
- Conformations, alpha-Helical Protein
- Protein Conformation, alpha Helical
- Protein Conformations, alpha-Helical
- alpha-Helical Protein Conformation
- alpha-Helical Protein Conformations
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Below are MeSH descriptors whose meaning is more general than "Protein Structure, Secondary".
Below are MeSH descriptors whose meaning is more specific than "Protein Structure, Secondary".
This graph shows the total number of publications written about "Protein Structure, Secondary" by people in this website by year, and whether "Protein Structure, Secondary" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1993 | 0 | 1 | 1 | | 1994 | 0 | 2 | 2 | | 1997 | 1 | 0 | 1 | | 1999 | 0 | 2 | 2 | | 2002 | 0 | 1 | 1 | | 2003 | 0 | 2 | 2 | | 2004 | 0 | 2 | 2 | | 2005 | 0 | 1 | 1 | | 2006 | 0 | 2 | 2 | | 2007 | 0 | 2 | 2 | | 2008 | 1 | 0 | 1 | | 2011 | 0 | 3 | 3 | | 2015 | 0 | 1 | 1 | | 2019 | 0 | 1 | 1 |
To return to the timeline, click here.
Below are the most recent publications written about "Protein Structure, Secondary" by people in Profiles.
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Chandra S, Roy A, Patel DR, Pahan K. PPARa Between Aspirin and Plaque Clearance. J Alzheimers Dis. 2019; 71(2):389-397.
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Lewis KM, Ronish LA, R?os E, Kang C. Characterization of Two Human Skeletal Calsequestrin Mutants Implicated in Malignant Hyperthermia and Vacuolar Aggregate Myopathy. J Biol Chem. 2015 Nov 27; 290(48):28665-74.
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Saccoccia F, Angelucci F, Boumis G, Brunori M, Miele AE, Williams DL, Bellelli A. On the mechanism and rate of gold incorporation into thiol-dependent flavoreductases. J Inorg Biochem. 2012 Mar; 108:105-11.
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Leung MY, Cohen FS. Increasing hydrophobicity of residues in an anti-HIV-1 Env peptide synergistically improves potency. Biophys J. 2011 Apr 20; 100(8):1960-8.
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Mollapour M, Tsutsumi S, Truman AW, Xu W, Vaughan CK, Beebe K, Konstantinova A, Vourganti S, Panaretou B, Piper PW, Trepel JB, Prodromou C, Pearl LH, Neckers L. Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity. Mol Cell. 2011 Mar 18; 41(6):672-81.
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Yang JY, Yang MQ, Dunker AK, Deng Y, Huang X. Investigation of transmembrane proteins using a computational approach. BMC Genomics. 2008; 9 Suppl 1:S7.
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Shieh HS, Mathis KJ, Williams JM, Hills RL, Wiese JF, Benson TE, Kiefer JR, Marino MH, Carroll JN, Leone JW, Malfait AM, Arner EC, Tortorella MD, Tomasselli A. High resolution crystal structure of the catalytic domain of ADAMTS-5 (aggrecanase-2). J Biol Chem. 2008 Jan 18; 283(3):1501-1507.
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Sagar GD, Gereben B, Callebaut I, Mornon JP, Ze?ld A, da Silva WS, Luongo C, Dentice M, Tente SM, Freitas BC, Harney JW, Zavacki AM, Bianco AC. Ubiquitination-induced conformational change within the deiodinase dimer is a switch regulating enzyme activity. Mol Cell Biol. 2007 Jul; 27(13):4774-83.
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Gupta V, Gylling A, Alonso JL, Sugimori T, Ianakiev P, Xiong JP, Arnaout MA. The beta-tail domain (betaTD) regulates physiologic ligand binding to integrin CD11b/CD18. Blood. 2007 Apr 15; 109(8):3513-20.
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Miedema H, Vrouenraets M, Wierenga J, Eisenberg B, Schirmer T, Basl? A, Meijberg W. Conductance and selectivity fluctuations in D127 mutants of the bacterial porin OmpF. Eur Biophys J. 2006 Dec; 36(1):13-22.
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