 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) |
G02.111.570.820.709.600
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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
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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 |
|---|
| 1992 | 2 | 0 | 2 | | 1993 | 4 | 6 | 10 | | 1994 | 5 | 6 | 11 | | 1995 | 5 | 7 | 12 | | 1996 | 14 | 6 | 20 | | 1997 | 8 | 10 | 18 | | 1998 | 6 | 11 | 17 | | 1999 | 1 | 19 | 20 | | 2000 | 1 | 14 | 15 | | 2001 | 0 | 22 | 22 | | 2002 | 4 | 19 | 23 | | 2003 | 2 | 18 | 20 | | 2004 | 3 | 19 | 22 | | 2005 | 1 | 27 | 28 | | 2006 | 2 | 24 | 26 | | 2007 | 0 | 23 | 23 | | 2008 | 0 | 17 | 17 | | 2009 | 2 | 11 | 13 | | 2010 | 3 | 14 | 17 | | 2011 | 1 | 21 | 22 | | 2012 | 0 | 10 | 10 | | 2013 | 2 | 18 | 20 | | 2014 | 1 | 16 | 17 | | 2015 | 2 | 16 | 18 | | 2016 | 0 | 10 | 10 | | 2017 | 1 | 5 | 6 | | 2018 | 0 | 13 | 13 | | 2019 | 1 | 8 | 9 |
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Below are the most recent publications written about "Protein Structure, Secondary" by people in Profiles.
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Prates ET, Crowley MF, Skaf MS, Beckham GT. Catalytic Mechanism of Aryl-Ether Bond Cleavage in Lignin by LigF and LigG. J Phys Chem B. 2019 12 05; 123(48):10142-10151.
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Bandi S, Singh SM, Shah DD, Upadhyay V, Mallela KMG. 2D NMR Analysis of the Effect of Asparagine Deamidation Versus Methionine Oxidation on the Structure, Stability, Aggregation, and Function of a Therapeutic Protein. Mol Pharm. 2019 11 04; 16(11):4621-4635.
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Narula A, Ellis J, Taliaferro JM, Rissland OS. Coding regions affect mRNA stability in human cells. RNA. 2019 12; 25(12):1751-1764.
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Fanni AM, Vander Zanden CM, Majewska PV, Majewski J, Chi EY. Membrane-mediated fibrillation and toxicity of the tau hexapeptide PHF6. J Biol Chem. 2019 10 18; 294(42):15304-15317.
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Pegram LM, Liddle JC, Xiao Y, Hoh M, Rudolph J, Iverson DB, Vigers GP, Smith D, Zhang H, Wang W, Moffat JG, Ahn NG. Activation loop dynamics are controlled by conformation-selective inhibitors of ERK2. Proc Natl Acad Sci U S A. 2019 07 30; 116(31):15463-15468.
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Zhang X, Peng Y, Grace PM, Metcalf MD, Kwilasz AJ, Wang Y, Zhang T, Wu S, Selfridge BR, Portoghese PS, Rice KC, Watkins LR, Hutchinson MR, Wang X. Stereochemistry and innate immune recognition: (+)-norbinaltorphimine targets myeloid differentiation protein 2 and inhibits toll-like receptor 4 signaling. FASEB J. 2019 08; 33(8):9577-9587.
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Shea D, Hsu CC, Bi TM, Paranjapye N, Childers MC, Cochran J, Tomberlin CP, Wang L, Paris D, Zonderman J, Varani G, Link CD, Mullan M, Daggett V. a-Sheet secondary structure in amyloid ß-peptide drives aggregation and toxicity in Alzheimer's disease. Proc Natl Acad Sci U S A. 2019 04 30; 116(18):8895-8900.
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Mant CT, Jiang Z, Gera L, Davis T, Nelson KL, Bevers S, Hodges RS. De Novo Designed Amphipathic a-Helical Antimicrobial Peptides Incorporating Dab and Dap Residues on the Polar Face To Treat the Gram-Negative Pathogen, Acinetobacter baumannii. J Med Chem. 2019 04 11; 62(7):3354-3366.
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Basak S, Nobrega RP, Tavella D, Deveau LM, Koga N, Tatsumi-Koga R, Baker D, Massi F, Matthews CR. Networks of electrostatic and hydrophobic interactions modulate the complex folding free energy surface of a designed ßa protein. Proc Natl Acad Sci U S A. 2019 04 02; 116(14):6806-6811.
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Henen MA, Mahlawat P, Zwieb C, Kodali RB, Hinck CS, Hanna RD, Krzysiak TC, Ilangovan U, Cano KE, Hinck G, Vonberg M, McCabe M, Hinck AP. TGF-ß2 uses the concave surface of its extended finger region to bind betaglycan's ZP domain via three residues specific to TGF-ß and inhibin-a. J Biol Chem. 2019 03 01; 294(9):3065-3080.
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