 Protein Conformation
"Protein Conformation" 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 characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
| Descriptor ID |
D011487
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| MeSH Number(s) |
G02.111.570.790.709
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| Concept/Terms |
Protein Conformation- Protein Conformation
- Conformation, Protein
- Conformations, Protein
- Protein Conformations
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Below are MeSH descriptors whose meaning is more general than "Protein Conformation".
Below are MeSH descriptors whose meaning is more specific than "Protein Conformation".
This graph shows the total number of publications written about "Protein Conformation" by people in this website by year, and whether "Protein Conformation" 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 |
|---|
| 1984 | 0 | 1 | 1 | | 1988 | 0 | 1 | 1 | | 1990 | 0 | 4 | 4 | | 1992 | 0 | 1 | 1 | | 1993 | 1 | 1 | 2 | | 1995 | 0 | 1 | 1 | | 1996 | 0 | 1 | 1 | | 1997 | 0 | 2 | 2 | | 1998 | 0 | 2 | 2 | | 1999 | 0 | 5 | 5 | | 2000 | 0 | 2 | 2 | | 2001 | 0 | 1 | 1 | | 2002 | 0 | 1 | 1 | | 2003 | 0 | 3 | 3 | | 2004 | 0 | 4 | 4 | | 2005 | 0 | 5 | 5 | | 2006 | 0 | 3 | 3 | | 2007 | 2 | 2 | 4 | | 2008 | 0 | 5 | 5 | | 2009 | 0 | 3 | 3 | | 2010 | 0 | 5 | 5 | | 2011 | 1 | 5 | 6 | | 2012 | 1 | 2 | 3 | | 2013 | 0 | 3 | 3 | | 2014 | 0 | 2 | 2 | | 2015 | 0 | 3 | 3 | | 2016 | 0 | 2 | 2 | | 2019 | 0 | 2 | 2 |
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Below are the most recent publications written about "Protein Conformation" by people in Profiles.
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Banh R, Cherny VV, Morgan D, Musset B, Thomas S, Kulleperuma K, Smith SME, Pomès R, DeCoursey TE. Hydrophobic gasket mutation produces gating pore currents in closed human voltage-gated proton channels. Proc Natl Acad Sci U S A. 2019 09 17; 116(38):18951-18961.
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Skowron KJ, Booker K, Cheng C, Creed S, David BP, Lazzara PR, Lian A, Siddiqui Z, Speltz TE, Moore TW. Steroid receptor/coactivator binding inhibitors: An update. Mol Cell Endocrinol. 2019 08 01; 493:110471.
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Sherman MA, LaCroix M, Amar F, Larson ME, Forster C, Aguzzi A, Bennett DA, Ramsden M, Lesné SE. Soluble Conformers of Aß and Tau Alter Selective Proteins Governing Axonal Transport. J Neurosci. 2016 09 14; 36(37):9647-58.
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DeCoursey TE, Morgan D, Musset B, Cherny VV. Insights into the structure and function of HV1 from a meta-analysis of mutation studies. J Gen Physiol. 2016 08; 148(2):97-118.
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DeCoursey TE. The Voltage-Gated Proton Channel: A Riddle, Wrapped in a Mystery, inside an Enigma. Biochemistry. 2015 Jun 02; 54(21):3250-68.
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Parker DL, Walsh S, Li B, Kim E, Sharipour A, Smith C, Chen YH, Berger R, Harper B, Zhang T, Park M, Shu M, Wu J, Xu J, Dewnani S, Sherer EC, Hruza A, Reichert P, Geissler W, Sonatore L, Ellsworth K, Balkovec J, Greenlee W, Wood HB. Rapid development of two factor IXa inhibitors from hit to lead. Bioorg Med Chem Lett. 2015 Jun 01; 25(11):2321-5.
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Cao Y, Gomes SA, Rangel EB, Paulino EC, Fonseca TL, Li J, Teixeira MB, Gouveia CH, Bianco AC, Kapiloff MS, Balkan W, Hare JM. S-nitrosoglutathione reductase-dependent PPAR? denitrosylation participates in MSC-derived adipogenesis and osteogenesis. J Clin Invest. 2015 Apr; 125(4):1679-91.
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Liu JL, Eisenberg B. Analytical models of calcium binding in a calcium channel. J Chem Phys. 2014 Aug 21; 141(7):075102.
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Adair BD, Altintas MM, Möller CC, Arnaout MA, Reiser J. Structure of the kidney slit diaphragm adapter protein CD2-associated protein as determined with electron microscopy. J Am Soc Nephrol. 2014 Jul; 25(7):1465-73.
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Nguyen JB, Pool CD, Wong CY, Treger RS, Williams DL, Cappello M, Lea WA, Simeonov A, Vermeire JJ, Modis Y. Peroxiredoxin-1 from the human hookworm Ancylostoma ceylanicum forms a stable oxidized decamer and is covalently inhibited by conoidin A. Chem Biol. 2013 Aug 22; 20(8):991-1001.
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