Protein Conformation, alpha-Helical
"Protein Conformation, alpha-Helical" 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.
A secondary structure of proteins that is a right-handed helix or coil, where each amino (N-H) group of the peptide backbone contributes a hydrogen bond to the carbonyl(C=O) group of the amino acid four residues N-terminal to it (n-4). It is the most common type of secondary structure.
| Descriptor ID |
D000072756
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| MeSH Number(s) |
G02.111.570.820.709.600.020
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| Concept/Terms |
Protein Conformation, alpha-Helical- Protein Conformation, alpha-Helical
- Protein Conformation, alpha Helical
- alpha-Helices
- alpha Helices
- alpha-Helical Conformation, Protein
- Conformation, Protein alpha-Helical
- Conformations, Protein alpha-Helical
- alpha Helical Conformation, Protein
- alpha-Helical Conformations, Protein
- alpha-Helical Protein Conformation
- Conformation, alpha-Helical Protein
- Conformations, alpha-Helical Protein
- Protein Conformations, alpha-Helical
- alpha Helical Protein Conformation
- alpha-Helical Protein Conformations
- alpha-Helix
- alpha Helix
- alpha-Helical Structures
- alpha Helical Structures
- alpha-Helical Structure
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Below are MeSH descriptors whose meaning is more general than "Protein Conformation, alpha-Helical".
Below are MeSH descriptors whose meaning is more specific than "Protein Conformation, alpha-Helical".
This graph shows the total number of publications written about "Protein Conformation, alpha-Helical" by people in this website by year, and whether "Protein Conformation, alpha-Helical" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2016 | 0 | 3 | 3 |
| 2018 | 0 | 2 | 2 |
| 2019 | 0 | 4 | 4 |
| 2020 | 0 | 1 | 1 |
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Below are the most recent publications written about "Protein Conformation, alpha-Helical" by people in Profiles.
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Komolov KE, Sulon SM, Bhardwaj A, van Keulen SC, Duc NM, Laurinavichyute DK, Lou HJ, Turk BE, Chung KY, Dror RO, Benovic JL. Structure of a GRK5-Calmodulin Complex Reveals Molecular Mechanism of GRK Activation and Substrate Targeting. Mol Cell. 2021 01 21; 81(2):323-339.e11.
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Supsrisunjai C, Hsu CK, Michael M, Duval C, Lee JYW, Yang HS, Huang HY, Chaikul T, Onoufriadis A, Steiner RA, Ari?ns RAS, Sarig O, Sprecher E, Eskin-Schwartz M, Samlaska C, Simpson MA, Calonje E, Parsons M, McGrath JA. Coagulation Factor XIII-A Subunit Missense Mutation in the Pathobiology of Autosomal Dominant Multiple Dermatofibromas. J Invest Dermatol. 2020 03; 140(3):624-635.e7.
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Cingolani G, McCauley M, Lobley A, Bryer AJ, Wesolowski J, Greco DL, Lokareddy RK, Ronzone E, Perilla JR, Paumet F. Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA. Nat Commun. 2019 06 21; 10(1):2747.
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Mercier R, Wolmarans A, Schubert J, Neuweiler H, Johnson JL, LaPointe P. The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation. Nat Commun. 2019 03 20; 10(1):1273.
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Cheng H, Schwell V, Curtis BR, Fazlieva R, Roder H, Campbell KS. Conformational Changes in the Cytoplasmic Region of KIR3DL1 upon Interaction with SHP-2. Structure. 2019 04 02; 27(4):639-650.e2.
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Quinn CM, Wang M, Fritz MP, Runge B, Ahn J, Xu C, Perilla JR, Gronenborn AM, Polenova T. Dynamic regulation of HIV-1 capsid interaction with the restriction factor TRIM5a identified by magic-angle spinning NMR and molecular dynamics simulations. Proc Natl Acad Sci U S A. 2018 11 06; 115(45):11519-11524.
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Sallam S, Dolog I, Paik BA, Jia X, Kiick KL, Wesdemiotis C. Sequence and Conformational Analysis of Peptide-Polymer Bioconjugates by Multidimensional Mass Spectrometry. Biomacromolecules. 2018 05 14; 19(5):1498-1507.
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Jeronimo C, Langelier MF, Bataille AR, Pascal JM, Pugh BF, Robert F. Tail and Kinase Modules Differently Regulate Core Mediator Recruitment and Function In?Vivo. Mol Cell. 2016 11 03; 64(3):455-466.
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Riccio AA, McCauley M, Langelier MF, Pascal JM. Tankyrase Sterile a Motif Domain Polymerization Is Required for Its Role in Wnt Signaling. Structure. 2016 09 06; 24(9):1573-81.
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Calero-Rubio C, Paik B, Jia X, Kiick KL, Roberts CJ. Predicting unfolding thermodynamics and stable intermediates for alanine-rich helical peptides with the aid of coarse-grained molecular simulation. Biophys Chem. 2016 10; 217:8-19.