 Microscopy, Atomic Force
"Microscopy, Atomic Force" 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 type of scanning probe microscopy in which a probe systematically rides across the surface of a sample being scanned in a raster pattern. The vertical position is recorded as a spring attached to the probe rises and falls in response to peaks and valleys on the surface. These deflections produce a topographic map of the sample.
| Descriptor ID |
D018625
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| MeSH Number(s) |
E01.370.350.515.666.400 E05.595.666.400
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| Concept/Terms |
Microscopy, Atomic Force- Microscopy, Atomic Force
- Force Microscopy
- Force Microscopies
- Microscopies, Force
- Microscopy, Force
- Scanning Force Microscopy
- Force Microscopies, Scanning
- Force Microscopy, Scanning
- Microscopies, Scanning Force
- Microscopy, Scanning Force
- Scanning Force Microscopies
- Atomic Force Microscopy
- Atomic Force Microscopies
- Microscopies, Atomic Force
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Below are MeSH descriptors whose meaning is more general than "Microscopy, Atomic Force".
Below are MeSH descriptors whose meaning is more specific than "Microscopy, Atomic Force".
This graph shows the total number of publications written about "Microscopy, Atomic Force" by people in this website by year, and whether "Microscopy, Atomic Force" 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 |
|---|
| 2002 | 0 | 1 | 1 | | 2007 | 0 | 1 | 1 | | 2009 | 0 | 1 | 1 | | 2014 | 1 | 3 | 4 | | 2016 | 0 | 1 | 1 | | 2017 | 0 | 1 | 1 | | 2018 | 0 | 1 | 1 | | 2019 | 0 | 1 | 1 | | 2020 | 1 | 0 | 1 |
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Below are the most recent publications written about "Microscopy, Atomic Force" by people in Profiles.
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Nelsen E, Hobson CM, Kern ME, Hsiao JP, O'Brien Iii ET, Watanabe T, Condon BM, Boyce M, Grinstein S, Hahn KM, Falvo MR, Superfine R. Combined Atomic Force Microscope and Volumetric Light Sheet System for Correlative Force and Fluorescence Mechanobiology Studies. Sci Rep. 2020 05 18; 10(1):8133.
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Drost CC, Rovas A, Kusche-Vihrog K, Van Slyke P, Kim H, Hoang VC, Maynes JT, Wennmann DO, Pavenstädt H, Linke W, Lukasz A, Hesse B, Kümpers P. Tie2 Activation Promotes Protection and Reconstitution of the Endothelial Glycocalyx in Human Sepsis. Thromb Haemost. 2019 Nov; 119(11):1827-1838.
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Maghsudi M, Shahabadi N, Kooshk MRA, Ghaemi N, Nemati L, Parvaneh S, Adeli K, Varmira K. Nontoxic silver nanocluster-induced folding, fibrillation, and aggregation of blood plasma proteins. Int J Biol Macromol. 2018 Nov; 119:838-848.
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Wen J, Tao H, Lau K, Liu H, Simmons CA, Sun Y, Hopyan S. Cell and Tissue Scale Forces Coregulate Fgfr2-Dependent Tetrads and Rosettes in the Mouse Embryo. Biophys J. 2017 May 23; 112(10):2209-2218.
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Li S, Donner E, Xiao H, Thompson M, Zhang Y, Rempel C, Liu Q. Preparation and characterization of soy protein films with a durable water resistance-adjustable and antimicrobial surface. Mater Sci Eng C Mater Biol Appl. 2016 Dec 01; 69:947-55.
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Muiznieks LD, Cirulis JT, van der Horst A, Reinhardt DP, Wuite GJ, Pomès R, Keeley FW. Modulated growth, stability and interactions of liquid-like coacervate assemblies of elastin. Matrix Biol. 2014 Jun; 36:39-50.
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Liu H, Wen J, Xiao Y, Liu J, Hopyan S, Radisic M, Simmons CA, Sun Y. In situ mechanical characterization of the cell nucleus by atomic force microscopy. ACS Nano. 2014 Apr 22; 8(4):3821-8.
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Walsh P, Vanderlee G, Yau J, Campeau J, Sim VL, Yip CM, Sharpe S. The mechanism of membrane disruption by cytotoxic amyloid oligomers formed by prion protein(106-126) is dependent on bilayer composition. J Biol Chem. 2014 Apr 11; 289(15):10419-30.
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Lee DW, Banquy X, Kristiansen K, Kaufman Y, Boggs JM, Israelachvili JN. Lipid domains control myelin basic protein adsorption and membrane interactions between model myelin lipid bilayers. Proc Natl Acad Sci U S A. 2014 Feb 25; 111(8):E768-75.
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Walsh P, Yau J, Simonetti K, Sharpe S. Morphology and secondary structure of stable beta-oligomers formed by amyloid peptide PrP(106-126). Biochemistry. 2009 Jun 30; 48(25):5779-81.
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