elastin - Books

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See LIMK1 (ELASTIN) LIM domain kinase 1 in the Gene database

elastin in Calypte anna Fundulus heteroclitus Sus scrofa All 6 Gene records

Results: 1 to 20 of 92 books (507 items)

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Select item 44036681.

StatPearls [Internet].

Treasure Island (FL): StatPearls Publishing; 2024 Jan-.

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Select item 14589842.

GeneReviews® [Internet].

Adam MP, Feldman J, Mirzaa GM, et al., editors.

Seattle (WA): University of Washington, Seattle; 1993-2024.

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Select item 46666223.

Mechanisms of Vascular Disease: A Reference Book for Vascular Specialists [Internet].

Fitridge R, Thompson M, editors.

Adelaide (AU): University of Adelaide Press; 2011.

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Select item 14152804.

Madame Curie Bioscience Database [Internet].

Austin (TX): Landes Bioscience; 2000-2013.

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Select item 31715805.

Air Pollution, the Automobile, and Public Health.

Watson AY, Bates RR, Kennedy D, editors.

Washington (DC): National Academies Press (US); 1988.

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Select item 53892306.

Textbook on Scar Management: State of the Art Management and Emerging Technologies [Internet].

Téot L, Mustoe TA, Middelkoop E, et al., editors.

Cham (CH): Springer; 2020.

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Select item 30698047.

The Health Consequences of Smoking—50 Years of Progress: A Report of the Surgeon General.

National Center for Chronic Disease Prevention and Health Promotion (US) Office on Smoking and Health.

Atlanta (GA): Centers for Disease Control and Prevention (US); 2014.

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Select item 18957888.

Molecular Biology of the Cell. 4th edition.

Alberts B, Johnson A, Lewis J, et al.

New York: Garland Science; 2002.

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Select item 45442909.

Etiology and Morphogenesis of Congenital Heart Disease: From Gene Function and Cellular Interaction to Morphology [Internet].

Nakanishi T, Markwald RR, Baldwin HS, et al., editors.

Tokyo: Springer; 2016.

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Select item 244094610.

How Tobacco Smoke Causes Disease: The Biology and Behavioral Basis for Smoking-Attributable Disease: A Report of the Surgeon General.

Centers for Disease Control and Prevention (US); National Center for Chronic Disease Prevention and Health Promotion (US); Office on Smoking and Health (US).

Atlanta (GA): Centers for Disease Control and Prevention (US); 2010.

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Select item 340129411.

Endotext [Internet].

Feingold KR, Anawalt B, Blackman MR, et al., editors.

South Dartmouth (MA): MDText.com, Inc.; 2000-.

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Select item 165096212.

Webvision: The Organization of the Retina and Visual System [Internet].

Kolb H, Fernandez E, Nelson R, editors.

Salt Lake City (UT): University of Utah Health Sciences Center; 1995-.

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Select item 493866813.

Skin Substitutes for Treating Chronic Wounds [Internet].

Snyder D, Sullivan N, Margolis D, et al.

Rockville (MD): Agency for Healthcare Research and Quality (US); 2020 Feb 2.

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Select item 166869014.

Holland-Frei Cancer Medicine. 6th edition.

Kufe DW, Pollock RE, Weichselbaum RR, et al., editors.

Hamilton (ON): BC Decker; 2003.

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Select item 493799415.

Diseases of the Chest, Breast, Heart and Vessels 2019-2022: Diagnostic and Interventional Imaging [Internet].

Hodler J, Kubik-Huch RA, von Schulthess GK, editors.

Cham (CH): Springer; 2019.

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Select item 296478816.

Pancreatic Cancer and Tumor Microenvironment.

Grippo PJ, Munshi HG, editors.

Trivandrum (India): Transworld Research Network; 2012.

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Select item 408782217.

Non-Ionizing Radiation, Part 2: Radiofrequency Electromagnetic Fields.

IARC Working Group on the Evaluation of Carcinogenic Risks to Humans.

Lyon (FR): International Agency for Research on Cancer; 2013. (IARC Monographs on the Evaluation of Carcinogenic Risks to Humans, No. 102.)

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Select item 327663818.

Nutrition During Pregnancy: Part I Weight Gain: Part II Nutrient Supplements.

Institute of Medicine (US) Committee on Nutritional Status During Pregnancy and Lactation.

Washington (DC): National Academies Press (US); 1990.

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Select item 327207219.

Indoor Pollutants.

National Research Council (US) Committee on Indoor Pollutants.

Washington (DC): National Academies Press (US); 1981.

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Select item 412940020.

Optically Induced Nanostructures: Biomedical and Technical Applications.

König K, Ostendorf A, editors.

Berlin: De Gruyter; 2015 Jun 23.

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Supplemental Content

Images search in Bookshelf

Figure 3-32Contrast between collagen and elastin

(A) Collagen is a triple helix formed by three extended protein chains that wrap around each other. Many rodlike collagen molecules are cross-linked together in the extracellular space to form inextensible collagen fibrils ( top) that have the tensile strength of steel. (B) Elastin polypeptide chains are cross-linked together to form elastic fibers. Each elastin molecule uncoils into a more extended conformation when the fiber is stretched. The striking contrast between the physical properties of elastin and collagen is due entirely to their very different amino acid sequences.

Protein Structure .

Alberts B, Bray D, Lewis J, et al. Molecular Biology of the Cell. 3rd edition. New York: Garland Science; 1994.
Figure 19-50Stretching a network of elastin molecules

The molecules are joined together by covalent bonds (indicated in red) to generate a cross-linked network. In the model shown each elastin molecule in the network can expand and contract as a random coil, so that the entire assembly can stretch and recoil like a rubber band.

The Extracellular Matrix of Animals .

Alberts B, Bray D, Lewis J, et al. Molecular Biology of the Cell. 3rd edition. New York: Garland Science; 1994.
Figure 19-52Stretching a network of elastin molecules

The molecules are joined together by covalent bonds (red) to generate a cross-linked network. In this model, each elastin molecule in the network can expand and contract as a random coil, so that the entire assembly can stretch and recoil like a rubber band.

The Extracellular Matrix of Animals.

Alberts B, Johnson A, Lewis J, et al. Molecular Biology of the Cell. 4th edition. New York: Garland Science; 2002.
Figure 3-28Collagen and elastin

(A) Collagen is a triple helix formed by three extended protein chains that wrap around one another (bottom). Many rodlike collagen molecules are cross-linked together in the extracellular space to form unextendable collagen fibrils (top) that have the tensile strength of steel. The striping on the collagen fibril is caused by the regular repeating arrangement of the collagen molecules within the fibril. (B) Elastin polypeptide chains are cross-linked together to form rubberlike, elastic fibers. Each elastin molecule uncoils into a more extended conformation when the fiber is stretched and recoils spontaneously as soon as the stretching force is relaxed.

The Shape and Structure of Proteins.

Alberts B, Johnson A, Lewis J, et al. Molecular Biology of the Cell. 4th edition. New York: Garland Science; 2002.