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NHS top managers, knowledge exchange and leadership: the early development of Academic Health Science Networks – a mixed-methods study.

Ferlie E, Nicolini D, Ledger J, et al.

Southampton (UK): NIHR Journals Library; 2017 May. (Health Services and Delivery Research, No. 5.17.)

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Select item 14152802.

Madame Curie Bioscience Database [Internet].

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

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StatPearls [Internet].

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

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Select item 14589844.

GeneReviews® [Internet].

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

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

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Endotext [Internet].

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

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

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Select item 18957886.

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 29807787.

Clustering for 21st Century Prosperity: Summary of a Symposium.

National Research Council (US) Committee on Competing in the 21st Century: Best Practice in State and Regional Innovation Initiatives.

Washington (DC): National Academies Press (US); 2012.

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Select item 28215248.

PDQ Cancer Information Summaries [Internet].

Bethesda (MD): National Cancer Institute (US); 2002-.

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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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Best Practices in State and Regional Innovation Initiatives: Competing in the 21st Century.

National Research Council (US) Committee on Competing in the 21st Century: Best Practice in State and Regional Innovation Initiatives; Wessner CW, editor.

Washington (DC): National Academies Press (US); 2013.

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Building the Ohio Innovation Economy: Summary of a Symposium.

National Research Council (US) Committee on Competing in the 21st Century: Best Practice in State and Regional Innovation Initiatives.

Washington (DC): National Academies Press (US); 2013.

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Select item 518980212.

Learning from Rapid Response, Innovation, and Adaptation to the COVID-19 Crisis: Proceedings of a Workshop—in Brief.

National Academies of Sciences, Engineering, and Medicine; Policy and Global Affairs; Government-University-Industry Research Roundtable; Whitacre P, editor.

Washington (DC): National Academies Press (US); 2021 Apr 19.

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WormBook: The Online Review of C. elegans Biology [Internet].

Pasadena (CA): WormBook; 2005-2018.

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Enhancing U.S. Science and Innovation with Novel Cross-Sector Partnerships: Proceedings of a Workshop—in Brief.

National Academies of Sciences, Engineering, and Medicine; Policy and Global Affairs; Government-University-Industry Research Roundtable; Whitacre P, editor.

Washington (DC): National Academies Press (US); 2022 Dec 21.

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Select item 166869015.

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 322594216.

Scientific Frontiers in Developmental Toxicology and Risk Assessment.

National Research Council (US) Committee on Developmental Toxicology.

Washington (DC): National Academies Press (US); 2000.

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Select item 555888417.

Systems Biology: Functional Strategies of Living Organisms [Internet]. 2nd edition.

Konieczny L, Roterman-Konieczna I, Spólnik P.

Cham (CH): Springer; 2023.

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Select item 160721218.

Developmental Biology. 6th edition.

Gilbert SF.

Sunderland (MA): Sinauer Associates; 2000.

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Retroviruses.

Coffin JM, Hughes SH, Varmus HE, editors.

Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 1997.

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Select item 186695420.

C. elegans II. 2nd edition.

Riddle DL, Blumenthal T, Meyer BJ, et al., editors.

Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 1997.

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Figure 12.52Structure of collagen

(A) Three polypeptide chains coil around one another in a characteristic triple helix structure. (B) The amino acid sequence of a collagen triple helix domain consists of Gly-X-Y repeats, in which X is frequently proline and Y is frequently hydroxyproline (Hyp).

Cell Walls and the Extracellular Matrix.

Cooper GM. The Cell: A Molecular Approach. 2nd edition. Sunderland (MA): Sinauer Associates; 2000.
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 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.
Figure 19-43The structure of a typical collagen molecule

(A) A model of part of a single collagen α chain in which each amino acid is represented by a sphere. The chain is about 1000 amino acids long. It is arranged as a left-handed helix, with three amino acids per turn and with glycine as every third amino acid. Therefore, an α chain is composed of a series of triplet Gly-X-Y sequences, in which X and Y can be any amino acid (although X is commonly proline and Y is commonly hydroxyproline). (B) A model of part of a collagen molecule in which three α chains, each shown in a different color, are wrapped around one another to form a triple-stranded helical rod. Glycine is the only amino acid small enough to occupy the crowded interior of the triple helix. Only a short length of the molecule is shown; the entire molecule is 300 nm long. (From model by B.L. Trus.)

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.

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Medicine and Improvement in the Scots Magazine; and Edinburgh Literary Miscellan...
Medicine and Improvement in the Scots Magazine; and Edinburgh Literary Miscellany (1804–17) - Cultures of Improvement in Scottish Romanticism, 1707–1840

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