Matrix Metalloproteinases (Biology of Extracellular Matrix) by William C. Parks, Robert P. Mecham PDF

By William C. Parks, Robert P. Mecham

ISBN-10: 0125450907

ISBN-13: 9780125450904

The chapters during this booklet completely conceal the constitution, rules, and serve as of matrix metalloproteinases, and supply details at the most recent recommendations to inhibit enzyme task. This paintings might be an crucial reference software for investigators with an curiosity in extracellular matrix biology, matrix turnover, enzymology and biochemistry of proteinases, developmental biology, pathology, and healing interventions. Key beneficial properties* presents state of the art info on a box with extensive implications to many parts of biology* contains specific assurance of the constitution and rules of all significant matrix metalloproteinases* Chapters concentrate on a well timed and increasing box* subject matters have direct relevance to knowing human ailment pathology of melanoma, arthritis, and vascular affliction* Discusses most recent ideas utilized in the advance of latest therapeutics to inhibit metalloproteinase task

Show description

Read or Download Matrix Metalloproteinases (Biology of Extracellular Matrix) PDF

Best molecular biology books

Read e-book online Mathematical Biology: I. An Introduction (Interdisciplinary PDF

Great publication, in nice situation and it bought within the correct position on the correct time.

New PDF release: Actin-Binding Proteins and Disease

This quantity, written via specialists within the box, is the 1st to house the connection among human disorder and the actin cytoskeleton. It presents overviews of actin and chosen actin-binding proteins, after which specializes in ailments that contain those proteins. particular chapters care for actin, cofilin, profilin, gelsolin and thymosin ¾4.

The Molecular Biology of Cancer: A Bridge from Bench to - download pdf or read online

 The Molecular Biology of melanoma, Stella Pelengaris & Michael Khan  This taking pictures, complete textual content, greatly revised and up to date for its moment variation, presents a close assessment of the molecular mechanisms underpinning the advance of melanoma and its therapy.  “Bench to Bedside”: A key power of this e-book that units it except basic melanoma biology references is the interweaving of all points of melanoma biology from the explanations, improvement and prognosis via to the therapy and care of melanoma sufferers – crucial for offering a broader view of melanoma and its impression.

New PDF release: A Genetic Switch: Phage Lambda Revisited

The 1st version of Mark Ptashne's 1986 e-book describing the foundations of gene legislation in phage lambda turned a vintage in either content material and shape, surroundings a customary of readability and distinct prose that has hardly ever been bettered. This version is a reprint of the unique textual content, including a brand new bankruptcy updating the tale to 2004.

Additional resources for Matrix Metalloproteinases (Biology of Extracellular Matrix)

Sample text

In the case of the rat homologue, the catalytic efficiency against type II collagen is approximately equal to that exhibited against types I and III. In the case of human MMP-13, the catalytic efficiency of the enzyme against type II collagen is some 10-fold higher than the efficiency of the enzyme on types I and II. , 1997). The biological significance of this unanticipated extra cleavage in cartilage collagen is unknown. In addition, it has been found that human MMP13 degrades denatured collagen extremely efficiently, as had previously been shown for rat collagenase.

J. (1986). The biological regulation of collagenase activity. P. ), pp. ] 24 JOHN J. JEFFREY When the data describing the energetics of MMP-1 activity are taken together with the considerations presented by the structural analyses of MMP-1, it is tempting to paint a picture of a combination of scissile bonds in a hydrophobic environment, requiring energy to transport the water of hydrolysis to the correct site. Together with major induced-fit changes in the enzyme molecule to fully enable an active site that appears to have difficulty accessing its substrate the result is a low rate ofproteolysis.

Collagen and collagenase--Pregnancy and parturition. Semin. Perinatol. 15, 118-126. , et al. (1983). Studies on the activation energy and deuterium effect of human skin collagenase on homologous collagen substrates. J. Biol. Chem. 258, 11123-11127. Jenne, D. (1991). Homology of placental protein 11 and pea seed albumin 2 with vitronectin. Biochem. Biophys. Res. Commun. 176, 1000-1006. K. (1987). Nucleotide sequence and organization of the human S-protein gene: Repeating peptide motifs in the pexin family and a model for their evolution.

Download PDF sample

Matrix Metalloproteinases (Biology of Extracellular Matrix) by William C. Parks, Robert P. Mecham


by Daniel
4.3

Rated 4.85 of 5 – based on 32 votes