By Jean D. Sipe
A first-stop reference on proteins linked to amyloidosis. This ebook is the 1st to give a scientific evaluation of all recognized fibril-forming proteins, together with their biochemical features and pathophysiology. It considers the clinically famous amyloid proteins which are recognized to be linked to the amyloid protein folding issues, facing their universal structural and thermodynamic gains that result in amyloid fibril formation and affliction. Emphasis is at the thermodynamics of protein folding, the constitution and physiologic results of universal oligomeric and subfibrillar intermediates and the effect of the extracellular matrix and mobile trafficking and metabolism at the genesis and catabolism of beta pleated sheet proteins. The chapters on particular amyloid proteins all persist with a typical constitution, permitting easy access to the specified biochemical and scientific information, making this a useful software for clinicians and researchers alike.
Read or Download Amyloid Proteins: The Beta Sheet Conformation and Disease PDF
Similar clinical chemistry books
Presents an advent to these desiring to exploit infrared spectroscopy for the 1st time, explaining the basic facets of this method, tips on how to receive a spectrum and the way to examine infrared information overlaying quite a lot of functions. contains instrumental and sampling strategies Covers organic and business functions comprises compatible questions and difficulties in every one bankruptcy to aid within the research and interpretation of consultant infrared spectra a part of the ANTS (Analytical innovations within the Sciences) sequence.
This ebook offers an important details in surgical oncology in an simply obtainable demeanour. it may be learn in the course of the size of a rotation on a surgical oncology carrier. Chapters are prepared via organ involvement. each one bankruptcy starts with epidemiology and screening following by way of tools of prognosis, preoperative assessment and staging.
One of many few books to hide all features of cyclin-dependent kinases (CDKs), Inhibitors of Cyclin-dependent Kinases as Anti-tumor brokers offers an summary of CDKs as molecular and sensible entities, their involvement in several disorder procedures, and their power for pharmacological modulation.
A lot contemporary examine in evolutionary developmental biology has inquisitive about the starting place of recent physique plans. although, such a lot evolutionary swap on the inhabitants and species point involves tinkering: small-scale adjustments in developmental pathways inside of a unmarried physique plan. Such microevolutionary occasions were good studied on a inhabitants genetic point and from the viewpoint of adaptive phenotypic evolution, yet their developmental mechanisms stay poorly studied.
- The ACS Style Guide: Effective Communication of Scientific Information (An American Chemical Society Publication)
- Flavourings: Production, Composition, Applications, Regulations
- Polysaccharides for Drug Delivery and Pharmaceutical Applications (ACS Symposium Series)
- Protein Purification (THE BASICS (Garland Science))
Extra resources for Amyloid Proteins: The Beta Sheet Conformation and Disease
Cohen, C. E. Jackson, Y. Kuroiwa, J. Nissim, E. Sohar, V. A. McKusick and M. W. Van Allen. Hereditary amyloidosis. Arthritis Rheum 1970, 13, 902–915. Ostertag, B. Demonstration einer eigenartigen familiären „Paramyloidose“. Zentralbl Pathol 1933, 56, 253–254. Costa, P. , A. S. Figueira and F. R. Bravo. Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy. Proc Natl Acad Sci USA 1978, 75, 4499–4503. , D. S. Goodman, R. E. Can- 112 113 114 115 116 117 118 119 120 field and F.
B. Natvig. Characterization of amyloid fibril proteins from medullary carcinoma of the thyroid. J Exp Med 1976, 143, 993–998. Benditt, E. P. and N. Eriksen. Chemical similarity among amyloid substances associated with long standing inflammation. Lab Invest 1962, 26, 615–625. Benditt, E. P. and N. Eriksen. Amyloid, III. A protein related to the subunit structure of human amyloid fibrils. Proc Natl Acad Sci USA 1966, 55, 308–316. Benditt, E. , N. Eriksen, M. A. Hermodson and L. H. Ericsson. The major proteins of human and monkey amyloid substance: common properties including unusual N-terminal amino acid sequences.
Heefner, W. A. and G. D. Sorenson. Experimental amyloidosis. I. Light and electron microscopic observations of spleen and lymph nodes. Lab Invest 1962, 11, 585–593. Cohen, A. S. and E. S. Cathcart. Caseinduced experimental amyloidosis. In Methods and Achievements in Experimental Pathology, E. Bajusz and G. Jasmin (eds). Karger, Basel, 1972, pp. 207–242. Shirahama, T. and A. S. Cohen. Intralysosomal formation of amyloid fibrils. Am J Pathol 1975, 81, 101–116. Gueft, B. and J. J. Ghidoni. The site of formation and ultrastructure of amyloid.