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Download Molecular Structure and Function of the Tight Junction: From Basic Mechanisms to Clinical Manifestations, Volume 1165 (Annals of the New York Academy of Sciences) fb2

by Michael Fromm,Jörg-Dieter Schulzke

Download Molecular Structure and Function of the Tight Junction: From Basic Mechanisms to Clinical Manifestations, Volume 1165 (Annals of the New York Academy of Sciences) fb2
Author: Michael Fromm,Jörg-Dieter Schulzke
ISBN: 1573317497
Language: English
Pages: 300 pages
Category: Medicine
Publisher: Wiley-Blackwell; 1 edition (June 22, 2009)
Rating: 4.6
Formats: mobi txt rtf lrf
FB2 size: 1175 kb | EPUB size: 1979 kb | DJVU size: 1848 kb

Tight junctions: Molecular structure meets function (Jörg-Dieter Schulzke and Michael Fromm). The Life and Work of Shoichiro Tsukita (James Melvin Anderson). 41. No static at all: A new perspective on molecular architecture of the tight junction (W. Vallen Graham, Amanda M. Marchiando, Le Shen and Jerrold R. Turner). 42. Lymphoepithelial Interactions: A new paradigm (Stephanie Dahan, Franziska Roth-Walter, Andrea P. Martin, Paul Arnaboldi and Lloyd Mayer).

Aim of this volume is to clarify the relationship between molecular structure and function of tight junction proteins, as well as their regulation and their role in diseases.

The relationship between the molecular structure and function of tight junction proteins, as well as their .

The relationship between the molecular structure and function of tight junction proteins, as well as their regulation and their role in disease, is discussed.

Article in Annals of the New York Academy of Sciences 1165:1-6 · June 2009 with 42 Reads. Occludin, tricellulin and members of the claudin family constitute and physically seal tight junctions ( Schulzke and Fromm, 2009). How we measure 'reads'. To date, 24 claudins with molecular weights ranging from 20 to 27 kDa have been identified in mammals with high sequence homology in extracellular loops and in the first and fourth transmembrane domains ( Schulzke and Fromm, 2009;Yamamoto et a. 2008). Tight junctions play a central role in maintaining structural integrity of the BB. .

The 13-digit and 10-digit formats both work.

Volume Title: Molecular Structure and Function of the Tight Junction: From Basic Mechanisms to Clinical Manifestations. Date Submitted by the Author: 17-Oct-2008. 3 claudins appear to belong to the basic pattern of epithelial tight junction proteins, as both are. 4. 5 found in combination in many organs, such as liver, lung, kidney, colon,22 and skin.

Annals of the New York Academy of Sciences ; v. 1165 . Rubrics: Cell junctions Tight junctions (Cell biology) Congresses Tight Junctions. On this site it is impossible to download the book, read the book online or get the contents of a book. The administration of the site is not responsible for the content of the site.

Molecular structure and function of the tight junction: from basic . M Fromm, JD Schulzke.

Molecular structure and function of the tight junction: from basic mechanisms to clinical manifestations. Conference on Molecular Structure and Function of the Tight Junction - From Basic Mechanisms to Clinical Manifestations -, Germany Duration: 25-Apr-2008 → 27-Apr-2008. Annals of the new york academy of sciences. BLACKWELL PUBLISHING.

Tight junctions consist of proteins that physically "seal" the tight junction but also form channels that allow . Jörg-Dieter Schulzke, Michael Fromm. Journal Annals of the New York Academy of Sciences. Pages 1-6. Publication Date 1 May 2009.

Tight junctions consist of proteins that physically "seal" the tight junction but also form channels that allow for permeation between the cells, resulting in epithelial surfaces of different tightness. The tight junction proteins occludin, tricellulin, and at least 24 members of the claudin family are characterized by four transmembranal domains and two extracellular loops that, like teeth of a zipper, contact the appropriate loops from opposing cell membranes.

Most claudins are tight junction (TJ)-forming proteins Annals of the New Yor. Cellular and Molecular Life Sciences CMLS.

Most claudins are tight junction (TJ)-forming proteins. However, their interaction on the molecular level remains unresolved. cle{F, title {Structure and function of extracellular claudin domains. author {Gerd Krause and Lars Winkler and Christian Piehl and Ingolf E Blasig and J{"o}rg Piontek and Sebastian L Mueller}, journal {Annals of the New York Academy of Sciences}, year {2009}, volume {1165}, pages {. Annals of the New Yor. 009.

Aim of this volume is to clarify the relationship between molecularstructure and function of tight junction proteins, as well as theirregulation and their role in diseases. Current research may form abasis for future diagnostic and therapeutic approaches to diseaseswhich seem to have not much in common but are characterized bydefects of organ barriers, like Crohn's disease, renalhypertension, inner ear deafness, and cancerous diseases.

Topics include the functions of distinct tight junction proteinsas barrier or channel formers for solutes and water,characteristics of the tight junction in inflammatory boweldiseases, posttranslational modifications of tight junctionproteins, the relation between renal tight junction proteins andblood pressure control, and the molecular structure ofclaudin-claudin interactions

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