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Gap Junctions in the Nervous System
Paperback

Gap Junctions in the Nervous System

$276.99
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This title is printed to order. This book may have been self-published. If so, we cannot guarantee the quality of the content. In the main most books will have gone through the editing process however some may not. We therefore suggest that you be aware of this before ordering this book. If in doubt check either the author or publisher’s details as we are unable to accept any returns unless they are faulty. Please contact us if you have any questions.

A Cytoplasm Connexon or Hemichannel Cytoplasm external loop I - P. M. N-Termlnus Fig. 1. 1. Topology of gap junction channels. (A) Cap junction channels, extending from the cytoplasm of one cell to the cytoplasm of another, are formed by two connexons or hemichannels connected across extracellular space. (B) Each connexon is formed from six connexin subunits, each having four membrane-spanning domains and both amino and carboxyl termini within the cytoplasm. External/oops (I and II} are believed to provide the high affinity interactions between the hemichannels. 4 Gap }unctions in the Nervous System P-region of voltage sensitive nonjunctional molecules; these contributed disulfide 9 channels. And Delmar’s group has ob- bridges are presumably involved in intra- tained evidence that intracellular acidifi- connexin and inter-EL loop tertiary struc- cation may result in a conformational ture. An old observation that should be change analogous to the ball and chain repeated stoichiometrically with modern techniques is that gap junction channels model of inactivation of voltage gated ionic can be split into connexons or hemi- channels, whereby the carboxyl terminal channels using hyperosmotic disaccharide portion of connexin43 binds to CL, closing 23 solutions again implying that linkage is the channel. Higher order structure of the channel not covalent. is believed to consist of six connexins form- ing the hemichannel or connexon in a 3.

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MORE INFO
Format
Paperback
Publisher
Springer-Verlag Berlin and Heidelberg GmbH & Co. KG
Country
Germany
Date
13 November 2013
Pages
317
ISBN
9783662219379

This title is printed to order. This book may have been self-published. If so, we cannot guarantee the quality of the content. In the main most books will have gone through the editing process however some may not. We therefore suggest that you be aware of this before ordering this book. If in doubt check either the author or publisher’s details as we are unable to accept any returns unless they are faulty. Please contact us if you have any questions.

A Cytoplasm Connexon or Hemichannel Cytoplasm external loop I - P. M. N-Termlnus Fig. 1. 1. Topology of gap junction channels. (A) Cap junction channels, extending from the cytoplasm of one cell to the cytoplasm of another, are formed by two connexons or hemichannels connected across extracellular space. (B) Each connexon is formed from six connexin subunits, each having four membrane-spanning domains and both amino and carboxyl termini within the cytoplasm. External/oops (I and II} are believed to provide the high affinity interactions between the hemichannels. 4 Gap }unctions in the Nervous System P-region of voltage sensitive nonjunctional molecules; these contributed disulfide 9 channels. And Delmar’s group has ob- bridges are presumably involved in intra- tained evidence that intracellular acidifi- connexin and inter-EL loop tertiary struc- cation may result in a conformational ture. An old observation that should be change analogous to the ball and chain repeated stoichiometrically with modern techniques is that gap junction channels model of inactivation of voltage gated ionic can be split into connexons or hemi- channels, whereby the carboxyl terminal channels using hyperosmotic disaccharide portion of connexin43 binds to CL, closing 23 solutions again implying that linkage is the channel. Higher order structure of the channel not covalent. is believed to consist of six connexins form- ing the hemichannel or connexon in a 3.

Read More
Format
Paperback
Publisher
Springer-Verlag Berlin and Heidelberg GmbH & Co. KG
Country
Germany
Date
13 November 2013
Pages
317
ISBN
9783662219379