Structural organization of intercellular channels II. Amino terminal domain of the connexins: sequence, functional roles, and structure

Autor: Gregory M. Lipkind, Eric C. Beyer, John W. Kyle, Viviana M. Berthoud

Publikováno v: Biochimica et Biophysica Acta (BBA) - Biomembranes. 1818(8):1823-1830

The amino terminal domain (NT) of the connexins consists of their first 22–23 amino acids. Site-directed mutagenesis studies have demonstrated that NT amino acids are determinants of gap junction channel properties including unitary conductance, pe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::413dfa388132e85c99cba925f535218e

The Tetrodotoxin Binding Site Is within the Outer Vestibule of the Sodium Channel

Autor: Harry A. Fozzard, Gregory M. Lipkind

Publikováno v: Marine Drugs, Vol 8, Iss 2, Pp 219-234 (2010)
Marine Drugs

Tetrodotoxin and saxitoxin are small, compact asymmetrical marine toxins that block voltage-gated Na channels with high affinity and specificity. They enter the channel pore's outer vestibule and bind to multiple residues that control permeation. Rad

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f86d2539cacfe28de1400eb20df092ec
http://www.mdpi.com/1660-3397/8/2/219/

THEORETICAL CONFORMATIONAL ANALYSIS OF METHYLAMIDES OF N-ACETYL-L-SERINE AND N-ACETYL-L-ASPARAGINE

Autor: E. M. Popov, Gregory M. Lipkind, S. F. Arkhipova

Publikováno v: International Journal of Peptide and Protein Research. 5:381-397

Theoretical analysis of conformations of methylamides of N-acetyl-L-serine and N-acetyl-L-asparagine was carried out proceeding from a mechanical molecular model. The important role of hydrogen bonds between the side chain and the backbone in stabili

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6f426e17ecc6b4c3f3f57c17d652e65
https://doi.org/10.1111/j.1399-3011.1973.tb02343.x

Insulin gene mutations as a cause of permanent neonatal diabetes

Autor: Siri Atma W. Greeley, Anna Pluzhnikov, Nancy J. Cox, Emma L. Edghill, Julie Støy, Sarah E. Flanagan, Louis H. Philipson, Honggang Ye, Donald F. Steiner, Jennifer E. Below, Andrew T. Hattersley, Veronica Paz, Rebecca B. Lipton, Gregory M. Lipkind, Sian Ellard, Graeme I. Bell, M. Geoffrey Hayes, Ann-Marie Patch

Publikováno v: Støy, J, Edghill, E L, Flanagan, S E, Ye, H, Paz, V P, Pluzhnikov, A, Below, J E, Hayes, M G, Cox, N J, Lipkind, G M, Lipton, R B, Greeley, S A W, Patch, A-M, Ellard, S, Steiner, D F, Hattersley, A T, Philipson, L H, Bell, G I & Neonatal Diabetes International Collaborative Group 2007, ' Insulin gene mutations as a cause of permanent neonatal diabetes ', Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 38, pp. 15040-4 . https://doi.org/10.1073/pnas.0707291104

We report 10 heterozygous mutations in the human insulin gene in 16 probands with neonatal diabetes. A combination of linkage and a candidate gene approach in a family with four diabetic members led to the identification of the initial INS gene mutat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3233c4a4bea945868ca35ac344af639
https://doi.org/10.1073/pnas.0707291104

Isoform-dependent interaction of voltage-gated sodium channels with protons

Autor: Gregory M. Lipkind, Harry A. Fozzard, A. Khan, John W. Kyle, Dorothy A. Hanck

Publikováno v: The Journal of Physiology. 576:493-501

Protons are potent physiological modifiers of voltage-gated Na+ channels, shifting the voltage range of channel gating and reducing current magnitude (pKa∼6). We recently showed that proton block of the skeletal muscle isoform (NaV1.4) resulted fro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::003bf0a2cc6cb8bde5bc6f74e6bd5dbb
https://doi.org/10.1113/jphysiol.2006.115659