Novel Sites of N-Glycosylation in ROMK1 Reveal the Putative Pore-forming Segment H5 as Extracellular-Reference-Cited by-同舟云学术

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Novel Sites of N-Glycosylation in ROMK1 Reveal the Putative Pore-forming Segment H5 as Extracellular

Published:1996-09 Issue:39 Volume:271 Page:24201-24206
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Schwalbe Ruth A.,Wang Zhiguo,Bianchi Laura,Brown Arthur M.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference33 articles.

1. Nature;Ho,1993

2. Science;Taglialatela,1994

3. Science;Ficker,1994

4. Strong voltage-dependent inward rectification of inward rectifier K+ channels is caused by intracellular spermine

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1. Rapid Preparation of Released N-Glycans for HILIC Analysis Using a Labeling Reagent that Facilitates Sensitive Fluorescence and ESI-MS Detection;Analytical Chemistry;2015-05-08

2. Sialic acids attached to N- and O-glycans within the Nav1.4 D1S5–S6 linker contribute to channel gating;Biochimica et Biophysica Acta (BBA) - General Subjects;2015-02

3. Modulation of Voltage‐Gated Ion Channels by Sialylation;Comprehensive Physiology;2012-04

4. Evidence against Extracellular Exposure of a Highly Immunogenic Region in the C-Terminal Domain of the Simian Immunodeficiency Virus gp41 Transmembrane Protein;Journal of Virology;2011-11-09

5. Impaired glycosylation blocks DPP10 cell surface expression and alters the electrophysiology of I to channel complex;Pflügers Archiv - European Journal of Physiology;2010-03-31

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