Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Steve A N Goldstein"'
Bunyavirus requirement for endosomal K+ reveals new roles of cellular ion channels during infection.
Autor:
Samantha Hover, Becky Foster, Juan Fontana, Alain Kohl, Steve A N Goldstein, John N Barr, Jamel Mankouri
Publikováno v:
PLoS Pathogens, Vol 14, Iss 1, p e1006845 (2018)
In order to multiply and cause disease a virus must transport its genome from outside the cell into the cytosol, most commonly achieved through the endocytic network. Endosomes transport virus particles to specific cellular destinations and viruses e
Externí odkaz:
https://doaj.org/article/4507de61e0c8440783ae8ed163af20ee
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(23)
The human voltage-gated proton channel (hHv1) is important for control of intracellular pH. We designed C6, a specific peptide inhibitor of hHv1, to evaluate the roles of the channel in sperm capacitation and in the inflammatory immune response of ne
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22d318ee003815591f16a09349c5a13c
https://pubmed.ncbi.nlm.nih.gov/35648818
https://pubmed.ncbi.nlm.nih.gov/35648818
Autor:
Ruiming, Zhao, Steve A N, Goldstein
Publikováno v:
Methods in enzymology. 654
In this method paper, we describe protocols for using membrane-tethered peptide toxins (T-toxins) to study the structure/function and biophysics of toxin-channel interactions with two-electrode voltage clamp (TEVC). Here, we show how T-toxins can be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b6be9bacdfebbbf6b4256f5649d17f5f
https://pubmed.ncbi.nlm.nih.gov/34120714
https://pubmed.ncbi.nlm.nih.gov/34120714
Autor:
Anthony, Lewis, Zoe A, McCrossan, Rían W, Manville, M Oana, Popa, Luis G, Cuello, Steve A N, Goldstein
Publikováno v:
FASEB J
TOKs are outwardly rectifying K(+) channels in fungi with two pore-loops and eight transmembrane spans. Here, we describe the TOKs from four pathogens that cause the majority of life-threatening fungal infections in humans. These TOKs pass large curr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3c4335c60f0f0316df72e07c9c7c278f
https://pubmed.ncbi.nlm.nih.gov/32519783
https://pubmed.ncbi.nlm.nih.gov/32519783
Publikováno v:
Cell reports
SUMMARY Acute cardiac hypoxia produces life-threatening elevations in late sodium current (ILATE) in the human heart. Here, we show the underlying mechanism: hypoxia induces rapid SUMOylation of NaV1.5 channels so they reopen when normally inactive,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9114b962f059e669873b5554bb0c59ef
https://pubmed.ncbi.nlm.nih.gov/32075761
https://pubmed.ncbi.nlm.nih.gov/32075761
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 114(32)
The slow delayed rectifier K+ current (IKs) determines the length of each human heartbeat because it activates after myocytes are excited and depolarize. This sensitivity to voltage, as well as dynamic regulation by hormones and second messengers, un
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::007db9f5e34de6bff9fcbd69a170de1b
https://pubmed.ncbi.nlm.nih.gov/28743749
https://pubmed.ncbi.nlm.nih.gov/28743749
Autor:
Daniel I, Levy, Egle, Cepaitis, Sherry, Wanderling, Peter T, Toth, Stephen L, Archer, Steve A N, Goldstein
Publikováno v:
The Journal of physiology. 588(Pt 14)
MiRP3, the single-span membrane protein encoded by KCNE4, is localized by immunofluorescence microscopy to the transverse tubules of murine cardiac myocytes. MiRP3 is found to co-localize with Kv4.2 subunits that contribute to cardiac transient outwa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e8fb55c194e196502cfb16a809fbd747
https://pubmed.ncbi.nlm.nih.gov/20498229
https://pubmed.ncbi.nlm.nih.gov/20498229
Autor:
Leo A, Kim, Johannes, Furst, David, Gutierrez, Margaret H, Butler, Shuhua, Xu, Steve A N, Goldstein, Nikolaus, Grigorieff
Publikováno v:
Neuron. 41(4)
Regulatory KChIP2 subunits assemble with pore-forming Kv4.2 subunits in 4:4 complexes to produce native voltage-gated potassium (Kv) channels like cardiac I(to) and neuronal I(A) subtypes. Here, negative stain electron microscopy (EM) and single part
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4844cbed2dfa0aecf5de7a4e9d91dc6c
https://pubmed.ncbi.nlm.nih.gov/14980201
https://pubmed.ncbi.nlm.nih.gov/14980201
Publikováno v:
Cell. 111(4)
Proteins with dibasic retention motifs are subject to retrograde transport to endoplasmic reticulum (ER) by COPI-coated vesicles. As forward transport requires escape from ER retention, general release mechanisms have been expected. Here, KCNK3 potas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fa850a676511213bffb6e57d7fbcb610
https://pubmed.ncbi.nlm.nih.gov/12437930
https://pubmed.ncbi.nlm.nih.gov/12437930
Autor:
Ruiming Zhao, Hui Dai, Rodolfo J. Arias, Gerardo A. De Blas, Gerardo Orta, Martín A. Pavarotti, Rong Shen, Eduardo Perozo, Luis S. Mayorga, Alberto Darszon, Steve A. N. Goldstein
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
The human voltage-gated proton channel (hHv1) maintains intracellular pH and membrane potential in sperm and neutrophils. Here, the authors show that albumin activates hHv1, by binding to the channel voltage sensor domains to enhance open probability
Externí odkaz:
https://doaj.org/article/c46008eddc1543f7b537b4b7900693ee