LIVIVO - Search results -

Search results

Result 1 - 10 of total 65

Search options

Article ; Online: 35 years of channelling potassium ions.

Nimigean, Crina M

2022 Volume 608, Issue 7924, Page(s) 670–672

MeSH term(s)	History, 20th Century ; History, 21st Century ; Ion Channels/history ; Ion Channels/metabolism ; Ion Transport ; Ions/metabolism ; Potassium/metabolism
Chemical Substances	Ion Channels ; Ions ; Potassium (RWP5GA015D)
Language	English
Publishing date	2022-08-15
Publishing country	England
Document type	Historical Article ; Journal Article
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/d41586-022-02163-3
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 9: Show issues
Zs.MO 244: Show issues

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Polyamine block of MthK potassium channels.

Nimigean, Crina M

The Journal of general physiology

2020 Volume 152, Issue 7

MeSH term(s)	Ion Channel Gating ; Polyamines ; Potassium Channels/metabolism ; Potassium Channels, Calcium-Activated/metabolism
Chemical Substances	Polyamines ; Potassium Channels ; Potassium Channels, Calcium-Activated
Language	English
Publishing date	2020-05-27
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	3118-5
ISSN	1540-7748 ; 0022-1295
ISSN (online)	1540-7748
ISSN	0022-1295
DOI	10.1085/jgp.202012614
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.150: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Ball-and-Chain Inactivation in Potassium Channels.

Sukomon, Nattakan / Fan, Chen / Nimigean, Crina M

Annual review of biophysics

2023 Volume 52, Page(s) 91–111

Abstract: Carefully orchestrated opening and closing of ion channels control the diffusion of ions across cell membranes, generating the electrical signals required for fast transmission of information throughout the nervous system. Inactivation is a parsimonious ... ...

Abstract	Carefully orchestrated opening and closing of ion channels control the diffusion of ions across cell membranes, generating the electrical signals required for fast transmission of information throughout the nervous system. Inactivation is a parsimonious means for channels to restrict ion conduction without the need to remove the activating stimulus. Voltage-gated channel inactivation plays crucial physiological roles, such as controlling action potential duration and firing frequency in neurons. The ball-and-chain moniker applies to a type of inactivation proposed first for sodium channels and later shown to be a universal mechanism. Still, structural evidence for this mechanism remained elusive until recently. We review the ball-and-chain inactivation research starting from its introduction as a crucial component of sodium conductance during electrical signaling in the classical Hodgkin and Huxley studies, through the discovery of its simple intuitive mechanism in potassium channels during the molecular cloning era, to the eventual elucidation of a potassium channel structure in a ball-and-chain inactivated state.
MeSH term(s)	Potassium Channels/chemistry ; Cell Membrane ; Signal Transduction
Chemical Substances	Potassium Channels
Language	English
Publishing date	2023-01-10
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	2434725-5
ISSN	1936-1238 ; 1936-122X
ISSN (online)	1936-1238
ISSN	1936-122X
DOI	10.1146/annurev-biophys-100322-072921
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Se 190: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Calcium-gated potassium channel blockade via membrane-facing fenestrations.

Fan, Chen / Flood, Emelie / Sukomon, Nattakan / Agarwal, Shubhangi / Allen, Toby W / Nimigean, Crina M

Nature chemical biology

2023 Volume 20, Issue 1, Page(s) 52–61

Abstract: Quaternary ammonium blockers were previously shown to bind in the pore to block both open and closed conformations of large-conductance calcium-activated potassium (BK and MthK) channels. Because blocker entry was assumed through the intracellular ... ...

Abstract	Quaternary ammonium blockers were previously shown to bind in the pore to block both open and closed conformations of large-conductance calcium-activated potassium (BK and MthK) channels. Because blocker entry was assumed through the intracellular entryway (bundle crossing), closed-pore access suggested that the gate was not at the bundle crossing. Structures of closed MthK, a Methanobacterium thermoautotrophicum homolog of BK channels, revealed a tightly constricted intracellular gate, leading us to investigate the membrane-facing fenestrations as alternative pathways for blocker access directly from the membrane. Atomistic free energy simulations showed that intracellular blockers indeed access the pore through the fenestrations, and a mutant channel with narrower fenestrations displayed no closed-state TPeA block at concentrations that blocked the wild-type channel. Apo BK channels display similar fenestrations, suggesting that blockers may use them as access paths into closed channels. Thus, membrane fenestrations represent a non-canonical pathway for selective targeting of specific channel conformations, opening novel ways to selectively drug BK channels.
MeSH term(s)	Large-Conductance Calcium-Activated Potassium Channels/metabolism ; Calcium/metabolism ; Calcium Channels/metabolism ; Potassium/metabolism ; Molecular Conformation
Chemical Substances	Large-Conductance Calcium-Activated Potassium Channels ; Calcium (SY7Q814VUP) ; Calcium Channels ; Potassium (RWP5GA015D)
Language	English
Publishing date	2023-08-31
Publishing country	United States
Document type	Journal Article
ZDB-ID	2202962-X
ISSN	1552-4469 ; 1552-4450
ISSN (online)	1552-4469
ISSN	1552-4450
DOI	10.1038/s41589-023-01406-2
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 6251: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MG 90: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Correlating ion channel structure and function.

Schmidpeter, Philipp A M / Nimigean, Crina M

Methods in enzymology

2021 Volume 652, Page(s) 3–30

Abstract: Recent developments in cryogenic electron microscopy (cryo-EM) led to an exponential increase in high-resolution structures of membrane proteins, and in particular ion channels. However, structures alone can only provide limited information about the ... ...

Abstract	Recent developments in cryogenic electron microscopy (cryo-EM) led to an exponential increase in high-resolution structures of membrane proteins, and in particular ion channels. However, structures alone can only provide limited information about the workings of these proteins. In order to understand ion channel function and regulation in molecular detail, the obtained structural data need to be correlated to functional states of the same protein. Here, we describe several techniques that can be employed to study ion channel structure and function in vitro and under defined, similar conditions. Lipid nanodiscs provide a native-like environment for membrane proteins and have become a valuable tool in membrane protein structural biology and biophysics. Combined with liposome-based flux assays for the kinetic analysis of ion channel activity as well as electrophysiological recordings, researchers now have access to an array of experimental techniques allowing for detailed structure-function correlations using purified components. Two examples are presented where we put emphasis on the lipid environment and time-resolved techniques together with mutations and protein engineering to interpret structural data obtained from single particle cryo-EM on cyclic nucleotide-gated or Ca
MeSH term(s)	Cryoelectron Microscopy ; Ion Channels ; Kinetics ; Lipids ; Membrane Proteins/genetics
Chemical Substances	Ion Channels ; Lipids ; Membrane Proteins
Language	English
Publishing date	2021-03-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1557-7988
ISSN (online)	1557-7988
DOI	10.1016/bs.mie.2021.02.016
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: A pentameric TRPV3 channel with a dilated pore.

Lansky, Shifra / Betancourt, John Michael / Zhang, Jingying / Jiang, Yining / Kim, Elizabeth D / Paknejad, Navid / Nimigean, Crina M / Yuan, Peng / Scheuring, Simon

Nature

2023 Volume 621, Issue 7977, Page(s) 206–214

Abstract: Transient receptor potential (TRP) channels are a large, eukaryotic ion channel superfamily that control diverse physiological functions, and therefore are attractive drug ... ...

Abstract	Transient receptor potential (TRP) channels are a large, eukaryotic ion channel superfamily that control diverse physiological functions, and therefore are attractive drug targets
MeSH term(s)	Anhydrides/chemistry ; Anhydrides/pharmacology ; Data Analysis ; Diffusion ; Protein Subunits/chemistry ; Protein Subunits/drug effects ; Protein Subunits/metabolism ; TRPV Cation Channels/chemistry ; TRPV Cation Channels/drug effects ; TRPV Cation Channels/metabolism ; TRPV Cation Channels/ultrastructure ; Microscopy, Atomic Force ; Molecular Targeted Therapy ; Cryoelectron Microscopy ; Protein Structure, Quaternary/drug effects ; Protein Multimerization/drug effects
Chemical Substances	Anhydrides ; Protein Subunits ; diphenylborate (83075-94-9) ; TRPV Cation Channels
Language	English
Publishing date	2023-08-30
Publishing country	England
Document type	Journal Article
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-023-06470-1
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 9: Show issues
Zs.MO 244: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Membrane phospholipids control gating of the mechanosensitive potassium leak channel TREK1.

Schmidpeter, Philipp A M / Petroff, John T / Khajoueinejad, Leila / Wague, Aboubacar / Frankfater, Cheryl / Cheng, Wayland W L / Nimigean, Crina M / Riegelhaupt, Paul M

Nature communications

2023 Volume 14, Issue 1, Page(s) 1077

Abstract: Tandem pore domain (K2P) potassium channels modulate resting membrane potentials and shape cellular excitability. For the mechanosensitive subfamily of K2Ps, the composition of phospholipids within the bilayer strongly influences channel activity. To ... ...

Abstract	Tandem pore domain (K2P) potassium channels modulate resting membrane potentials and shape cellular excitability. For the mechanosensitive subfamily of K2Ps, the composition of phospholipids within the bilayer strongly influences channel activity. To examine the molecular details of K2P lipid modulation, we solved cryo-EM structures of the TREK1 K2P channel bound to either the anionic lipid phosphatidic acid (PA) or the zwitterionic lipid phosphatidylethanolamine (PE). At the extracellular face of TREK1, a PA lipid inserts its hydrocarbon tail into a pocket behind the selectivity filter, causing a structural rearrangement that recapitulates mutations and pharmacology known to activate TREK1. At the cytoplasmic face, PA and PE lipids compete to modulate the conformation of the TREK1 TM4 gating helix. Our findings demonstrate two distinct pathways by which anionic lipids enhance TREK1 activity and provide a framework for a model that integrates lipid gating with the effects of other mechanosensitive K2P modulators.
MeSH term(s)	Potassium Channels, Tandem Pore Domain/genetics ; Phospholipids ; Membrane Potentials ; Potassium/metabolism
Chemical Substances	Potassium Channels, Tandem Pore Domain ; Phospholipids ; Potassium (RWP5GA015D)
Language	English
Publishing date	2023-02-25
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-36765-w
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Reconstitution of Membrane Proteins into Platforms Suitable for Biophysical and Structural Analyses.

Schmidpeter, Philipp A M / Sukomon, Nattakan / Nimigean, Crina M

Methods in molecular biology (Clifton, N.J.)

2020 Volume 2127, Page(s) 191–205

Abstract: Integral membrane proteins have historically been challenging targets for biophysical research due to their low solubility in aqueous solution. Their importance for chemical and electrical signaling between cells, however, makes them fascinating targets ... ...

Abstract	Integral membrane proteins have historically been challenging targets for biophysical research due to their low solubility in aqueous solution. Their importance for chemical and electrical signaling between cells, however, makes them fascinating targets for investigators interested in the regulation of cellular and physiological processes. Since membrane proteins shunt the barrier imposed by the cell membrane, they also serve as entry points for drugs, adding pharmaceutical research and development to the interests. In recent years, detailed understanding of membrane protein function has significantly increased due to high-resolution structural information obtained from single-particle cryo-EM, X-ray crystallography, and NMR. In order to further advance our mechanistic understanding on membrane proteins as well as foster drug development, it is crucial to generate more biophysical and functional data on these proteins under defined conditions. To that end, different techniques have been developed to stabilize integral membrane proteins in native-like environments that allow both structural and biophysical investigations-amphipols, lipid bicelles, and lipid nanodiscs. In this chapter, we provide detailed protocols for the reconstitution of membrane proteins according to these three techniques. We also outline some of the possible applications of each technique and discuss their advantages and possible caveats.
MeSH term(s)	Biophysics/methods ; Chemistry, Analytic ; Detergents/chemistry ; Detergents/pharmacology ; Lipid Bilayers/chemistry ; Lipid Bilayers/metabolism ; Liposomes/chemistry ; Membrane Microdomains/chemistry ; Membrane Microdomains/metabolism ; Membrane Proteins/chemistry ; Membrane Proteins/isolation & purification ; Membrane Proteins/metabolism ; Micelles ; Models, Molecular ; Nanostructures/chemistry ; Polymers/chemistry ; Polymers/pharmacology ; Propylamines/chemistry ; Propylamines/pharmacology ; Protein Conformation ; Protein Folding ; Protein Renaturation/drug effects ; Protein Stability ; Solubility
Chemical Substances	Detergents ; Lipid Bilayers ; Liposomes ; Membrane Proteins ; Micelles ; Polymers ; Propylamines ; amphipol A8-35
Language	English
Publishing date	2020-02-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-0373-4_14
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- Full text online
- Order with fees

Article ; Online: Prolyl isomerization controls activation kinetics of a cyclic nucleotide-gated ion channel.

Schmidpeter, Philipp A M / Rheinberger, Jan / Nimigean, Crina M

Nature communications

2020 Volume 11, Issue 1, Page(s) 6401

Abstract: SthK, a cyclic nucleotide-modulated ion channel from Spirochaeta thermophila, activates slowly upon cAMP increase. This is reminiscent of the slow, cAMP-induced activation reported for the hyperpolarization-activated and cyclic nucleotide-gated channel ... ...

Abstract	SthK, a cyclic nucleotide-modulated ion channel from Spirochaeta thermophila, activates slowly upon cAMP increase. This is reminiscent of the slow, cAMP-induced activation reported for the hyperpolarization-activated and cyclic nucleotide-gated channel HCN2 in the family of so-called pacemaker channels. Here, we investigate slow cAMP-induced activation in purified SthK channels using stopped-flow assays, mutagenesis, enzymatic catalysis and inhibition assays revealing that the cis/trans conformation of a conserved proline in the cyclic nucleotide-binding domain determines the activation kinetics of SthK. We propose that SthK exists in two forms: trans Pro300 SthK with high ligand binding affinity and fast activation, and cis Pro300 SthK with low affinity and slow activation. Following channel activation, the cis/trans equilibrium, catalyzed by prolyl isomerases, is shifted towards trans, while steady-state channel activity is unaffected. Our results reveal prolyl isomerization as a regulatory mechanism for SthK, and potentially eukaryotic HCN channels. This mechanism could contribute to electrical rhythmicity in cells.
MeSH term(s)	Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding Sites ; Cryoelectron Microscopy ; Cyclic AMP/metabolism ; Cyclic Nucleotide-Gated Cation Channels/chemistry ; Cyclic Nucleotide-Gated Cation Channels/genetics ; Cyclic Nucleotide-Gated Cation Channels/metabolism ; Cyclosporine/pharmacology ; Ion Channel Gating/physiology ; Isomerism ; Kinetics ; Models, Molecular ; Peptidylprolyl Isomerase/metabolism ; Proline/metabolism ; Spirochaeta/metabolism
Chemical Substances	Bacterial Proteins ; Cyclic Nucleotide-Gated Cation Channels ; Cyclosporine (83HN0GTJ6D) ; Proline (9DLQ4CIU6V) ; Cyclic AMP (E0399OZS9N) ; Peptidylprolyl Isomerase (EC 5.2.1.8)
Language	English
Publishing date	2020-12-16
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-020-20104-4
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Discrimination between cyclic nucleotides in a cyclic nucleotide-gated ion channel.

Pan, Yangang / Pohjolainen, Emmi / Schmidpeter, Philipp A M / Vaiana, Andrea C / Nimigean, Crina M / Grubmüller, Helmut / Scheuring, Simon

Nature structural & molecular biology

2023 Volume 30, Issue 4, Page(s) 512–520

Abstract: Cyclic nucleotide-gated ion channels are crucial in many physiological processes such as vision and pacemaking in the heart. SthK is a prokaryotic homolog with high sequence and structure similarities to hyperpolarization-activated and cyclic nucleotide- ... ...

Abstract	Cyclic nucleotide-gated ion channels are crucial in many physiological processes such as vision and pacemaking in the heart. SthK is a prokaryotic homolog with high sequence and structure similarities to hyperpolarization-activated and cyclic nucleotide-modulated and cyclic nucleotide-gated channels, especially at the level of the cyclic nucleotide binding domains (CNBDs). Functional measurements showed that cyclic adenosine monophosphate (cAMP) is a channel activator while cyclic guanosine monophosphate (cGMP) barely leads to pore opening. Here, using atomic force microscopy single-molecule force spectroscopy and force probe molecular dynamics simulations, we unravel quantitatively and at the atomic level how CNBDs discriminate between cyclic nucleotides. We find that cAMP binds to the SthK CNBD slightly stronger than cGMP and accesses a deep-bound state that a cGMP-bound CNBD cannot reach. We propose that the deep binding of cAMP is the discriminatory state that is essential for cAMP-dependent channel activation.
MeSH term(s)	Nucleotides, Cyclic ; Cyclic Nucleotide-Gated Cation Channels/chemistry ; Ion Channel Gating/physiology ; Cyclic AMP/metabolism ; Cyclic GMP/metabolism
Chemical Substances	Nucleotides, Cyclic ; Cyclic Nucleotide-Gated Cation Channels ; Cyclic AMP (E0399OZS9N) ; Cyclic GMP (H2D2X058MU)
Language	English
Publishing date	2023-03-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2126708-X
ISSN	1545-9985 ; 1545-9993
ISSN (online)	1545-9985
ISSN	1545-9993
DOI	10.1038/s41594-023-00955-3
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 4101: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 56: Show issues

Order via subito

Details ▾

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito