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Article ; Online: STRUCTURE, GATING, AND REGULATION OF THE CFTR ANION CHANNEL.

Csanády, László / Vergani, Paola / Gadsby, David C

2018 Volume 99, Issue 1, Page(s) 707–738

Abstract: The cystic fibrosis transmembrane conductance regulator (CFTR) belongs to the ATP binding cassette (ABC) transporter superfamily but functions as an anion channel crucial for salt and water transport across epithelial cells. CFTR dysfunction, because of ... ...

Abstract	The cystic fibrosis transmembrane conductance regulator (CFTR) belongs to the ATP binding cassette (ABC) transporter superfamily but functions as an anion channel crucial for salt and water transport across epithelial cells. CFTR dysfunction, because of mutations, causes cystic fibrosis (CF). The anion-selective pore of the CFTR protein is formed by its two transmembrane domains (TMDs) and regulated by its cytosolic domains: two nucleotide binding domains (NBDs) and a regulatory (R) domain. Channel activation requires phosphorylation of the R domain by cAMP-dependent protein kinase (PKA), and pore opening and closing (gating) of phosphorylated channels is driven by ATP binding and hydrolysis at the NBDs. This review summarizes available information on structure and mechanism of the CFTR protein, with a particular focus on atomic-level insight gained from recent cryo-electron microscopic structures and on the molecular mechanisms of channel gating and its regulation. The pharmacological mechanisms of small molecules targeting CFTR's ion channel function, aimed at treating patients suffering from CF and other diseases, are briefly discussed.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Animals ; Anions/metabolism ; Cystic Fibrosis Transmembrane Conductance Regulator/chemistry ; Cystic Fibrosis Transmembrane Conductance Regulator/metabolism ; Humans ; Ion Channel Gating/physiology ; Mutation/genetics ; Phosphorylation/physiology
Chemical Substances	Anions ; Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6) ; Adenosine Triphosphate (8L70Q75FXE)
Language	English
Publishing date	2018-12-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	209902-0
ISSN	1522-1210 ; 0031-9333
ISSN (online)	1522-1210
ISSN	0031-9333
DOI	10.1152/physrev.00007.2018
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Article ; Online: Ion channels versus ion pumps: the principal difference, in principle.

Gadsby, David C

Nature reviews. Molecular cell biology

2009 Volume 10, Issue 5, Page(s) 344–352

Abstract: The incessant traffic of ions across cell membranes is controlled by two kinds of border guards: ion channels and ion pumps. Open channels let selected ions diffuse rapidly down electrical and concentration gradients, whereas ion pumps labour tirelessly ... ...

Abstract	The incessant traffic of ions across cell membranes is controlled by two kinds of border guards: ion channels and ion pumps. Open channels let selected ions diffuse rapidly down electrical and concentration gradients, whereas ion pumps labour tirelessly to maintain the gradients by consuming energy to slowly move ions thermodynamically uphill. Because of the diametrically opposed tasks and the divergent speeds of channels and pumps, they have traditionally been viewed as completely different entities, as alike as chalk and cheese. But new structural and mechanistic information about both of these classes of molecular machines challenges this comfortable separation and forces its re-evaluation.
MeSH term(s)	Animals ; Humans ; Ion Channels/chemistry ; Ion Channels/metabolism ; Ion Channels/physiology ; Ion Pumps/chemistry ; Ion Pumps/metabolism ; Ion Pumps/physiology ; Protein Structure, Secondary
Chemical Substances	Ion Channels ; Ion Pumps
Language	English
Publishing date	2009-04-02
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2031313-5
ISSN	1471-0080 ; 1471-0072
ISSN (online)	1471-0080
ISSN	1471-0072
DOI	10.1038/nrm2668
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Article ; Online: Route, mechanism, and implications of proton import during Na+/K+ exchange by native Na+/K+-ATPase pumps.

Vedovato, Natascia / Gadsby, David C

The Journal of general physiology

2014 Volume 143, Issue 4, Page(s) 449–464

Abstract: A single Na(+)/K(+)-ATPase pumps three Na(+) outwards and two K(+) inwards by alternately exposing ion-binding sites to opposite sides of the membrane in a conformational sequence coupled to pump autophosphorylation from ATP and auto-dephosphorylation. ... ...

Abstract	A single Na(+)/K(+)-ATPase pumps three Na(+) outwards and two K(+) inwards by alternately exposing ion-binding sites to opposite sides of the membrane in a conformational sequence coupled to pump autophosphorylation from ATP and auto-dephosphorylation. The larger flow of Na(+) than K(+) generates outward current across the cell membrane. Less well understood is the ability of Na(+)/K(+) pumps to generate an inward current of protons. Originally noted in pumps deprived of external K(+) and Na(+) ions, as inward current at negative membrane potentials that becomes amplified when external pH is lowered, this proton current is generally viewed as an artifact of those unnatural conditions. We demonstrate here that this inward current also flows at physiological K(+) and Na(+) concentrations. We show that protons exploit ready reversibility of conformational changes associated with extracellular Na(+) release from phosphorylated Na(+)/K(+) pumps. Reversal of a subset of these transitions allows an extracellular proton to bind an acidic side chain and to be subsequently released to the cytoplasm. This back-step of phosphorylated Na(+)/K(+) pumps that enables proton import is not required for completion of the 3 Na(+)/2 K(+) transport cycle. However, the back-step occurs readily during Na(+)/K(+) transport when external K(+) ion binding and occlusion are delayed, and it occurs more frequently when lowered extracellular pH raises the probability of protonation of the externally accessible carboxylate side chain. The proton route passes through the Na(+)-selective binding site III and is distinct from the principal pathway traversed by the majority of transported Na(+) and K(+) ions that passes through binding site II. The inferred occurrence of Na(+)/K(+) exchange and H(+) import during the same conformational cycle of a single molecule identifies the Na(+)/K(+) pump as a hybrid transporter. Whether Na(+)/K(+) pump-mediated proton inflow may have any physiological or pathophysiological significance remains to be clarified.
MeSH term(s)	Animals ; Binding Sites/physiology ; Female ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proton Pumps/chemistry ; Proton Pumps/metabolism ; Sodium-Potassium-Exchanging ATPase/chemistry ; Sodium-Potassium-Exchanging ATPase/metabolism ; Xenopus Proteins/chemistry ; Xenopus Proteins/metabolism ; Xenopus laevis
Chemical Substances	Proton Pumps ; Xenopus Proteins ; atp1a1 protein, Xenopus (EC 3.6.1.-) ; Sodium-Potassium-Exchanging ATPase (EC 7.2.2.13)
Language	English
Publishing date	2014-03-31
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	3118-5
ISSN	1540-7748 ; 0022-1295
ISSN (online)	1540-7748
ISSN	0022-1295
DOI	10.1085/jgp.201311148
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Article ; Online: Structural biology: ion pumps made crystal clear.

Gadsby, David C

Nature

2007 Volume 450, Issue 7172, Page(s) 957–959

MeSH term(s)	Animals ; Crystallography, X-Ray ; Ion Transport ; Models, Molecular ; Protein Conformation ; Proton Pumps/chemistry ; Proton Pumps/metabolism ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/chemistry ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/metabolism ; Sodium-Potassium-Exchanging ATPase/chemistry ; Sodium-Potassium-Exchanging ATPase/metabolism ; Structural Homology, Protein
Chemical Substances	Proton Pumps ; Sarcoplasmic Reticulum Calcium-Transporting ATPases (EC 3.6.3.8) ; Sodium-Potassium-Exchanging ATPase (EC 3.6.3.9)
Language	English
Publishing date	2007-12-13
Publishing country	England
Document type	Comment ; News
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/450957a
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Article ; Online: Cysteine accessibility probes timing and extent of NBD separation along the dimer interface in gating CFTR channels.

Chaves, Luiz A Poletto / Gadsby, David C

The Journal of general physiology

2015 Volume 145, Issue 4, Page(s) 261–283

Abstract: Cystic fibrosis transmembrane conductance regulator (CFTR) channel opening and closing are driven by cycles of adenosine triphosphate (ATP) binding-induced formation and hydrolysis-triggered disruption of a heterodimer of its cytoplasmic nucleotide- ... ...

Abstract	Cystic fibrosis transmembrane conductance regulator (CFTR) channel opening and closing are driven by cycles of adenosine triphosphate (ATP) binding-induced formation and hydrolysis-triggered disruption of a heterodimer of its cytoplasmic nucleotide-binding domains (NBDs). Although both composite sites enclosed within the heterodimer interface contain ATP in an open CFTR channel, ATP hydrolysis in the sole catalytically competent site causes channel closure. Opening of the NBD interface at that site then allows ADP-ATP exchange. But how frequently, and how far, the NBD surfaces separate at the other, inactive composite site remains unclear. We assessed separation at each composite site by monitoring access of nucleotide-sized hydrophilic, thiol-specific methanothiosulfonate (MTS) reagents to interfacial target cysteines introduced into either LSGGQ-like ATP-binding cassette signature sequence (replacing equivalent conserved serines: S549 and S1347). Covalent MTS-dependent modification of either cysteine while channels were kept closed by the absence of ATP impaired subsequent opening upon ATP readdition. Modification while channels were opening and closing in the presence of ATP caused macroscopic CFTR current to decline at the same speed as when the unmodified channels shut upon sudden ATP withdrawal. These results suggest that the target cysteines can be modified only in closed channels; that after modification the attached MTS adduct interferes with ATP-mediated opening; and that modification in the presence of ATP occurs rapidly once channels close, before they can reopen. This interpretation was corroborated by the finding that, for either cysteine target, the addition of the hydrolysis-impairing mutation K1250R (catalytic site Walker A Lys) similarly slowed, by an order of magnitude, channel closing on ATP removal and the speed of modification by MTS reagent in ATP. We conclude that, in every CFTR channel gating cycle, the NBD dimer interface separates simultaneously at both composite sites sufficiently to allow MTS reagents to access both signature-sequence serines. Relatively rapid modification of S1347C channels by larger reagents-MTS-glucose, MTS-biotin, and MTS-rhodamine-demonstrates that, at the noncatalytic composite site, this separation must exceed 8 Å.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Cysteine/genetics ; Cystic Fibrosis Transmembrane Conductance Regulator/chemistry ; Cystic Fibrosis Transmembrane Conductance Regulator/metabolism ; Humans ; Ion Channel Gating ; Molecular Sequence Data ; Protein Binding ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Protein Subunits/metabolism ; Xenopus
Chemical Substances	CFTR protein, human ; Protein Subunits ; Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6) ; Adenosine Triphosphate (8L70Q75FXE) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2015-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	3118-5
ISSN	1540-7748 ; 0022-1295
ISSN (online)	1540-7748
ISSN	0022-1295
DOI	10.1085/jgp.201411347
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Article ; Online: Ion transport: spot the difference.

Gadsby, David C

Nature

2004 Volume 427, Issue 6977, Page(s) 795–797

MeSH term(s)	Animals ; Antiporters/chemistry ; Antiporters/genetics ; Antiporters/metabolism ; Biological Transport, Active ; Chloride Channels/chemistry ; Chloride Channels/genetics ; Chloride Channels/metabolism ; Chlorides/metabolism ; Electric Conductivity ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Ion Transport ; Models, Biological ; Proton Pumps/chemistry ; Proton Pumps/genetics ; Proton Pumps/metabolism ; Protons ; Structure-Activity Relationship
Chemical Substances	Antiporters ; Chloride Channels ; Chlorides ; Escherichia coli Proteins ; Proton Pumps ; Protons
Language	English
Publishing date	2004-02-26
Publishing country	England
Document type	Comment ; News
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/427795a
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Article ; Online: The two C-terminal tyrosines stabilize occluded Na/K pump conformations containing Na or K ions.

Vedovato, Natascia / Gadsby, David C

The Journal of general physiology

2010 Volume 136, Issue 1, Page(s) 63–82

Abstract: ... K pump crystal structures show that the extended C terminus of the Na,K-adenosine triphosphatase ... assays further suggested that C-terminal truncations also interfere with low affinity Na interactions ... interactions with extracellular Na ions are influenced by C-terminal truncations. We deleted the last two (YY ...

Abstract	Interactions of the three transported Na ions with the Na/K pump remain incompletely understood. Na/K pump crystal structures show that the extended C terminus of the Na,K-adenosine triphosphatase (ATPase) alpha subunit directly contacts transmembrane helices. Deletion of the last five residues (KETYY in almost all Na/K pumps) markedly lowered the apparent affinity for Na activation of pump phosphorylation from ATP, a reflection of cytoplasmic Na affinity for forming the occluded E1P(Na3) conformation. ATPase assays further suggested that C-terminal truncations also interfere with low affinity Na interactions, which are attributable to extracellular effects. Because extracellular Na ions traverse part of the membrane's electric field to reach their binding sites in the Na/K pump, their movements generate currents that can be monitored with high resolution. We report here electrical measurements to examine how Na/K pump interactions with extracellular Na ions are influenced by C-terminal truncations. We deleted the last two (YY) or five (KESYY) residues in Xenopus laevis alpha1 Na/K pumps made ouabain resistant by either of two kinds of point mutations and measured their currents as 10-mM ouabain-sensitive currents in Xenopus oocytes after silencing endogenous Xenopus Na/K pumps with 1 microM ouabain. We found the low affinity inhibitory influence of extracellular Na on outward Na/K pump current at negative voltages to be impaired in all of the C-terminally truncated pumps. Correspondingly, voltage jump-induced transient charge movements that reflect pump interactions with extracellular Na ions were strongly shifted to more negative potentials; this signals a several-fold reduction of the apparent affinity for extracellular Na in the truncated pumps. Parallel lowering of Na affinity on both sides of the membrane argues that the C-terminal contacts provide important stabilization of the occluded E1P(Na3) conformation, regardless of the route of Na ion entry into the binding pocket. Gating measurements of palytoxin-opened Na/K pump channels additionally imply that the C-terminal contacts also help stabilize pump conformations with occluded K ions.
MeSH term(s)	Acrylamides/pharmacology ; Amino Acid Substitution/physiology ; Animals ; Binding, Competitive/physiology ; Cnidarian Venoms ; Electrophysiological Phenomena/drug effects ; Electrophysiological Phenomena/physiology ; Ion Channel Gating/drug effects ; Ion Channel Gating/physiology ; Membrane Potentials/physiology ; Oocytes/metabolism ; Ouabain/pharmacology ; Patch-Clamp Techniques ; Poisons/pharmacology ; Potassium/metabolism ; Protein Binding/physiology ; Protein Conformation/drug effects ; RNA, Complementary/genetics ; Sequence Deletion/physiology ; Sodium/metabolism ; Sodium-Potassium-Exchanging ATPase/drug effects ; Sodium-Potassium-Exchanging ATPase/physiology ; Tyrosine/physiology ; Xenopus Proteins/drug effects ; Xenopus Proteins/physiology ; Xenopus laevis
Chemical Substances	Acrylamides ; Cnidarian Venoms ; Poisons ; RNA, Complementary ; Xenopus Proteins ; Tyrosine (42HK56048U) ; Ouabain (5ACL011P69) ; Sodium (9NEZ333N27) ; atp1a1 protein, Xenopus (EC 3.6.1.-) ; Sodium-Potassium-Exchanging ATPase (EC 7.2.2.13) ; palytoxin (OQ17NC0MOV) ; Potassium (RWP5GA015D)
Language	English
Publishing date	2010-06-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	3118-5
ISSN	1540-7748 ; 0022-1295
ISSN (online)	1540-7748
ISSN	0022-1295
DOI	10.1085/jgp.201010407
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Article ; Online: Molecular Structure of the Human CFTR Ion Channel.

Liu, Fangyu / Zhang, Zhe / Csanády, László / Gadsby, David C / Chen, Jue

Cell

2017 Volume 169, Issue 1, Page(s) 85–95.e8

Abstract: The cystic fibrosis transmembrane conductance regulator (CFTR) is an ATP-binding cassette (ABC) transporter that uniquely functions as an ion channel. Here, we present a 3.9 Å structure of dephosphorylated human CFTR without nucleotides, determined by ... ...

Abstract	The cystic fibrosis transmembrane conductance regulator (CFTR) is an ATP-binding cassette (ABC) transporter that uniquely functions as an ion channel. Here, we present a 3.9 Å structure of dephosphorylated human CFTR without nucleotides, determined by electron cryomicroscopy (cryo-EM). Close resemblance of this human CFTR structure to zebrafish CFTR under identical conditions reinforces its relevance for understanding CFTR function. The human CFTR structure reveals a previously unresolved helix belonging to the R domain docked inside the intracellular vestibule, precluding channel opening. By analyzing the sigmoid time course of CFTR current activation, we propose that PKA phosphorylation of the R domain is enabled by its infrequent spontaneous disengagement, which also explains residual ATPase and gating activity of dephosphorylated CFTR. From comparison with MRP1, a feature distinguishing CFTR from all other ABC transporters is the helix-loop transition in transmembrane helix 8, which likely forms the structural basis for CFTR's channel function.
MeSH term(s)	ATP-Binding Cassette Transporters/chemistry ; Adenosine Triphosphate/metabolism ; Animals ; Cattle ; Cryoelectron Microscopy ; Cystic Fibrosis Transmembrane Conductance Regulator/chemistry ; Humans ; Hydrolysis ; Models, Molecular ; Protein Domains ; Xenopus laevis ; Zebrafish ; Zebrafish Proteins/chemistry
Chemical Substances	ATP-Binding Cassette Transporters ; CFTR protein, human ; CFTR protein, zebrafish ; Zebrafish Proteins ; Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6) ; Adenosine Triphosphate (8L70Q75FXE)
Language	English
Publishing date	2017-03-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2017.02.024
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Article ; Online: Ion permeation through the Na+,K+-ATPase.

Reyes, Nicolás / Gadsby, David C

Nature

2006 Volume 443, Issue 7110, Page(s) 470–474

Abstract: P-type ATPase pumps generate concentration gradients of cations across membranes in nearly all cells. They provide a polar transmembrane pathway, to which access is strictly controlled by coupled gates that are constrained to open alternately, thereby ... ...

Abstract	P-type ATPase pumps generate concentration gradients of cations across membranes in nearly all cells. They provide a polar transmembrane pathway, to which access is strictly controlled by coupled gates that are constrained to open alternately, thereby enabling thermodynamically uphill ion transport (for example, see ref. 1). Here we examine the ion pathway through the Na+,K+-ATPase, a representative P-type pump, after uncoupling its extra- and intracellular gates with the marine toxin palytoxin. We use small hydrophilic thiol-specific reagents as extracellular probes and we monitor their reactions, and the consequences, with cysteine residues introduced along the anticipated cation pathway through the pump. The distinct effects of differently charged reagents indicate that a wide outer vestibule penetrates deep into the Na+,K+-ATPase, where the pathway narrows and leads to a charge-selectivity filter. Acidic residues in this region, which are conserved to coordinate pumped ions, allow the approach of cations but exclude anions. Reversing the charge at just one of those positions converts the pathway from cation selective to anion selective. Close structural homology among the catalytic subunits of Ca2+-, Na+,K+- and H+,K+-ATPases argues that their extracytosolic cation exchange pathways all share these physical characteristics.
MeSH term(s)	Acrylamides/pharmacology ; Animals ; Cations, Monovalent/metabolism ; Ion Transport/drug effects ; Models, Molecular ; Potassium/metabolism ; Protein Structure, Tertiary ; Sodium/metabolism ; Sodium-Potassium-Exchanging ATPase/chemistry ; Sodium-Potassium-Exchanging ATPase/genetics ; Sodium-Potassium-Exchanging ATPase/metabolism ; Static Electricity ; Substrate Specificity ; Xenopus
Chemical Substances	Acrylamides ; Cations, Monovalent ; Sodium (9NEZ333N27) ; Sodium-Potassium-Exchanging ATPase (EC 3.6.3.9) ; palytoxin (OQ17NC0MOV) ; Potassium (RWP5GA015D)
Language	English
Publishing date	2006-09-28
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/nature05129
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Article: Ouabain affinity determining residues lie close to the Na/K pump ion pathway.

Artigas, Pablo / Gadsby, David C

Proceedings of the National Academy of Sciences of the United States of America

2006 Volume 103, Issue 33, Page(s) 12613–12618

Abstract: The Na/K pump establishes essential ion concentration gradients across animal cell membranes. Cardiotonic steroids, such as ouabain, are specific inhibitors of the Na/K pump. We exploited the marine toxin, palytoxin, to probe both the ion translocation ... ...

Abstract	The Na/K pump establishes essential ion concentration gradients across animal cell membranes. Cardiotonic steroids, such as ouabain, are specific inhibitors of the Na/K pump. We exploited the marine toxin, palytoxin, to probe both the ion translocation pathway through the Na/K pump and the site of its interaction with ouabain. Palytoxin uncouples the pump's gates, which normally open strictly alternately, thus allowing both gates to sometimes be open, so transforming the pump into an ion channel. Palytoxin therefore permits electrophysiological analysis of even a single Na/K pump. We used outside-out patch recording of Xenopus alpha1beta3 Na/K pumps, which were made ouabain-resistant by point mutation, after expressing them in Xenopus oocytes. Endogenous, ouabain-sensitive, Xenopus alpha1beta3 Na/K pumps were silenced by continuous exposure to ouabain. We found that side-chain charge of two residues at either end of the alpha subunit's first extracellular loop, known to make a major contribution to ouabain affinity, strongly influenced conductance of single palytoxin-bound pump-channels by an electrostatic mechanism. The effects were mimicked by modification of cysteines introduced at those two positions with variously charged methanethiosulfonate reagents. The consequences of these modifications demonstrate that both residues lie in a wide vestibule near the mouth of the pump's ion pathway. Bound ouabain protects the site with the strongest influence on conductance from methanethiosulfonate modification, while leaving the site with the weaker influence unprotected. The results suggest a method for mapping the footprint of bound cardiotonic steroid on the extracellular surface of the Na/K pump.
MeSH term(s)	Acrylamides/metabolism ; Amino Acid Sequence ; Animals ; Cnidarian Venoms/metabolism ; Enzyme Inhibitors/metabolism ; Ions/metabolism ; Isoenzymes/chemistry ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Models, Molecular ; Molecular Sequence Data ; Ouabain/metabolism ; Patch-Clamp Techniques ; Point Mutation ; Protein Structure, Secondary ; Protein Subunits/chemistry ; Protein Subunits/genetics ; Protein Subunits/metabolism ; Sequence Alignment ; Sodium-Potassium-Exchanging ATPase/chemistry ; Sodium-Potassium-Exchanging ATPase/genetics ; Sodium-Potassium-Exchanging ATPase/metabolism ; Xenopus laevis
Chemical Substances	Acrylamides ; Cnidarian Venoms ; Enzyme Inhibitors ; Ions ; Isoenzymes ; Protein Subunits ; Ouabain (5ACL011P69) ; Sodium-Potassium-Exchanging ATPase (EC 7.2.2.13) ; palytoxin (OQ17NC0MOV)
Language	English
Publishing date	2006-08-07
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.0602720103
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In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito