Log in

Relevant bibliographies by topics / C-type inactivation / Journal articles

To see the other types of publications on this topic, follow the link: C-type inactivation.

Journal articles on the topic 'C-type inactivation'

Author: Grafiati

Published: 14 March 2023

Last updated: 31 July 2025

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'C-type inactivation.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Yan, Jiusheng, Qin Li, and Richard W. Aldrich. "Closed state-coupled C-type inactivation in BK channels." Proceedings of the National Academy of Sciences 113, no. 25 (2016): 6991–96. http://dx.doi.org/10.1073/pnas.1607584113.

Full text

Abstract:

Ion channels regulate ion flow by opening and closing their pore gates. K+ channels commonly possess two pore gates, one at the intracellular end for fast channel activation/deactivation and the other at the selectivity filter for slow C-type inactivation/recovery. The large-conductance calcium-activated potassium (BK) channel lacks a classic intracellular bundle-crossing activation gate and normally show no C-type inactivation. We hypothesized that the BK channel’s activation gate may spatially overlap or coexist with the C-type inactivation gate at or near the selectivity filter. We induced

APA, Harvard, Vancouver, ISO, and other styles

2

Li, Xiaoyan, Glenna C. L. Bett, Xuejun Jiang, Vladimir E. Bondarenko, Michael J. Morales, and Randall L. Rasmusson. "Regulation of N- and C-type inactivation of Kv1.4 by pHo and K+: evidence for transmembrane communication." American Journal of Physiology-Heart and Circulatory Physiology 284, no. 1 (2003): H71—H80. http://dx.doi.org/10.1152/ajpheart.00392.2002.

Full text

Abstract:

Kv1.4 encodes a slowly recovering transient outward current ( I to), which inactivates by a fast N-type (intracellular ball and chain) mechanism but has slow recovery due to C-type inactivation. C-type inactivation of the NH2-terminal deletion mutant (fKv1.4ΔN) was inhibited by 98 mM extracellular K+concentration ([K+]o), whereas N-type was unaffected. In 98 mM [K+]o, removal of intracellular K+ concentration ([K+]i) speeded C-type inactivation but had no effect on N-type inactivation, suggesting that C-type inactivation is sensitive to K+ binding to intracellular sites. C-type inactivation is

APA, Harvard, Vancouver, ISO, and other styles

3

Villalba-Galea, Carlos A., Takeharu Kawano, and Diomedes E. Logothetis. "C-Type Inactivation in KV2.1 Channels." Biophysical Journal 116, no. 3 (2019): 15a. http://dx.doi.org/10.1016/j.bpj.2018.11.122.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Kurata, Harley T., Zhuren Wang, and David Fedida. "NH2-terminal Inactivation Peptide Binding to C-type–inactivated Kv Channels." Journal of General Physiology 123, no. 5 (2004): 505–20. http://dx.doi.org/10.1085/jgp.200308956.

Full text

Abstract:

In many voltage-gated K+ channels, N-type inactivation significantly accelerates the onset of C-type inactivation, but effects on recovery from inactivation are small or absent. We have exploited the Na+ permeability of C-type–inactivated K+ channels to characterize a strong interaction between the inactivation peptide of Kv1.4 and the C-type–inactivated state of Kv1.4 and Kv1.5. The presence of the Kv1.4 inactivation peptide results in a slower decay of the Na+ tail currents normally observed through C-type–inactivated channels, an effective blockade of the peak Na+ tail current, and also a d

APA, Harvard, Vancouver, ISO, and other styles

5

Claydon, T. W., M. R. Boyett, A. Sivaprasadarao, and C. H. Orchard. "Two pore residues mediate acidosis-induced enhancement of C-type inactivation of the Kv1.4 K+ channel." American Journal of Physiology-Cell Physiology 283, no. 4 (2002): C1114—C1121. http://dx.doi.org/10.1152/ajpcell.00542.2001.

Full text

Abstract:

Acidosis inhibits current through the Kv1.4 K+ channel, perhaps as a result of enhancement of C-type inactivation. The mechanism of action of acidosis on C-type inactivation has been studied. A mutant Kv1.4 channel that lacks N-type inactivation (fKv1.4 Δ2–146) was expressed in Xenopus oocytes, and currents were recorded using two-microelectrode voltage clamp. Acidosis increased fKv1.4 Δ2–146 C-type inactivation. Replacement of a pore histidine with cysteine (H508C) abolished the increase. Application of positively charged thiol-specific methanethiosulfonate to fKv1.4 Δ2–146 H508C increased C-

APA, Harvard, Vancouver, ISO, and other styles

6

Trefilov, B. B., N. V. Nikitina, and I. K. Leonov. "THE KINETICS OF THE INACTIVATION OF THE HEPATITIS VIRUS TYPE I (AVIHEPATOVIRUS, PICORNAVIRIDAE)." Problems of Virology, Russian journal 63, no. 3 (2018): 135–38. http://dx.doi.org/10.18821/0507-4088-2018-63-3-135-138.

Full text

Abstract:

Experimental data on the kinetics of the inactivation of the vaccine strain of the duckling hepatitis virus of the type I with increased temperature and aminoethyl ethylenimine are presented. It was shown that the vaccine strain 3M-UNIIP of the hepatitis virus of ducklings of type I was comparatively thermostable at 56°C and sensitive to the action of aminoethyl ethylenimine; the time of complete inactivation of the virus at a final concentration of 0.1% at 37°C was 24 h. The obtained results suggest that aminoethyl ethylenimine can be used as an inactivator in manufacturing inactivated vaccin

APA, Harvard, Vancouver, ISO, and other styles

7

Mathes, Chris, Joshua J. C. Rosenthal, Clay M. Armstrong, and William F. Gilly. "Fast Inactivation of Delayed Rectifier K Conductance in Squid Giant Axon and Its Cell Bodies." Journal of General Physiology 109, no. 4 (1997): 435–48. http://dx.doi.org/10.1085/jgp.109.4.435.

Full text

Abstract:

Inactivation of delayed rectifier K conductance (gK) was studied in squid giant axons and in the somata of giant fiber lobe (GFL) neurons. Axon measurements were made with an axial wire voltage clamp by pulsing to VK (∼−10 mV in 50–70 mM external K) for a variable time and then assaying available gK with a strong, brief test pulse. GFL cells were studied with whole-cell patch clamp using the same prepulse procedure as well as with long depolarizations. Under our experimental conditions (12–18°C, 4 mM internal MgATP) a large fraction of gK inactivates within 250 ms at −10 mV in both cell bodies

APA, Harvard, Vancouver, ISO, and other styles

8

Ogielska, Eva M., and Richard W. Aldrich. "Functional Consequences of a Decreased Potassium Affinity in a Potassium Channel Pore." Journal of General Physiology 113, no. 2 (1999): 347–58. http://dx.doi.org/10.1085/jgp.113.2.347.

Full text

Abstract:

Ions bound near the external mouth of the potassium channel pore impede the C-type inactivation conformational change (Lopez-Barneo, J., T. Hoshi, S. Heinemann, and R. Aldrich. 1993. Receptors Channels. 1:61– 71; Baukrowitz, T., and G. Yellen. 1995. Neuron. 15:951–960). In this study, we present evidence that the occupancy of the C-type inactivation modulatory site by permeant ions is not solely dependent on its intrinsic affinity, but is also a function of the relative affinities of the neighboring sites in the potassium channel pore. The A463C mutation in the S6 region of Shaker decreases th

APA, Harvard, Vancouver, ISO, and other styles

9

Starkus, John G., Lioba Kuschel, Martin D. Rayner, and Stefan H. Heinemann. "Ion Conduction through C-Type Inactivated Shaker Channels." Journal of General Physiology 110, no. 5 (1997): 539–50. http://dx.doi.org/10.1085/jgp.110.5.539.

Full text

Abstract:

C-type inactivation of Shaker potassium channels involves entry into a state (or states) in which the inactivated channels appear nonconducting in physiological solutions. However, when Shaker channels, from which fast N-type inactivation has been removed by NH2-terminal deletions, are expressed in Xenopus oocytes and evaluated in inside-out patches, complete removal of K+ ions from the internal solution exposes conduction of Na+ and Li+ in C-type inactivated conformational states. The present paper uses this observation to investigate the properties of ion conduction through C-type inactivate

APA, Harvard, Vancouver, ISO, and other styles

10

Biagi, B. A., and J. J. Enyeart. "Multiple calcium currents in a thyroid C-cell line: biophysical properties and pharmacology." American Journal of Physiology-Cell Physiology 260, no. 6 (1991): C1253—C1263. http://dx.doi.org/10.1152/ajpcell.1991.260.6.c1253.

Full text

Abstract:

The whole cell version of the patch-clamp technique was used to characterize voltage-gated Ca2+ channels in the calcitonin-secreting rat thyroid C-cell line 6-23 (clone 6). Three types of Ca2+ channels could be distinguished based on differences in voltage dependence, kinetics, and pharmacological sensitivity. T-type current was half-maximal at -31 mV, showed steady-state voltage-dependent inactivation that was half-maximal at -57 mV, inactivated with a voltage-dependent time constant that reached a minimum of 20 ms at potentials positive to -20 mV, and deactivated with a single time constant

APA, Harvard, Vancouver, ISO, and other styles

11

Farag, N. E., D. Jeong, T. Claydon, J. Warwicker, and M. R. Boyett. "Polyunsaturated fatty acids inhibit Kv1.4 by interacting with positively charged extracellular pore residues." American Journal of Physiology-Cell Physiology 311, no. 2 (2016): C255—C268. http://dx.doi.org/10.1152/ajpcell.00277.2015.

Full text

Abstract:

Polyunsaturated fatty acids (PUFAs) modulate voltage-gated K+ channel inactivation by an unknown site and mechanism. The effects of ω-6 and ω-3 PUFAs were investigated on the heterologously expressed Kv1.4 channel. PUFAs inhibited wild-type Kv1.4 during repetitive pulsing as a result of slowing of recovery from inactivation. In a mutant Kv1.4 channel lacking N-type inactivation, PUFAs reversibly enhanced C-type inactivation ( Kd, 15–43 μM). C-type inactivation was affected by extracellular H+ and K+ as well as PUFAs and there was an interaction among the three: the effect of PUFAs was reversed

APA, Harvard, Vancouver, ISO, and other styles

12

Lipinsky, Maya, William Sam Tobelaim, Asher Peretz, et al. "A unique mechanism of inactivation gating of the Kv channel family member Kv7.1 and its modulation by PIP2 and calmodulin." Science Advances 6, no. 51 (2020): eabd6922. http://dx.doi.org/10.1126/sciadv.abd6922.

Full text

Abstract:

Inactivation of voltage-gated K+ (Kv) channels mostly occurs by fast N-type or/and slow C-type mechanisms. Here, we characterized a unique mechanism of inactivation gating comprising two inactivation states in a member of the Kv channel superfamily, Kv7.1. Removal of external Ca2+ in wild-type Kv7.1 channels produced a large, voltage-dependent inactivation, which differed from N- or C-type mechanisms. Glu295 and Asp317 located, respectively, in the turret and pore entrance are involved in Ca2+ coordination, allowing Asp317 to form H-bonding with the pore helix Trp304, which stabilizes the sele

APA, Harvard, Vancouver, ISO, and other styles

13

Nuanualsuwan, Suphachai, and Dean O. Cliver. "Infectivity of RNA from Inactivated Poliovirus." Applied and Environmental Microbiology 69, no. 3 (2003): 1629–32. http://dx.doi.org/10.1128/aem.69.3.1629-1632.2003.

Full text

Abstract:

ABSTRACT During inactivation of poliovirus type 1 (PV-1) by exposure to UV, hypochlorite, and heat (72°C), the infectivity of the virus was compared with that of its RNA. DEAE-dextran (1-mg/ml concentration in Dulbecco's modified Eagle medium buffered with 0.05 M Tris, pH 7.4) was used to facilitate transfecting PV-1 RNA into FRhK-4 host cells. After interaction of PV-1 RNA with cell monolayer at room temperature (21 to 22°C) for 20 min, the monolayers were washed with 5 ml of Hanks balanced salt solution. The remainder of the procedure was the same as that for the conventional plaque techniqu

APA, Harvard, Vancouver, ISO, and other styles

14

Armstrong, Clay M., and Toshinori Hoshi. "K+ channel gating: C-type inactivation is enhanced by calcium or lanthanum outside." Journal of General Physiology 144, no. 3 (2014): 221–30. http://dx.doi.org/10.1085/jgp.201411223.

Full text

Abstract:

Many voltage-gated K+ channels exhibit C-type inactivation. This typically slow process has been hypothesized to result from dilation of the outer-most ring of the carbonyls in the selectivity filter, destroying this ring’s ability to bind K+ with high affinity. We report here strong enhancement of C-type inactivation upon extracellular addition of 10–40 mM Ca2+ or 5–50 µM La3+. These multivalent cations mildly increase the rate of C-type inactivation during depolarization and markedly promote inactivation and/or suppress recovery when membrane voltage (Vm) is at resting levels (−80 to −100 mV

APA, Harvard, Vancouver, ISO, and other styles

15

CALUGARU, Sergei V., Srinivasan KRISHNAN, Calvin J. CHANY, Barry G. HALL та Michael L. SINNOTT. "Larger increases in sensitivity to paracatalytic inactivation than in catalytic competence during experimental evolution of the second β-galactosidase of Escherichia coli". Biochemical Journal 325, № 1 (1997): 117–21. http://dx.doi.org/10.1042/bj3250117.

Full text

Abstract:

Second-order rate constants (M-1·s-1) at 25 °C and pH 7.5 for inactivation of first-generation (ebga and ebgb), second-generation(ebgab and ebgabcd) and third-generation (ebgabcde) experimental evolvants of the title enzyme by 2′,4′-dinitrophenyl 2-deoxy-2-fluoro-β-d-galactopyranoside are 0.042, 0.30, 10, 24 and 57 respectively. Only partial inactivation is observed, except forebgabcde. At a single high inactivator concentration, inactivation of the wild-type ebgo is also seen. The changes in sensitivity to the paracatalytic inactivator (over a range of 103.3) are larger than changes in kcat/K

APA, Harvard, Vancouver, ISO, and other styles

16

Kurata, Harley T., Gordon S. Soon, and David Fedida. "Altered State Dependence of C-Type Inactivation in the Long and Short Forms of Human Kv1.5." Journal of General Physiology 118, no. 3 (2001): 315–32. http://dx.doi.org/10.1085/jgp.118.3.315.

Full text

Abstract:

Evidence from both human and murine cardiomyocytes suggests that truncated isoforms of Kv1.5 can be expressed in vivo. Using whole-cell patch-clamp recordings, we have characterized the activation and inactivation properties of Kv1.5ΔN209, a naturally occurring short form of human Kv1.5 that lacks roughly 75% of the T1 domain. When expressed in HEK 293 cells, this truncated channel exhibited a V1/2 of −19.5 ± 0.9 mV for activation and −35.7 ± 0.7 mV for inactivation, compared with a V1/2 of −11.2 ± 0.3 mV for activation and −0.9 ± 1.6 mV for inactivation in full-length Kv.15. Kv1.5ΔN209 channe

APA, Harvard, Vancouver, ISO, and other styles

17

Shimizu, H., K. Yamada, and S. Oiki. "An ion binding site competing with C-type inactivation." Seibutsu Butsuri 41, supplement (2001): S214. http://dx.doi.org/10.2142/biophys.41.s214_1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Cuello, Luis G., Vishwanath Jogini, D. Marien Cortes, and Eduardo Perozo. "Structural mechanism of C-type inactivation in K+ channels." Nature 466, no. 7303 (2010): 203–8. http://dx.doi.org/10.1038/nature09153.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Hoshi, Toshinori, Wonpil Im, and Clay M. Armstrong. "Pore Dilation in C-Type Inactivation of Potassium Channels." Biophysical Journal 98, no. 3 (2010): 522a. http://dx.doi.org/10.1016/j.bpj.2009.12.2836.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Yan, Jiusheng, Wei Wang, and Richard W. Aldrich. "Closed State Coupled C-Type Inactivation in BK Channels." Biophysical Journal 106, no. 2 (2014): 642a. http://dx.doi.org/10.1016/j.bpj.2013.11.3554.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

González-Pérez, Vivian, Alan Neely, Christian Tapia, et al. "Slow Inactivation in Shaker K Channels Is Delayed by Intracellular Tetraethylammonium." Journal of General Physiology 132, no. 6 (2008): 633–50. http://dx.doi.org/10.1085/jgp.200810057.

Full text

Abstract:

After removal of the fast N-type inactivation gate, voltage-sensitive Shaker (Shaker IR) K channels are still able to inactivate, albeit slowly, upon sustained depolarization. The classical mechanism proposed for the slow inactivation observed in cell-free membrane patches—the so called C inactivation—is a constriction of the external mouth of the channel pore that prevents K+ ion conduction. This constriction is antagonized by the external application of the pore blocker tetraethylammonium (TEA). In contrast to C inactivation, here we show that, when recorded in whole Xenopus oocytes, slow in

APA, Harvard, Vancouver, ISO, and other styles

22

Wang, Jinling, Matthew C. Trudeau, Angelina M. Zappia, and Gail A. Robertson. "Regulation of Deactivation by an Amino Terminal Domain in Human Ether-à-go-go –related Gene Potassium Channels." Journal of General Physiology 112, no. 5 (1998): 637–47. http://dx.doi.org/10.1085/jgp.112.5.637.

Full text

Abstract:

Abnormalities in repolarization of the cardiac ventricular action potential can lead to life-threatening arrhythmias associated with long QT syndrome. The repolarization process depends upon the gating properties of potassium channels encoded by the human ether-à-go-go–related gene (HERG), especially those governing the rate of recovery from inactivation and the rate of deactivation. Previous studies have demonstrated that deletion of the NH2 terminus increases the deactivation rate, but the mechanism by which the NH2 terminus regulates deactivation in wild-type channels has not been elucidate

APA, Harvard, Vancouver, ISO, and other styles

23

CREST, M., E. EHILE, T. PIN, K. WATANABE, and M. GOLA. "Plateau-Generating Nerve Cells in Helix: Properties of the Repolarizing Voltage-Gated and Ca2+-Activated Potassium Currents." Journal of Experimental Biology 152, no. 1 (1990): 211–41. http://dx.doi.org/10.1242/jeb.152.1.211.

Full text

Abstract:

The aim of this study was to identify and characterize the repolarizing currents present in Helix nerve cells that generate long-lasting Ca2+-dependent depolarized plateaus in response to low-frequency stimulation. Two K+ currents were identified: a voltage-gated K(V) current and a Ca2+-activated K+ current or C current. These currents were studied separately in cells injected with either EGTA, tetraethylammonium (TEA+) or Cs+. C current activation was found to be rate-limited by the size of the inward Ca2+ current. Both K(V) and C currents displayed a pronounced relaxation during sustained de

APA, Harvard, Vancouver, ISO, and other styles

24

Decrey, Loïc, Shinobu Kazama, and Tamar Kohn. "Ammonia as anIn SituSanitizer: Influence of Virus Genome Type on Inactivation." Applied and Environmental Microbiology 82, no. 16 (2016): 4909–20. http://dx.doi.org/10.1128/aem.01106-16.

Full text

Abstract:

ABSTRACTTreatment of human excreta and animal manure (HEAM) is key in controlling the spread of persistent enteric pathogens, such as viruses. The extent of virus inactivation during HEAM storage and treatment appears to vary with virus genome type, although the reasons for this variability are not clear. Here, we investigated the inactivation of viruses of different genome types under conditions representative of HEAM storage or mesophilic digestion. The goals were to characterize the influence of HEAM solution conditions on inactivation and to determine the potential mechanisms involved. Spe

APA, Harvard, Vancouver, ISO, and other styles

25

YELLEN, GARY. "The moving parts of voltage-gated ion channels." Quarterly Reviews of Biophysics 31, no. 3 (1998): 239–95. http://dx.doi.org/10.1017/s0033583598003448.

Full text

Abstract:

Ion channels, like many other proteins, have moving parts that perform useful functions. The channel proteins contain an aqueous, ion-selective pore that crosses the plasma membrane, and they use a number of distinct ‘gating’ mechanisms to open and close this pore in response to biological stimuli such as the binding of a ligand or a change in the transmembrane voltage.This review is written at a watershed in our understanding of ion channels.1. INTRODUCTION 2401.1 Basic structure of voltage-activated channels 2411.2 What are the physical motions of the channel protein during gating? 2431.3 Ga

APA, Harvard, Vancouver, ISO, and other styles

26

Li, Jing, Jared Ostmeyer, Luis G. Cuello, Eduardo Perozo, and Benoît Roux. "Rapid constriction of the selectivity filter underlies C-type inactivation in the KcsA potassium channel." Journal of General Physiology 150, no. 10 (2018): 1408–20. http://dx.doi.org/10.1085/jgp.201812082.

Full text

Abstract:

C-type inactivation is a time-dependent process observed in many K+ channels whereby prolonged activation by an external stimulus leads to a reduction in ionic conduction. While C-type inactivation is thought to be a result of a constriction of the selectivity filter, the local dynamics of the process remain elusive. Here, we use molecular dynamics (MD) simulations of the KcsA channel to elucidate the nature of kinetically delayed activation/inactivation gating coupling. Microsecond-scale MD simulations based on the truncated form of the KcsA channel (C-terminal domain deleted) provide a first

APA, Harvard, Vancouver, ISO, and other styles

27

Starkus, John G., Lioba Kuschel, Martin D. Rayner, and Stefan H. Heinemann. "Macroscopic Na+ Currents in the “Nonconducting” Shaker Potassium Channel Mutant W434F." Journal of General Physiology 112, no. 1 (1998): 85–93. http://dx.doi.org/10.1085/jgp.112.1.85.

Full text

Abstract:

C-type inactivation in Shaker potassium channels inhibits K+ permeation. The associated structural changes appear to involve the outer region of the pore. Recently, we have shown that C-type inactivation involves a change in the selectivity of the Shaker channel, such that C-type inactivated channels show maintained voltage-sensitive activation and deactivation of Na+ and Li+ currents in K+-free solutions, although they show no measurable ionic currents in physiological solutions. In addition, it appears that the effective block of ion conduction produced by the mutation W434F in the pore regi

APA, Harvard, Vancouver, ISO, and other styles

28

Shirokov, Roman, Gonzalo Ferreira, Jianxun Yi, and Eduardo Ríos. "Inactivation of Gating Currents of L-Type Calcium Channels." Journal of General Physiology 111, no. 6 (1998): 807–23. http://dx.doi.org/10.1085/jgp.111.6.807.

Full text

Abstract:

In studies of gating currents of rabbit cardiac Ca channels expressed as α1C/β2a or α1C/β2a/α2δ subunit combinations in tsA201 cells, we found that long-lasting depolarization shifted the distribution of mobile charge to very negative potentials. The phenomenon has been termed charge interconversion in native skeletal muscle (Brum, G., and E. Ríos. 1987. J. Physiol. (Camb.). 387:489–517) and cardiac Ca channels (Shirokov, R., R. Levis, N. Shirokova, and E. Ríos. 1992. J. Gen. Physiol. 99:863–895). Charge 1 (voltage of half-maximal transfer, V1/2 ≃ 0 mV) gates noninactivated channels, while cha

APA, Harvard, Vancouver, ISO, and other styles

29

Basso, Claudia, Pedro Labarca, Enrico Stefani, Osvaldo Alvarez, and Ramon Latorre. "Pore accessibility during C-type inactivation in Shaker K+ channels." FEBS Letters 429, no. 3 (1998): 375–80. http://dx.doi.org/10.1016/s0014-5793(98)00635-8.

Full text

APA, Harvard, Vancouver, ISO, and other styles

30

Ogielska, E. M., W. N. Zagotta, T. Hoshi, S. H. Heinemann, J. Haab, and R. W. Aldrich. "Cooperative subunit interactions in C-type inactivation of K channels." Biophysical Journal 69, no. 6 (1995): 2449–57. http://dx.doi.org/10.1016/s0006-3495(95)80114-1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

31

Levy, D. I., and C. Deutsch. "Recovery from C-type inactivation is modulated by extracellular potassium." Biophysical Journal 70, no. 2 (1996): 798–805. http://dx.doi.org/10.1016/s0006-3495(96)79619-4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

32

Jamieson, Quentin, and Stephen W. Jones. "Shaker IR T449 Mutants Separate C- from U-Type Inactivation." Journal of Membrane Biology 247, no. 4 (2014): 319–30. http://dx.doi.org/10.1007/s00232-014-9634-3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Cordero-Morales, Julio F., Vishwanath Jogini, Sudha Chakrapani, and Eduardo Perozo. "A Multipoint Hydrogen-Bond Network Underlying KcsA C-Type Inactivation." Biophysical Journal 100, no. 10 (2011): 2387–93. http://dx.doi.org/10.1016/j.bpj.2011.01.073.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Armstrong, Clay M., and Toshinori Hoshi. "Enhancement of C-Type Inactivation by External Ca2+ and La3+." Biophysical Journal 106, no. 2 (2014): 537a. http://dx.doi.org/10.1016/j.bpj.2013.11.2995.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Zhang, Shetuan, Harley T. Kurata, Steven J. Kehl, and David Fedida. "Rapid Induction of P/C-type Inactivation Is the Mechanism for Acid-induced K+ Current Inhibition." Journal of General Physiology 121, no. 3 (2003): 215–25. http://dx.doi.org/10.1085/jgp.20028760.

Full text

Abstract:

Extracellular acidification is known to decrease the conductance of many voltage-gated potassium channels. In the present study, we investigated the mechanism of H+o-induced current inhibition by taking advantage of Na+ permeation through inactivated channels. In hKv1.5, H+o inhibited open-state Na+ current with a similar potency to K+ current, but had little effect on the amplitude of inactivated-state Na+ current. In support of inactivation as the mechanism for the current reduction, Na+ current through noninactivating hKv1.5-R487V channels was not affected by [H+o]. At pH 6.4, channels were

APA, Harvard, Vancouver, ISO, and other styles

36

Garg, Vivek, Frank B. Sachse, and Michael C. Sanguinetti. "Tuning of EAG K+ channel inactivation: Molecular determinants of amplification by mutations and a small molecule." Journal of General Physiology 140, no. 3 (2012): 307–24. http://dx.doi.org/10.1085/jgp.201210826.

Full text

Abstract:

Ether-à-go-go (EAG) and EAG-related gene (ERG) K+ channels are close homologues but differ markedly in their gating properties. ERG1 channels are characterized by rapid and extensive C-type inactivation, whereas mammalian EAG1 channels were previously considered noninactivating. Here, we show that human EAG1 channels exhibit an intrinsic voltage-dependent slow inactivation that is markedly enhanced in rate and extent by 1–10 µM 3-nitro-N-(4-phenoxyphenyl) benzamide, or ICA105574 (ICA). This compound was previously reported to have the opposite effect on ERG1 channels, causing an increase in cu

APA, Harvard, Vancouver, ISO, and other styles

37

Takagi, Shuichi, Yasuki Kihara, Shigetake Sasayama, and Tamotsu Mitsuiye. "Slow inactivation of cardiac L-type Ca2+ channel induced by cold acclimation of guinea pig." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 274, no. 2 (1998): R348—R356. http://dx.doi.org/10.1152/ajpregu.1998.274.2.r348.

Full text

Abstract:

Whole cell L-type Ca2+ current was recorded in ventricular myocytes dissociated from guinea pigs that were bred at ambient temperatures ranging between daily averages of 4 and 29°C. The dynamic voltage range of inactivation, as measured using 400-ms conditioning pulses and a holding potential of −40 mV, extended from −50 to −20 mV in myocytes prepared in summer. In winter, the inactivation curve was shifted to more negative potentials than in summer. Double-pulse experiments revealed that the negative shift was due to slow-inactivation kinetics. The negative shift of inactivation could be indu

APA, Harvard, Vancouver, ISO, and other styles

38

Loots, E., and E. Y. Isacoff. "Protein Rearrangements Underlying Slow Inactivation of the Shaker K+ Channel." Journal of General Physiology 112, no. 4 (1998): 377–89. http://dx.doi.org/10.1085/jgp.112.4.377.

Full text

Abstract:

Voltage-dependent ion channels transduce changes in the membrane electric field into protein rearrangements that gate their transmembrane ion permeation pathways. While certain molecular elements of the voltage sensor and gates have been identified, little is known about either the nature of their conformational rearrangements or about how the voltage sensor is coupled to the gates. We used voltage clamp fluorometry to examine the voltage sensor (S4) and pore region (P-region) protein motions that underlie the slow inactivation of the Shaker K+ channel. Fluorescent probes in both the P-region

APA, Harvard, Vancouver, ISO, and other styles

39

Sobsey, Mark D., Carla E. Oldham, and Donald E. McCall. "Comparative Inactivation of Hepatitis A Virus and Other Enteroviruses in Water by Iodine." Water Science and Technology 24, no. 2 (1991): 331–37. http://dx.doi.org/10.2166/wst.1991.0085.

Full text

Abstract:

Iodine is used as a disinfectant of small and field water supplies, but little is known about its ability to inactivate important waterborne viruses such as hepatitis A virus (HAV). In laboratory studies we determined the inactivation of purified, aggregated HAV, poliovirus type 1 and echovirus type 1 by 8 and 16 mg/l doses of iodine in both phosphate buffered, iodine demand-free (clean) water and the same water containing 10 mg/l of a 1:1 mixture of humic and fulvic acids and 5 NTU of bentonite clay turbidity (dirty water). Virus inactivation studies in clean water were done at pH 4.5, 7.0 an

APA, Harvard, Vancouver, ISO, and other styles

40

Panaghie, Gianina, Kerry Purtell, Kwok-Keung Tai, and Geoffrey W. Abbott. "Voltage-Dependent C-Type Inactivation in a Constitutively Open K+ Channel." Biophysical Journal 95, no. 6 (2008): 2759–78. http://dx.doi.org/10.1529/biophysj.108.133678.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Ghadikolaei, Azadeh Nikouee, and Stephan Grissmer. "Scorpion Toxins Modify C-Type Inactivation in a Mutant Potassium Channel." Biophysical Journal 100, no. 3 (2011): 566a. http://dx.doi.org/10.1016/j.bpj.2010.12.3285.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Pérez-Cornejo, Patricia. "H + ion modulation of C-type inactivation of Shaker K + channels." Pfl�gers Archiv European Journal of Physiology 437, no. 6 (1999): 865–70. http://dx.doi.org/10.1007/s004240050856.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Li, Jing, Jared Jostmey, Eduardo Perozo, and Benoit Roux. "A Universal Molecular Mechanism for C-type Inactivation in Potassium Channels." Biophysical Journal 114, no. 3 (2018): 474a—475a. http://dx.doi.org/10.1016/j.bpj.2017.11.2611.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Chen, Yi-Hung, King-Chuen Wu, Chin-Tsang Yang, et al. "Coumarsabin hastens C-type inactivation gating of voltage-gated K+ channels." European Journal of Pharmacology 704, no. 1-3 (2013): 41–48. http://dx.doi.org/10.1016/j.ejphar.2013.01.062.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Conti, Luca, Jakob Renhorn, Anders Gabrielsson, et al. "A Reciprocal Voltage Sensor-To-Pore Coupling in C-Type Inactivation." Biophysical Journal 110, no. 3 (2016): 104a. http://dx.doi.org/10.1016/j.bpj.2015.11.620.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Rintelen, Claudia, Subramanian Yegneswaran, and John Griffin. "Anticoagulant Dysfunction of Human Arg352Trp-Activated Protein C Caused by Defective Factor Va Inactivation." Thrombosis and Haemostasis 85, no. 02 (2001): 274–79. http://dx.doi.org/10.1055/s-0037-1615694.

Full text

Abstract:

SummaryThe dysfunctional mutant R352W-protein C was found in two patients with venous thrombosis. The mutant R352A-protein C was constructed to define the contribution of charge/size of the residue at 352 on protein C (chymotrypsin numbering 187). Compared with wild type-protein C, R352W-protein C showed no difference in activation by thrombin·thrombomodulin or α-thrombin. However, R352W-activated protein C (APC) anticoagulant activity (aPTT assay) was reduced to ~65%. Although the catalytic efficiency of R352W-APC towards the oligopeptide substrate S-2366 was unperturbed, factor Va and R506Q-

APA, Harvard, Vancouver, ISO, and other styles

47

Somodi, Sándor, Zoltán Varga, Péter Hajdu, et al. "pH-dependent modulation of Kv1.3 inactivation: role of His399." American Journal of Physiology-Cell Physiology 287, no. 4 (2004): C1067—C1076. http://dx.doi.org/10.1152/ajpcell.00438.2003.

Full text

Abstract:

The Kv1.3 K+ channel lacks N-type inactivation, but during prolonged depolarized periods it inactivates via the slow (P/C type) mechanism. It bears a titratable histidine residue in position 399 (equivalent of Shaker 449), a site known to influence the rate of slow inactivation. As opposed to several other voltage-gated K+ channels, slow inactivation of Kv1.3 is slowed when extracellular pH (pHo) is lowered under physiological conditions. Our findings are as follows. First, when His399 was mutated to a lysine, arginine, leucine, valine or tyrosine, extracellular acidification (pH 5.5) accelera

APA, Harvard, Vancouver, ISO, and other styles

48

Gomez-Lagunas, Froylan, Imilla Arias-Olguin, and Elisa Carrillo. "Shab K Channel Slow Inactivation. A Mechanism that Departs from Both C and U-Type Inactivation Mechanisms." Biophysical Journal 102, no. 3 (2012): 530a. http://dx.doi.org/10.1016/j.bpj.2011.11.2896.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

KIM, SOO-HWAN, SANG-HYUN PARK, SANG-SOON KIM, and DONG-HYUN KANG. "Inactivation of Staphylococcus aureus Biofilms on Food Contact Surfaces by Superheated Steam Treatment." Journal of Food Protection 82, no. 9 (2019): 1496–500. http://dx.doi.org/10.4315/0362-028x.jfp-18-572.

Full text

Abstract:

ABSTRACT The objective of this study was to compare the inactivation efficacy of saturated steam (SS) and superheated steam (SHS) on Staphylococcus aureus biofilms on food contact surfaces, including type 304 stainless steel coupons with No. 4 finish (STS No. 4), type 304 stainless steel coupons with 2B finish (STS 2B), high-density polyethylene (HDPE), and polypropylene (PP). In addition, the effects of the surface characteristics on the inactivation efficacy were evaluated. Biofilms were formed on each food contact coupon surface using a three-strain cocktail of S. aureus. Five-day-old biofi

APA, Harvard, Vancouver, ISO, and other styles

50

Fuchs, Beth Burgwyn, George P. Tegos, Michael R. Hamblin, and Eleftherios Mylonakis. "Susceptibility of Cryptococcus neoformans to Photodynamic Inactivation Is Associated with Cell Wall Integrity." Antimicrobial Agents and Chemotherapy 51, no. 8 (2007): 2929–36. http://dx.doi.org/10.1128/aac.00121-07.

Full text

Abstract:

ABSTRACT Photodynamic therapy is a rapidly developing antimicrobial technology which combines a nontoxic photoactivatable dye or photosensitizer with harmless visible light of the correct wavelength to excite the dye to its reactive triplet state to generate reactive oxygen species toxic to cells. In this report we present evidence that the fungal pathogen Cryptococcus neoformans is susceptible to photodynamic inactivation by use of a polycationic conjugate of polyethyleneimine and the photosensitizer chlorin(e6). A C. neoformans rom2 mutant, with a mutation involving a putative Rho1 guanyl nu

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!