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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/02/20 22:26:27」(JST)

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Comparison of transport proteins

A uniporter is an integral membrane protein that is involved in facilitated diffusion. They can be either ion channels or carrier proteins.

Uniporter carrier proteins work by binding to one molecule of substrate at a time and transporting it with its concentration gradient. Uniporter channels open in response to a stimulus and allow the free flow of specific molecules. Both kinds of uniporters rely on passive transport, as they do not directly require cellular energy to function.

There are several ways in which the opening of uniporter channels may be regulated:

Voltage - Regulated by the difference in voltage across the membrane
Stress - Regulated by physical pressure on the transporter (as in the cochlea of the ear)
Ligand - Regulated by the binding of a ligand to either the intracellular or extracellular side of the cell

Uniporters are involved in many biological processes, including action potentials in neurons. Voltage-gated sodium channels are involved in the propagation of a nerve impulse across the neuron. During transmission of the signal from one neuron to the next, calcium is transported into the presynaptic neuron by voltage-gated calcium channels. Potassium leak channels, also regulated by voltage, then help to restore the resting membrane potential after impulse transmission.

In the ear, sound waves cause the stress-regulated channels in the ear to open, sending an impulse to the vestibulocochlear nerve (VIII).

References

Alberts, Bruce et al. — Essential Cell Biology, 1st edition. Garland Publishing, New York: 1998.
M. G. Wolfersberger: Uniporters, symporters and antiporters. In: The Journal of experimental biology. Band 196, November 1994, S. 5–6, ISSN 0022-0949. PMID 7823043.

English Journal

High-Hall-Mobility Al-Doped ZnO Films Having Textured Polycrystalline Structure with a Well-Defined (0001) Orientation.

Nomoto J1, Makino H2, Yamamoto T2.
Nanoscale research letters.Nanoscale Res Lett.2016 Dec;11(1):320. doi: 10.1186/s11671-016-1535-1. Epub 2016 Jun 30.
Five hundred-nanometer-thick ZnO-based textured polycrystalline films consisting of 490-nm-thick Al-doped ZnO (AZO) films deposited on 10-nm-thick Ga-doped ZnO (GZO) films exhibited a high Hall mobility (μ H) of 50.1 cm(2)/Vs with a carrier concentration (N) of 2.55 × 10(20) cm(-3). Firstly,
PMID 27365000

Single Nanoparticle Translocation Through Chemically Modified Solid Nanopore.

Tan S1, Wang L2, Liu H3, Wu H4, Liu Q5.
Nanoscale research letters.Nanoscale Res Lett.2016 Dec;11(1):50. doi: 10.1186/s11671-016-1255-6. Epub 2016 Feb 1.
The nanopore sensor as a high-throughput and low-cost technology can detect single nanoparticle in solution. In the present study, the silicon nitride nanopores were fabricated by focused Ga ion beam (FIB), and the surface was functionalized with 3-aminopropyltriethoxysilane to change its surface ch
PMID 26831688

Synthesis of Mesoporous ZnO Nanosheets via Facile Solvothermal Method as the Anode Materials for Lithium-ion Batteries.

Wang X1, Huang L2,3, Zhao Y4,5, Zhang Y6,7, Zhou G8.
Nanoscale research letters.Nanoscale Res Lett.2016 Dec;11(1):37. doi: 10.1186/s11671-016-1244-9. Epub 2016 Jan 27.
Mesoporous ZnO nanosheets are synthesized through a room temperature solvothermal method. Transmission and scanning electronic microscopy observations indicate that as-prepared ZnO hierarchical aggregates are composed and assembled by nanosheets with a length of 1-2 μm and a thickness of 10-20 nm
PMID 26815606

Japanese Journal

1 port ＆ 1 puncture法による胸腔鏡下ブラ切除術の経験

小野寺賢,野田雅史,三友英紀,前田寿美子,岡田克典,近藤丘
日本呼吸器外科学会雑誌 27(2), 187-190, 2013
近年自然気胸に対して単孔法による胸腔鏡下手術が行われている．しかし，これまでの報告例では単孔法といえども皮膚切開の延長を要しており，加えて通常の胸腔鏡下手術と同様の手技が困難であることが多いと言える．我々は皮膚切開の延長をしない通常の1 port ＆ 1 puncture法により，従来の3 port法で行う手技と同等にブラの切除，ポリグルコール酸（PGA）シートによる被覆，フィブリン糊の塗布による …
NAID 130003368762

HKT1 mediates sodium uniport in roots. Pitfalls in the expression of HKT1 in yeast

HARO R
Plant Physiol. 139, 1495-1506, 2005
NAID 80017751557

Substitutional mutations in the uncoupling protein-specific sequences of mitochondrial uncoupling protein UCP1 lead to the reduction of fatty acid-induced H^+ uniport