WordNet

operating or moving or allowing movement in one direction only; "a unidirectional flow"; "a unidirectional antenna"; "a unidirectional approach to a problem"
moving or permitting movement in one direction only; "one-way streets"; "a one-way ticket"

PrepTutorEJDIC

一方だけに作用する,一定方向の
一方向だけの / 《米》(切符の)片道の / (話など)一方的な

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. 肩関節多方向不安定症 multidirectional instability of the shoulder
2. 不整脈のリエントリーおよび発現 reentry and the development of cardiac arrhythmias
3. 心房内リエントリ性頻拍 intraatrial reentrant tachycardia
4. 分子遺伝学の原理 principles of molecular genetics
5. 洞房結節の一時停止、停止、および進出ブロック sinoatrial nodal pause arrest and exit block

English Journal

Rotary catalysis of the stator ring of F(1)-ATPase.

Iino R, Noji H.AbstractF(1)-ATPase is a rotary motor protein in which 3 catalytic β-subunits in a stator α(3)β(3) ring undergo unidirectional and cooperative conformational changes to rotate the rotor γ-subunit upon adenosine triphosphate hydrolysis. The prevailing view of the mechanism behind this rotary catalysis elevated the γ-subunit as a "dictator" completely controlling the chemical and conformational states of the 3 catalytic β-subunits. However, our recent observations using high-speed atomic force microscopy clearly revealed that the 3 β-subunits undergo cyclic conformational changes even in the absence of the rotor γ-subunit, thus dethroning it from its dictatorial position. Here, we introduce our results in detail and discuss the possible operating principle behind the F(1)-ATPase, along with structurally related hexameric ATPases, also mentioning the possibility of generating hybrid nanomotors. This article is part of a Special Issue entitled: 17th European Bioenergetics Conference (EBEC 2012).
Biochimica et biophysica acta.Biochim Biophys Acta.2012 Oct;1817(10):1732-9. Epub 2012 Mar 16.
F(1)-ATPase is a rotary motor protein in which 3 catalytic β-subunits in a stator α(3)β(3) ring undergo unidirectional and cooperative conformational changes to rotate the rotor γ-subunit upon adenosine triphosphate hydrolysis. The prevailing view of the mechanism behind this rotary catalysis el
PMID 22465022

The inhibitory effects of vinylphosphonate-linked thymidine dimers on the unidirectional translocation of PcrA helicase along DNA: a molecular modelling study.

Wang H, Laughton CA.SourceDepartment of Medicinal Chemistry, School of Pharmacy, Ningxia Medical University, 1160 Shengli Street, Yinchuan, Ningxia 750004, P. R. China. paxhw@yahoo.co.uk.
Physical chemistry chemical physics : PCCP.Phys Chem Chem Phys.2012 Sep 21;14(35):12230-7. Epub 2012 Aug 6.
The PcrA DNA helicases are important bacterial enzymes and quintessential examples of molecular motors. Through conformational changes caused by ATP hydrolysis, they move along the template double helix, breaking the hydrogen bonds holding the two strands together, and separating the template chains
PMID 22864246

Functional reconstitution and characterization of the Arabidopsis Mg(2+) transporter AtMRS2-10 in proteoliposomes.

Ishijima S, Shigemi Z, Adachi H, Makinouchi N, Sagami I.AbstractMagnesium (Mg(2+)) plays critical role in many physiological processes. The mechanism of Mg(2+) transport has been well documented in bacteria; however, less is known about Mg(2+) transporters in eukaryotes. The AtMRS2 family, which consists of 10 Arabidopsis genes, belongs to a eukaryotic subset of the CorA superfamily proteins. Proteins in this superfamily have been identified by a universally conserved GlyMetAsn motif and have been characterized as Mg(2+) transporters. Some members of the AtMRS2 family, including AtMRS2-10, may complement bacterial mutants or yeast mutants that lack Mg(2+) transport capabilities. Here, we report the purification and functional reconstitution of AtMRS2-10 into liposomes. AtMRS2-10, which contains an N-terminal His-tag, was expressed in Escherichia coli and solubilized with sarcosyl. The purified AtMRS2-10 protein was reconstituted into liposomes. AtMRS2-10 was inserted into liposomes in a unidirectional orientation. Direct measurement of Mg(2+) uptake into proteoliposomes revealed that reconstituted AtMRS2-10 transported Mg(2+) without any accessory proteins. Mutation in the GMN motif, M400 to I, inactivated Mg(2+) uptake. The AtMRS2-10-mediated Mg(2+) influx was blocked by Co(III)hexamine, and was independent of the external pH from 5 to 9. The activity of AtMRS2-10 was inhibited by Co(2+) and Ni(2+); however, it was not inhibited by Ca(2+), Fe(2+), or Fe(3+). While these results indicate that AtMRS2-10 has similar properties to the bacterial CorA proteins, unlike bacterial CorA proteins, AtMRS2-10 was potently inhibited by Al(3+). These studies demonstrate the functional capability of the AtMRS2 proteins in proteoliposomes to study structure-function relationships.
Biochimica et biophysica acta.Biochim Biophys Acta.2012 Sep;1818(9):2202-8. Epub 2012 Apr 26.
Magnesium (Mg(2+)) plays critical role in many physiological processes. The mechanism of Mg(2+) transport has been well documented in bacteria; however, less is known about Mg(2+) transporters in eukaryotes. The AtMRS2 family, which consists of 10 Arabidopsis genes, belongs to a eukaryotic subset of
PMID 22560897