WordNet

resistant to destruction or fading; "fast colors"
abstaining from food (同)fasting
securely fixed in place; "the post was still firm after being hit by the car" (同)firm, immobile
firmly or closely; "held fast to the rope"; "her foot was stuck fast"; "held tight" (同)tight
(of a photographic lens or emulsion) causing a shortening of exposure time; "a fast lens"
(of surfaces) conducive to rapid speeds; "a fast road"; "grass courts are faster than clay"
(used of timepieces) indicating a time ahead of or later than the correct time; "my watch is fast"
abstain from certain foods, as for religious or medical reasons; "Catholics sometimes fast during Lent"
abstain from eating; "Before the medical exam, you must fast"
acting or moving or capable of acting or moving quickly; "fast film"; "on the fast track in school"; "set a fast pace"; "a fast car"
at a rapid tempo; "the band played a fast fox trot"
quickly or rapidly (often used as a combining form); "how fast can he get here?"; "ran as fast as he could"; "needs medical help fast"; "fast-running rivers"; "fast-breaking news"; "fast-opening (or fast-closing) shutters"
the syllable naming the fourth (subdominant) note of the diatonic scale in solmization
a trodden path (同)footpath

PrepTutorEJDIC

『速い』,急速な,すばやい,敏速な / (時計が)『進んでいる』 / 『しっかりした』,ぐらつかない / 心の変わらない,忠実な(faithful) / (色が)あせない / 《古》(女性が)身持ちの悪い;《まれに》(生活が)享楽的な / (フイルムが)高感度の,(レンズが)高速撮影用の / 『速く』;すばやく(quickly) / 『しっかりと』,固く(firmly) / 『ぐっすりと』(soundly) / どしどし,ひっきりなしに
断食(だんじき),絶食 / (宗教的行事としての)断食日,断食期間 / 断食する,絶食する / (…で)精進する《+『on』+『名』》
ファ(全音階の第4音)
道,小道(path)

UpToDate Contents

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1. 視神経膠腫 optic pathway glioma
2. Anatomy, pathophysiology, and localization of accessory pathways in the preexcitation syndrome
3. 成人患者に行う麻酔後ケアの概要 overview of post anesthetic care for adult patients
4. 小児や青年にとってのファストフード fast food for children and adolescents
5. 副伝導路が関与する房室回帰性頻拍（AVRT） atrioventricular reentrant tachycardia avrt associated with an accessory pathway

English Journal

Equilibrium thermodynamics and folding kinetics of a short, fast-folding, beta-hairpin.

Jimenez-Cruz CA1, Garcia AE.Author information 1Department of Physics, Applied Physics and Astronomy, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.AbstractEquilibrium thermodynamics of a short beta-hairpin are studied using unbiased all-atom replica exchange molecular dynamics simulations in explicit solvent. An exploratory analysis of the free energy landscape of the system is provided in terms of various structural characteristics, for both the folded and unfolded ensembles. We find that the favorable interactions between the ends introduced by the tryptophan cap, along with the flexibility of the turn region, explain the remarkable stability of the folded state. Charging of the N termini results in effective roughening of the free energy landscape and stabilization of non-native contacts. Folding-unfolding dynamics are further discussed using a set of 2413 independent molecular dynamics simulations, 2 ns to 20 ns long, at the melting temperature of the beta-hairpin. A novel method for the construction of Markov models consisting of an iterative refinement of the discretization in reduced dimensionality is presented and used to generate a detailed kinetic network of the system. The hairpin is found to fold heterogeneously on sub-microsecond timescales, with the relative position of the tryptophan side chains driving the selection of the specific pathway.
Physical chemistry chemical physics : PCCP.Phys Chem Chem Phys.2014 Apr 14;16(14):6422-9. doi: 10.1039/c3cp54336f. Epub 2014 Jan 29.
Equilibrium thermodynamics of a short beta-hairpin are studied using unbiased all-atom replica exchange molecular dynamics simulations in explicit solvent. An exploratory analysis of the free energy landscape of the system is provided in terms of various structural characteristics, for both the fold
PMID 24472872

α-Actinin-3 deficiency alters muscle adaptation in response to denervation and immobilization.

Garton FC1, Seto JT, Quinlan KG, Yang N, Houweling PJ, North KN.Author information 1The Institute for Neuroscience and Muscle Research, The Children's Hospital Westmead, Sydney, Australia.AbstractHomozygosity for a common null polymorphism (R577X) in the ACTN3 gene results in the absence of the fast fibre-specific protein, α-actinin-3 in ∼16% of humans worldwide. α-Actinin-3 deficiency is detrimental to optimal sprint performance and benefits endurance performance in elite athletes. In the general population, α-actinin-3 deficiency is associated with reduced muscle mass, strength and fast muscle fibre area, and poorer muscle function with age. The Actn3 knock-out (KO) mouse model mimics the human phenotype, with fast fibres showing a shift towards slow/oxidative metabolism without a change in myosin heavy chain (MyHC) isoform. We have recently shown that these changes are attributable to increased activity of the calcineurin-dependent signalling pathway in α-actinin-3 deficient muscle, resulting in enhanced response to exercise training. This led us to hypothesize that the Actn3 genotype influences muscle adaptation to disuse, irrespective of neural innervation. Separate cohorts of KO and wild-type mice underwent 2 weeks immobilization and 2 and 8 weeks of denervation. Absence of α-actinin-3 resulted in reduced atrophic response and altered adaptation to disuse, as measured by a change in MyHC isoform. KO mice had a lower threshold to switch from the predominantly fast to a slower muscle phenotype (in response to immobilization) and a higher threshold to switch to a faster muscle phenotype (in response to denervation). We propose that this change is mediated through baseline alterations in the calcineurin signalling pathway of Actn3 KO muscle. Our findings have important implications for understanding individual responses to muscle disuse/disease and training in the general population.
Human molecular genetics.Hum Mol Genet.2014 Apr 1;23(7):1879-93. doi: 10.1093/hmg/ddt580. Epub 2013 Nov 13.
Homozygosity for a common null polymorphism (R577X) in the ACTN3 gene results in the absence of the fast fibre-specific protein, α-actinin-3 in ∼16% of humans worldwide. α-Actinin-3 deficiency is detrimental to optimal sprint performance and benefits endurance performance in elite athletes. In t
PMID 24234654