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RISS 인기검색어
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- 저자 : Rice James M. (검색결과 2 건)
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Enhancement of the Electron Spin Resonance of Single-Walled Carbon Nanotubes by Oxygen Removal
Rice, William D.,Weber, Ralph T.,Leonard, Ashley D.,Tour, James M.,Nikolaev, Pavel,Arepalli, Sivaram,Berka, Vladimir,Tsai, Ah-Lim,Kono, Junichiro American Chemical Society 2012 ACS NANO Vol.6 No.3
<P>We have observed a nearly 4-fold increase in the electron spin resonance (ESR) signal from an ensemble of single-walled carbon nanotubes (SWCNTs) due to oxygen desorption. By performing temperature-dependent ESR spectroscopy both before and after thermal annealing, we found that the ESR in SWCNTs can be reversibly altered <I>via</I> the molecular oxygen content in the samples. Independent of the presence of adsorbed oxygen, a Curie law (spin susceptibility ∝ 1/<I>T</I>) is seen from ∼4 to 300 K, indicating that the probed spins are finite-level species. For both the pre-annealed and post-annealed sample conditions, the ESR line width decreased as the temperature was increased, a phenomenon we identify as motional narrowing. From the temperature dependence of the line width, we extracted an estimate of the intertube hopping energy; for both sample conditions, we found this hopping energy to be ∼1.2 meV. Since the spin hopping energy changes only slightly when oxygen is desorbed, we conclude that only the spin susceptibility, not spin transport, is affected by the presence of physisorbed molecular oxygen in SWCNT ensembles. Surprisingly, no line width change is observed when the amount of oxygen in the SWCNT sample is altered, contrary to other carbonaceous systems and certain 1D conducting polymers. We hypothesize that physisorbed molecular oxygen acts as an acceptor (p-type), compensating the donor-like (n-type) defects that are responsible for the ESR signal in bulk SWCNTs.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/ancac3/2012/ancac3.2012.6.issue-3/nn204094s/production/images/medium/nn-2011-04094s_0009.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/nn204094s'>ACS Electronic Supporting Info</A></P>
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Ghalali Aram,Wang Liangzhe,Stopsack Konrad H.,Rice James M.,Wu Shulin,Wu Chin-Lee,Zetter Bruce R.,Rogers Michael S. 생화학분자생물학회 2022 Experimental and molecular medicine Vol.54 No.-
The transcript encoding Antizyme Inhibitor 1 (AZIN1) is frequently edited in various cancers, and this editing is associated with enhanced tumor aggressiveness. After comparison of wild-type AZIN1 (wtAZIN1) and edited AZIN1 (edAZIN1, which contains a Ser367Gly substitution), we report differential binding of edAZIN1 to a small set of proteins; specifically, edAZIN1 binds to alpha-smooth muscle actin (ACTA2), gamma actin 1 (ACTG1), and myosin9, whereas wtAZIN1 does not. This binding enables nuclear translocation of edAZIN1. In contrast to overexpression of edAZIN1 and, to a lesser extent, (editable) wtAZIN1, overexpression of an uneditable AZIN1 allele does not promote a cellular phenotype associated with increased tumorigenicity. In patients, both editing and nuclear localization of AZIN1 are common and are associated with tumor aggressiveness, i.e., a higher Gleason score, higher genomic instability, and a shorter progression-free survival time. In conclusion, the data indicate that binding of edAZIN1 to the actin/myosin9 complex supports its nuclear translocation, leading to enhanced cellular aggressiveness, and is associated with worse prostate cancer outcomes.
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