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Kim, Kyung Hwan,Muniyappan, Srinivasan,Oang, Key Young,Kim, Jong Goo,Nozawa, Shunsuke,Sato, Tokushi,Koshihara, Shin-ya,Henning, Robert,Kosheleva, Irina,Ki, Hosung,Kim, Youngmin,Kim, Tae Wu,Kim, Jeongh American Chemical Society 2012 JOURNAL OF THE AMERICAN CHEMICAL SOCIETY - Vol.134 No.16
<P/><P>Proteins serve as molecular machines in performing their biological functions, but the detailed structural transitions are difficult to observe in their native aqueous environments in real time. For example, despite extensive studies, the solution-phase structures of the intermediates along the allosteric pathways for the transitions between the relaxed (R) and tense (T) forms have been elusive. In this work, we employed picosecond X-ray solution scattering and novel structural analysis to track the details of the structural dynamics of wild-type homodimeric hemoglobin (HbI) from the clam <I>Scapharca inaequivalvis</I> and its F97Y mutant over a wide time range from 100 ps to 56.2 ms. From kinetic analysis of the measured time-resolved X-ray solution scattering data, we identified three structurally distinct intermediates (I<SUB>1</SUB>, I<SUB>2</SUB>, and I<SUB>3</SUB>) and their kinetic pathways common for both the wild type and the mutant. The data revealed that the singly liganded and unliganded forms of each intermediate share the same structure, providing direct evidence that the ligand photolysis of only a single subunit induces the same structural change as the complete photolysis of both subunits does. In addition, by applying novel structural analysis to the scattering data, we elucidated the detailed structural changes in the protein, including changes in the heme–heme distance, the quaternary rotation angle of subunits, and interfacial water gain/loss. The earliest, R-like I<SUB>1</SUB> intermediate is generated within 100 ps and transforms to the R-like I<SUB>2</SUB> intermediate with a time constant of 3.2 ± 0.2 ns. Subsequently, the late, T-like I<SUB>3</SUB> intermediate is formed via subunit rotation, a decrease in the heme–heme distance, and substantial gain of interfacial water and exhibits ligation-dependent formation kinetics with time constants of 730 ± 120 ns for the fully photolyzed form and 5.6 ± 0.8 μs for the partially photolyzed form. For the mutant, the overall kinetics are accelerated, and the formation of the T-like I<SUB>3</SUB> intermediate involves interfacial water loss (instead of water entry) and lacks the contraction of the heme–heme distance, thus underscoring the dramatic effect of the F97Y mutation. The ability to keep track of the detailed movements of the protein in aqueous solution in real time provides new insights into the protein structural dynamics.</P>
Characterization of the Vertical Position of the Trapped Charge in Charge-trap Flash Memory
Kim, Seunghyun,Kwon, Dae Woong,Lee, Sang-Ho,Park, Sang-Ku,Kim, Youngmin,Kim, Hyungmin,Kim, Young Goan,Cho, Seongjae,Park, Byung-Gook The Institute of Electronics and Information Engin 2017 Journal of semiconductor technology and science Vol.17 No.2
In this paper, the characterization of the vertical position of trapped charges in the charge-trap flash (CTF) memory is performed in the novel CTF memory cell with gate-all-around structure using technology computer-aided design (TCAD) simulation. In the CTF memories, injected charges are not stored in the conductive poly-crystalline silicon layer in the trapping layer such as silicon nitride. Thus, a reliable technique for exactly locating the trapped charges is required for making up an accurate macro-models for CTF memory cells. When a programming operation is performed initially, the injected charges are trapped near the interface between tunneling oxide and trapping nitride layers. However, as the program voltage gets higher and a larger threshold voltage shift is resulted, additional charges are trapped near the blocking oxide interface. Intrinsic properties of nitride including trap density and effective capture cross-sectional area substantially affect the position of charge centroid. By exactly locating the charge centroid from the charge distribution in programmed cells under various operation conditions, the relation between charge centroid and program operation condition is closely investigated.
Kim, Tae Wu,Yang, Cheolhee,Kim, Youngmin,Kim, Jong Goo,Kim, Jeongho,Jung, Yang Ouk,Jun, Sunhong,Lee, Sang Jin,Park, Sungjun,Kosheleva, Irina,Henning, Robert,van Thor, Jasper J.,Ihee, Hyotcherl The Royal Society of Chemistry 2016 Physical chemistry chemical physics Vol.18 No.13
<P>Real-time probing of structural transitions of a photoactive protein is challenging owing to the lack of a universal time-resolved technique that can probe the changes in both global conformation and light-absorbing chromophores of the protein. In this work, we combine time-resolved X-ray solution scattering (TRXSS) and transient absorption (TA) spectroscopy to investigate how the global conformational changes involved in the photoinduced signal transduction of photoactive yellow protein (PYP) is temporally and spatially related to the local structural change around the light-absorbing chromophore. In particular, we examine the role of internal proton transfer in developing a signaling state of PYP by employing its E46Q mutant (E46Q-PYP), where the internal proton transfer is inhibited by the replacement of a proton donor. The comparison of TRXSS and TA spectroscopy data directly reveals that the global conformational change of the protein, which is probed by TRXSS, is temporally delayed by tens of microseconds from the local structural change of the chromophore, which is probed by TA spectroscopy. The molecular shape of the signaling state reconstructed from the TRXSS curves directly visualizes the three-dimensional conformations of protein intermediates and reveals that the smaller structural change in E46Q-PYP than in wild-type PYP suggested by previous studies is manifested in terms of much smaller protrusion, confirming that the signaling state of E46Q-PYP is only partially developed compared with that of wildtype PYP. This finding provides direct evidence of how the environmental change in the vicinity of the chromophore alters the conformational change of the entire protein matrix.</P>
Kim, Hyeong Seok,Jang, Jin-Young,Han, Youngmin,Lee, Kyoung Bun,Joo, Ijin,Lee, Doo-Ho,Kim, Jae Ri,Kim, Hongbeom,Kwon, Wooil,Kim, Sun-Whe The Korean Surgical Society 2017 Annals of Surgical Treatment and Research(ASRT) Vol.93 No.4
<P><B>Purpose</B></P><P>Neoadjuvant treatment may provide improved survival outcomes for patients with borderline resectable pancreatic cancer (BRPC). The purpose of this study is to evaluate the clinical outcomes of neoadjuvant treatment and to identify prognostic factors.</P><P><B>Methods</B></P><P>Forty patients who met the National Comprehensive Cancer Network definition of BRPC and received neoadjuvant treatment followed by surgery between 2007 and 2015 were evaluated. Prospectively collected clinicopathological outcomes were analyzed retrospectively.</P><P><B>Results</B></P><P>The mean age was 61.7 years and the male-to-female ratio was 1.8:1. Twenty-six, 3, and 11 patients received gemcitabine-based chemotherapy, 5-fluorouracil, and FOLFIRINOX, respectively. The 2-year survival rate (2YSR) was 36.6% and the median overall survival (OS) was 20 months. Of the 40 patients, 34 patients underwent resection and the 2YSR was 41.2% while the 2YSR of patients who did not undergo resection was 16.7% (P = 0.011). The 2YSR was significantly higher in patients who had partial response compared to stable disease (60.6% <I>vs</I>. 24.3%, P = 0.038), in patients who did than did not show a CA 19-9 response after neoadjuvant treatment (40.5% <I>vs</I>. 0%, P = 0.039) and in patients who did than did not receive radiotherapy (50.8% <I>vs</I>. 25.3%, P = 0.036). Five patients had local recurrence and 17 patients had systemic recurrence with a median disease specific survival of 15 months.</P><P><B>Conclusion</B></P><P>Neoadjuvant treatment followed by resection is effective for BRPC. Pancreatectomy and neoadjuvant treatment response may affect survival. Effective systemic therapy is needed to improve long-term survival since systemic metastasis accounts for a high proportion of recurrence.</P>
Kim Sinae,Nguyen Tam T.,Taitt Afeisha S.,전현정,Park Ho-Young,Kim Sung-Han,Kim Yong-Gil,Song Eun Young,Lee Youngmin,Yum Hokee,Shin Kyeong-Cheol,Choi Yang Kyu,송창선,Yeom Su Cheong,Kim Byoungguk,Netea Mihai 대한면역학회 2021 Immune Network Vol.21 No.6
Recently, a new severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) (B.1.1.529) Omicron variant originated from South Africa in the middle of November 2021. SARS-CoV-2 is also called coronavirus disease 2019 (COVID-19) since SARS-CoV-2 is the causative agent of COVID-19. Several studies already suggested that the SARS-CoV-2 Omicron variant would be the fastest transmissible variant compared to the previous 10 SARS-CoV-2 variants of concern, interest, and alert. Few clinical studies reported the high transmissibility of the Omicron variant but there is insufficient time to perform actual experiments to prove it, since the spread is so fast. We analyzed the SARS-CoV-2 Omicron variant, which revealed a very high rate of mutation at amino acid residues that interact with angiostatin-converting enzyme 2. The mutation rate of COVID-19 is faster than what we prepared vaccine program, antibody therapy, lockdown, and quarantine against COVID-19 so far. Thus, it is necessary to find better strategies to overcome the current crisis of COVID-19 pandemic.