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- 저자 : Youngsoo Jeong (검색결과 88 건)
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Jeong, Hanbin,Park, Jumi,Jun, Youngsoo,Lee, Changwook National Academy of Sciences 2017 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.114 No.45
<P>The endoplasmic reticulum (ER)-mitochondria encounter structure (ERMES) comprises mitochondrial distribution and morphology 12 (Mdm12), maintenance of mitochondrial morphology 1 (Mmm1), Mdm34, and Mdm10 and mediates physical membrane contact sites and nonvesicular lipid trafficking between the ER and mitochondria in yeast. Herein, we report two crystal structures of the synaptotagmin-like mitochondrial lipid-binding protein (SMP) domain of Mmm1 and the Mdm12-Mmm1 complex at 2.8 angstrom and 3.8 angstrom resolution, respectively. Mmm1 adopts a dimeric SMP structure augmented with two extra structural elements at the N and C termini that are involved in tight self-association and phospholipid coordination. Mmm1 binds two phospholipids inside the hydrophobic cavity, and the phosphate ion of the distal phospholipid is specifically recognized through extensive H-bonds. A positively charged concave surface on the SMP domain not only mediates ER membrane docking but also results in preferential binding to glycerophospholipids such as phosphatidylcholine (PC), phosphatidic acid (PA), phosphatidylglycerol (PG), and phosphatidylserine (PS), some of which are substrates for lipid-modifying enzymes in mitochondria. The Mdm12-Mmm1 structure reveals two Mdm12s binding to the SMP domains of the Mmm1 dimer in a pairwise head-to-tail manner. Direct association of Mmm1 and Mdm12 generates a 210-angstrom-long continuous hydrophobic tunnel that facilitates phospholipid transport. The Mdm12-Mmm1 complex binds all glycerophospholipids except for phosphatidylethanolamine (PE) in vitro.</P>
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Peptide–nanoparticle conjugates: a next generation of diagnostic and therapeutic platforms?
Jeong Woo-jin,Bu Jiyoon,Kubiatowicz Luke J.,Chen Stephanie S.,Kim YoungSoo,Hong Seungpyo 나노기술연구협의회 2018 Nano Convergence Vol.5 No.38
Peptide–nanoparticle conjugates (PNCs) have recently emerged as a versatile tool for biomedical applications. Synergism between the two promising classes of materials allows enhanced control over their biological behaviors, overcoming intrinsic limitations of the individual materials. Over the past decades, a myriad of PNCs has been developed for various applications, such as drug delivery, inhibition of pathogenic biomolecular interactions, molecular imaging, and liquid biopsy. This paper provides a comprehensive overview of existing technologies that have been recently developed in the broad field of PNCs, offering a guideline especially for investigators who are new to this field.
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Mechanistic insight into the nucleus–vacuole junction based on the Vac8p–Nvj1p crystal structure
Jeong, Hanbin,Park, Jumi,Kim, Hye-In,Lee, Miriam,Ko, Young-Joon,Lee, Sanghwa,Jun, Youngsoo,Lee, Changwook National Academy of Sciences 2017 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.114 No.23
<P>Formation of the nucleus-vacuole junction (NVJ) is mediated by direct interaction between the vacuolar protein Vac8p and the outer nuclear endoplasmic reticulum membrane protein Nvj1p. Herein we report the crystal structure of Vac8p bound to Nvj1p at 2.4-angstrom resolution. Vac8p comprises a flexibly connected N-terminal H1 helix followed by 12 armadillo repeats (ARMs) that form a right-handed superhelical structure. The extended 80-angstrom-long loop of Nvj1p specifically binds the highly conserved inner groove formed from ARM1-12 of Vac8p. Disruption of the Nvj1p-Vac8p interaction results in the loss of tight NVJs, which impairs piecemeal microautophagy of the nucleus in Saccharomyces cerevisiae. Vac8p cationic triad (Arg276, Arg317, and Arg359) motifs interacting with Nvj1p are also critical to the recognition of Atg13p, a key component of the cytoplasm-to-vacuole targeting (CVT) pathway, indicating competitive binding to Vac8p. Indeed, mutation of the cationic triad abolishes CVT of Ape1p in vivo. Combined with biochemical data, the crystal structure reveals a Vac8p homodimer formed from ARM1, and this self-association, likely regulated by the flexible H1 helix and the C terminus of Nvj1p, is critical for Vac8p cellular functions.</P>
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YOUNGSOO CHO,KYUNGMIN JEONG,SUNG-UK LEE,SEUNGHO JUNG 한국원자력학회 2008 Nuclear Engineering and Technology Vol.40 No.5
During the overhaul period of nuclear power plants in Korea, an ROV(Remotely Operated Vehicle) enters the cold-leg pipes connected with the reactor to examine the state of the thermal sleeves and their positions in the safety injection nozzles. To measure the positions of the thermal sleeves or scratches with video images recorded during the examination, timevarying camera parameters should be known, such as the focal length and principal points used for the capturing each video image. In this paper, we propose a camera calibration and measurement scheme by using a single image containing two circular grooves of a cylindrical nozzle whose radius and distance are known.
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