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황종석(Jong Seok Hwang),나건연(Gun Yoen Na),정상립(Sang Lip Chung),전재복(Jae Bok Jun) 대한피부과학회 1986 대한피부과학회지 Vol.24 No.2
A 50-year-old woman with lupus erythematosus profundus of about a year's duration was reported. The patient had no history of discoid lupus erythematosus or systemic lupus erythematosus. Dermatologic examination revealed two, firm, freely movable, well demarcated, subcutaneous plaques, with mildly erythematous overlying skin, measuring 2 x 2 cm (right), 5 x 5 cm (left), was present on the both deltoid region. Histopathologically, this showed panniculitis. Diret immunofluorescence studies showed IgG and IgM deposition on the dermoepidermal junction.
Lee, Jong-Ho,Kim, Na-Hyang,Winstel, Volker,Kurokawa, Kenji,Larsen, Jesper,An, Jang-Hyun,Khan, Adnan,Seong, Min-Young,Lee, Min Ja,Andersen, Paal Skytt,Peschel, Andreas,Lee, Bok Luel American Society for Microbiology 2015 Infection and immunity Vol.83 No.11
<P>The cell envelopes of many Gram-positive bacteria contain wall teichoic acids (WTAs). <I>Staphylococcus aureus</I> WTAs are composed of ribitol phosphate (RboP) or glycerol phosphate (GroP) backbones substituted with <SMALL>d</SMALL>-alanine and <I>N</I>-acetyl-<SMALL>d</SMALL>-glucosamine (GlcNAc) or <I>N</I>-acetyl-<SMALL>d</SMALL>-galactosamine (GalNAc). Two WTA glycosyltransferases, TarM and TarS, are responsible for modifying the RboP WTA with α-GlcNAc and β-GlcNAc, respectively. We recently reported that purified human serum anti-WTA IgG specifically recognizes β-GlcNAc of the staphylococcal RboP WTA and then facilitates complement C3 deposition and opsonophagocytosis of <I>S. aureus</I> laboratory strains. This prompted us to examine whether anti-WTA IgG can induce C3 deposition on a diverse set of clinical <I>S. aureus</I> isolates. To this end, we compared anti-WTA IgG-mediated C3 deposition and opsonophagocytosis abilities using 13 different staphylococcal strains. Of note, the majority of <I>S. aureus</I> strains tested was recognized by anti-WTA IgG, resulting in C3 deposition and opsonophagocytosis. A minority of strains was not recognized by anti-WTA IgG, which correlated with either extensive capsule production or an alteration in the WTA glycosylation pattern. Our results demonstrate that the presence of WTAs with TarS-mediated glycosylation with β-GlcNAc in clinically isolated <I>S. aureus</I> strains is an important factor for induction of anti-WTA IgG-mediated C3 deposition and opsonophagocytosis.</P>
나종희(Jong Hee Na),윤준혁(Joon Hyeok Yoon),전재복(Jae Bok Jun),김도원(Do Won Kim) 대한피부과학회 1994 대한피부과학회지 Vol.32 No.1
Blue rubber bleb nevus syndrome is a rare disease of cutaneous hemangioma of a variant of the carvenous type which is clinically characterized by multiple, protutert nt, dark blue, generally soft, rubbery, and compressible cutaneous masses usually sssocia
Cloning and Characterization of the Catalytic Subunit of Human Histone Acetyltransferase, Hat1
Yoon, Jong-Bok,Chung, Hyo-Young,Suh, Na-Young The Korea Science and Technology Center 1998 BMB Reports Vol.31 No.5
Acetylation of lysine residues within the amino-terminal domains of the core histones plays a critical role in chromatin assembly as well as in regulation of gene expression. To study the biochemical function of histone acetylation, we have cloned a cDNA encoding the catalytic subunit of human histone acetyltransferase, Hat1. Analysis of the predicted amino acid sequence of human Hat1 revealed an open reading frame of 419 amino acids with a calculated molecular mass of 49.5 kDa and an isoelectric point of 5.5. The amino acid sequence of human Hat1 is homologous to those of known and putative Hat1 proteins from various species throughout the entire open reading frame. The recombinant human Hat1 protein expressed in bacteria possesses histone H4 acetyltransferase activity in vitro. Both RbAp46 and RbAp48, which participate in various processes of histone metabolism, enhance the histone acetyltransferase activity of the recombinant human Hat1, indicating that they are both able to functionally interact with the human Hat1 in vitro.