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- 저자 : Dangl, Jeffery L. (검색결과 4 건)
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Widmann Gerlig,Dangl Marcel,Lutz Elisa,Fleckenstein Bernhard,Offermanns Vincent,Offermanns Vincent,Puelacher Wolfgang,Salbrechter Lukas 대한영상치의학회 2023 Imaging Science in Dentistry Vol.53 No.1
Purpose: Maxillofacial trauma predominantly affects young adults between 20 and 40 years of age. Although radioprotection is a legal requirement, the significant potential of dose reduction in computed tomography (CT) is still underused in the clinical routine. The objective of this study was to evaluate whether maxillofacial fractures can be reliably detected and classified using ultra-low-dose CT. Materials and Methods: CT images of 123 clinical cases with maxillofacial fractures were classified by two readers using the AOCOIAC software and compared with the corresponding results from post-treatment images. In group 1, consisting of 97 patients with isolated facial trauma, pre-treatment CT images at different dose levels (volumetric computed tomography dose index: ultra-low dose, 2.6 mGy; low dose, <10 mGy; and regular dose, <20 mGy) were compared with post-treatment cone-beam computed tomography (CBCT). In group 2, consisting of 31 patients with complex midface fractures, pre-treatment shock room CT images were compared with post-treatment CT at different dose levels or CBCT. All images were presented in random order and classified by 2 readers blinded to the clinical results. All cases with an unequal classification were re-evaluated. Results: In both groups, ultra-low-dose CT had no clinically relevant effect on fracture classification. Fourteen cases in group 2 showed minor differences in the classification code, which were no longer obvious after comparing the images directly to each other. Conclusion: Ultra-low-dose CT images allowed the correct diagnosis and classification of maxillofacial fractures. These results might lead to a substantial reconsideration of current reference dose levels.
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Nam,Jae Sung,Dangl,Jeffery L. 한국생명과학회 2001 한국생명과학회 학술발표회 Vol.33 No.-
Disease resistance in plants is often controlled by a gene-for-gene mechanism in which avirulence(avr) gene products of phytopathogen are recognized, either directly or indirectly, by plant resistance gene (R) products. Members of the NBS-LRR class of R genes encode proteins containing a putative nucleotide binding site(NBS) and carboxy terminal leucine-rich repeats (LRR). Because NBS-LRR proteins do not contain predicted transmembrane domains, singnal peptides for secretion, or post-translation modification sequence for targeting to membrane, it has been suspected that they are soluble cytoplasmic proteins. we determined the localization of RPM1 protein, a NBS-LRR class of R gene from Arabidopsis which confers resistance to Psedomonas syringae expressing either the avrRpm1 or avrB, by an epitope tag. In contrast to previous suggestion, the functional RPM1::Myc protein resides peripherally on the cytoplasmic face of the plasm membrane. Its association with the membrane is likely maintained through interaction with unknown integral membrane proteins, because RPM1::Myc protein does not contain any predicted sequence for membrane targeting. Recently a potential RPM1 membrane anchoring protein has been identified using the N-terminal part of RPM1 protein as a bait in a yeast two-hybrid screen. The N-terminus of this protein contains 6-7 potential transmembrane domains and a novel C-terminal cytoplasmic domain that interacts with RPM1. Furthermore, RPM1 protein is degraded coincident with the onset of the hypersensitive response, suggesting the existence of a desensitization mechanism to control the extent of cell death and overall resistance response at the site of infection.
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Redditt, Thomas J.,Chung, Eui-Hwan,Karimi, Hana Zand,Rodibaugh, Natalie,Zhang, Yixiang,Trinidad, Jonathan C.,Kim, Jin Hee,Zhou, Qian,Shen, Mingzhe,Dangl, Jeffery L.,Mackey, David,Innes, Roger W. American Society of Plant Biologists 2019 The Plant cell Vol.31 No.11
<P>The <I>Pseudomonas syringae</I> effector protein AvrRpm1 ADP ribosylates RIN4 proteins from Arabidopsis and soybean, which promotes association of RIN4 with EXO70E2 and suppression of callose deposition.</P><P>The <I>Pseudomonas syringae</I> effector protein AvrRpm1 activates the Arabidopsis (<I>Arabidopsis thaliana</I>) intracellular innate immune receptor protein RESISTANCE TO PSEUDOMONAS MACULICOLA1 (RPM1) via modification of a second Arabidopsis protein, RPM1-INTERACTING PROTEIN4 (<I>At</I>RIN4). Prior work has shown that AvrRpm1 induces phosphorylation of <I>At</I>RIN4, but homology modeling indicated that AvrRpm1 may be an ADP-ribosyl transferase. Here, we show that AvrRpm1 induces ADP-ribosylation of RIN4 proteins from both Arabidopsis and soybean (<I>Glycine max</I>) within two highly conserved nitrate-induced (NOI) domains. It also ADP ribosylates at least 10 additional Arabidopsis NOI domain-containing proteins. The ADP-ribosylation activity of AvrRpm1 is required for subsequent phosphorylation on Thr-166 of <I>At</I>RIN4, an event that is necessary and sufficient for RPM1 activation. We also show that the C-terminal NOI domain of AtRIN4 interacts with the exocyst subunits EXO70B1, EXO70E1, EXO70E2, and EXO70F1. Mutation of either EXO70B1 or EXO70E2 inhibited secretion of callose induced by the bacterial flagellin-derived peptide flg22. Substitution of RIN4 Thr-166 with Asp enhanced the association of <I>At</I>RIN4 with EXO70E2, which we posit inhibits its callose deposition function. Collectively, these data indicate that AvrRpm1 ADP-ribosyl transferase activity contributes to virulence by promoting phosphorylation of RIN4 Thr-166, which inhibits the secretion of defense compounds by promoting the inhibitory association of RIN4 with EXO70 proteins.</P><P>[Figure]</P>
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