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26


Diffuse talc granulomatosis in a patient with Crohn's disease [Case Report]

Weiner, Justin; Chandak, Twinkle; Caperna, April; Malieckal, Deepa; Xu, Weisheng; Reder, Ilan; Shah, Rakesh
PMID: 23027858
ISSN: 1535-4970
CID: 3129902

Thermoelectric magnetohydrodynamic stirring of liquid metals

Jaworski, M A; Gray, T K; Antonelli, M; Kim, J J; Lau, C Y; Lee, M B; Neumann, M J; Xu, W; Ruzic, D N
The direct observation of a thermoelectric magnetohydrodynamic (TEMHD) flow has been achieved and is reported here. The origin of the flow is identified based on a series of qualitative tests and corresponds, quantitatively, with a swirling flow TEMHD model. A theory for determining the dominant driver of a free-surface flow, TEMHD or thermocapillary (TC), is found to be consistent with the experimental results. The use of the analytical form for an open geometry develops a new dimensionless parameter describing the ratio of TEMHD to TC generated flows.
PMID: 20366988
ISSN: 1079-7114
CID: 3989062

Plant responses to environmental stress: regulation and functions of the Arabidopsis TCH genes

Braam, J; Sistrunk, M L; Polisensky, D H; Xu, W; Purugganan, M M; Antosiewicz, D M; Campbell, P; Johnson, K A
Expression of the Arabidopsis TCH genes is markedly upregulated in response to a variety of environmental stimuli including the seemingly innocuous stimulus of touch. Understanding the mechanism(s) and factors that control TCH gene regulation will shed light on the signaling pathways that enable plants to respond to environmental conditions. The TCH proteins include calmodulin, calmodulin-related proteins and a xyloglucan endotransglycosylase. Expression analyses and localization of protein accumulation indicates that the potential sites of TCH protein function include expanding cells and tissues under mechanical strain. We hypothesize that at least a subset of the TCH proteins may collaborate in cell wall biogenesis.
PMID: 9299794
ISSN: 0032-0935
CID: 3116742

Life in a changing world: TCH gene regulation of expression and responses to environmental signals

Braam, J; Sistrunk, M L; Polisensky, D H; Xu, W; Purugganan, M M; Antosiewicz, D M; Campbell, P; Johnson, K A
The Arabidopsis TCH genes were discovered as a consequence of their marked upregulation of expression in response to seemingly innocuous stimuli such as touch. Further analyses have indicated that these genes are upregulated by a variety of diverse stimuli. Understanding the mechanism(s) and factors that control TCH gene regulation will shed light on the signaling pathways that enable plants to respond to changing environmental conditions. The TCH proteins include calmodulin, calmodulin-related proteins and a xyloglucan endotransglycosylase. Expression analyses and localization of protein accumulation indicate that the potential sites of TCH protein function include expanding cells and tissues under mechanical strain. We hypothesize that the TCH proteins may collaborate in cell wall biogenesis.
PMID: 11539337
ISSN: 0031-9317
CID: 3116712

Arabidopsis TCH4, regulated by hormones and the environment, encodes a xyloglucan endotransglycosylase

Xu, W; Purugganan, M M; Polisensky, D H; Antosiewicz, D M; Fry, S C; Braam, J
Adaptation of plants to environmental conditions requires that sensing of external stimuli be linked to mechanisms of morphogenesis. The Arabidopsis TCH (for touch) genes are rapidly upregulated in expression in response to environmental stimuli, but a connection between this molecular response and developmental alterations has not been established. We identified TCH4 as a xyloglucan endotransglycosylase by sequence similarity and enzyme activity. Xyloglucan endotransglycosylases most likely modify cell walls, a fundamental determinant of plant form. We determined that TCH4 expression is regulated by auxin and brassinosteroids, by environmental stimuli, and during development, by a 1-kb region. Expression was restricted to expanding tissues and organs that undergo cell wall modification. Regulation of genes encoding cell wall-modifying enzymes, such as TCH4, may underlie plant morphogenetic responses to the environment.
PMCID:161010
PMID: 7580251
ISSN: 1040-4651
CID: 3116722

Crystal structure of a paired domain-DNA complex at 2.5 A resolution reveals structural basis for Pax developmental mutations

Xu, W; Rould, M A; Jun, S; Desplan, C; Pabo, C O
The 2.5 A resolution structure of a cocrystal containing the paired domain from the Drosophila paired (prd) protein and a 15 bp site shows structurally independent N-terminal and C-terminal subdomains. Each of these domains contains a helical region resembling the homeodomain and the Hin recombinase. The N-terminal domain makes extensive DNA contacts, using a novel beta turn motif that binds in the minor groove and a helix-turn-helix unit with a docking arrangement surprisingly similar to that of the lambda repressor. The C-terminal domain is not essential for prd binding and does not contact the optimized site. All known developmental missense mutations in the paired box of mammalian Pax genes map to the N-terminal subdomain, and most of them are found at the protein-DNA interface.
PMID: 7867071
ISSN: 0092-8674
CID: 1695302