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Xiang Zhu

Researcher at University of Georgia

Publications -  8
Citations -  783

Xiang Zhu is an academic researcher from University of Georgia. The author has contributed to research in topics: Membrane protein & Secondary cell wall. The author has an hindex of 8, co-authored 8 publications receiving 676 citations.

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An Arabidopsis Cell Wall Proteoglycan Consists of Pectin and Arabinoxylan Covalently Linked to an Arabinogalactan Protein

TL;DR: A cell wall proteoglycan with pectin and arabinoxylan covalently attached to an arabinogalactan protein is described, identifying a cross-linked matrix polysaccharide wall protein architecture with implications for wall structure, function, and synthesis.
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Galacturonosyltransferase (GAUT)1 and GAUT7 are the core of a plant cell wall pectin biosynthetic homogalacturonan:galacturonosyltransferase complex

TL;DR: This study provides conclusive evidence that the GAUT1:GAUT7 complex is the catalytic core of an HG:GalAT complex and that cell wall matrix polysaccharide biosynthesis occurs via protein complexes.
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Biosynthesis of 4-thiouridine in tRNA in the methanogenic archaeon Methanococcus maripaludis

TL;DR: In vitro assays suggest that S2− is a physiologically relevant sulfur donor for s4U formation catalyzed by MMP1354, indicating that methanogenic archaea developed a strategy for sulfur incorporation into s4 U that differs from bacteria; this may be an adaptation to life in sulfide-rich environments.
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Loss of Arabidopsis GAUT12/IRX8 causes anther indehiscence and leads to reduced G lignin associated with altered matrix polysaccharide deposition

TL;DR: It is shown that male sterility in the irx8 mutant is due to indehiscent anthers caused by reduced deposition of xylan and lignin in the endothecium cell layer, which supports the hypothesis that GAUT12 functions in the synthesis of a structure required for xylanand lignIn deposition during secondary cell wall formation.
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Identification and Localization of Myxococcus xanthus Porins and Lipoproteins

TL;DR: Results suggest that ECM proteins have a unique method of secretion and it is now possible to target lipoproteins to specific IM, OM and ECM locations by manipulating the amino acid sequence near the +1 cysteine processing site.