Publications by authors named "Qiaohui Lin"

Appointment no-shows have a negative impact on patient health and have caused substantial loss in resources and revenue for health care systems. Intervention strategies to reduce no-show rates can be more effective if targeted to the subpopulations of patients with higher risk of not showing to their appointments. We use electronic health records (EHR) from a large medical center to predict no-show patients based on demographic and health care features.

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To elucidate the mechanisms of molecular regulations underlying primary dysmenorrhea (PD), we used our previously published mRNA expression profile of uterus from PD syndrome rats to construct protein-protein interactions (PPI) network via STRING Interactome. Consequently, 34 subnetworks, including a "continent" (Subnetwork 1) and 33 "islands" (Subnetwork 2-34) were generated. The nodes, with relative expression ratios, were visualized in the PPI networks and their connections were identified.

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Maize () mutations are beneficial for endosperm nutritional quality but cause negative pleiotropic effects for reasons that are not fully understood. Direct targets of the bZIP transcriptional regulator encoded by include and that specify pyruvate phosphate dikinase (PPDK). This enzyme reversibly converts AMP, pyrophosphate, and phosphoenolpyruvate to ATP, orthophosphate, and pyruvate and provides diverse functions in plants.

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Isoamylase-type starch debranching enzymes (ISA) play important roles in starch biosynthesis in chloroplast-containing organisms, as shown by the strict conservation of both catalytically active ISA1 and the noncatalytic homolog ISA2. Functional distinctions exist between species, although they are not understood yet. Numerous plant tissues require both ISA1 and ISA2 for normal starch biosynthesis, whereas monocot endosperm and leaf exhibit nearly normal starch metabolism without ISA2.

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Conserved isoamylase-type starch debranching enzymes (ISAs), including the catalytic ISA1 and noncatalytic ISA2, are major starch biosynthesis determinants. Arabidopsis thaliana leaves require ISA1 and ISA2 for physiological function, whereas endosperm starch is near normal with only ISA1. ISA functions were characterized in maize (Zea mays) leaves to determine whether species-specific distinctions in ISA1 primary structure, or metabolic differences in tissues, are responsible for the differing ISA2 requirement.

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Article Synopsis
  • The study investigates genetic interactions between two maize genes, dull1 (du1) and isa2, which are involved in starch synthesis and debranching.
  • Mutants lacking ISA2 still have a related enzyme (ISA1), and various du1 mutations were analyzed for their effects on amylopectin structure, showing complex alterations not solely due to substrate preference.
  • Double mutants lacking both SSIII and ISA2 resulted in starch deficiency and accumulation of phytoglycogen, indicating that these enzymes interact to regulate proper starch formation and prevent undesirable storage forms like phytoglycogen.
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The maize (Zea mays) opaque5 (o5) locus was shown to encode the monogalactosyldiacylglycerol synthase MGD1. Null and point mutations of o5 that affect the vitreous nature of mature endosperm engendered an allelic series of lines with stepwise reductions in gene function. C(18:3)/C(18:2) galactolipid abundance in seedling leaves was reduced proportionally, without significant effects on total galactolipid content.

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Functions of isoamylase-type starch-debranching enzyme (ISA) proteins and complexes in maize (Zea mays) endosperm were characterized. Wild-type endosperm contained three high molecular mass ISA complexes resolved by gel permeation chromatography and native-polyacrylamide gel electrophoresis. Two complexes of approximately 400 kD contained both ISA1 and ISA2, and an approximately 300-kD complex contained ISA1 but not ISA2.

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Starch biosynthetic enzymes from maize (Zea mays) and wheat (Triticum aestivum) amyloplasts exist in cell extracts in high molecular weight complexes; however, the nature of those assemblies remains to be defined. This study tested the interdependence of the maize enzymes starch synthase IIa (SSIIa), SSIII, starch branching enzyme IIb (SBEIIb), and SBEIIa for assembly into multisubunit complexes. Mutations that eliminated any one of those proteins also prevented the others from assembling into a high molecular mass form of approximately 670 kD, so that SSIII, SSIIa, SBEIIa, and SBEIIb most likely all exist together in the same complex.

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