@article{howard_hu_babaoglu_chandra_borghi_tan_he_winter-sederoff_gassmann_veronese_et al._2013, title={High-Throughput RNA Sequencing of Pseudomonas-Infected Arabidopsis Reveals Hidden Transcriptome Complexity and Novel Splice Variants}, volume={8}, ISSN={["1932-6203"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-84885077606&partnerID=MN8TOARS}, DOI={10.1371/journal.pone.0074183}, abstractNote={We report the results of a genome-wide analysis of transcription in Arabidopsis thaliana after treatment with Pseudomonas syringae pathovar tomato. Our time course RNA-Seq experiment uses over 500 million read pairs to provide a detailed characterization of the response to infection in both susceptible and resistant hosts. The set of observed differentially expressed genes is consistent with previous studies, confirming and extending existing findings about genes likely to play an important role in the defense response to Pseudomonas syringae. The high coverage of the Arabidopsis transcriptome resulted in the discovery of a surprisingly large number of alternative splicing (AS) events – more than 44% of multi-exon genes showed evidence for novel AS in at least one of the probed conditions. This demonstrates that the Arabidopsis transcriptome annotation is still highly incomplete, and that AS events are more abundant than expected. To further refine our predictions, we identified genes with statistically significant changes in the ratios of alternative isoforms between treatments. This set includes several genes previously known to be alternatively spliced or expressed during the defense response, and it may serve as a pool of candidate genes for regulated alternative splicing with possible biological relevance for the defense response against invasive pathogens.}, number={10}, journal={PLOS ONE}, author={Howard, Brian E. and Hu, Qiwen and Babaoglu, Ahmet Can and Chandra, Manan and Borghi, Monica and Tan, Xiaoping and He, Luyan and Winter-Sederoff, Heike and Gassmann, Walter and Veronese, Paola and et al.}, year={2013}, month={Oct} }
 @article{tsou_lee_allen_winter-sederoff_robertson_2012, title={An ER-targeted calcium-binding peptide confers salt and drought tolerance mediated by CIPK6 in Arabidopsis}, volume={235}, ISSN={["1432-2048"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-84857634774&partnerID=MN8TOARS}, DOI={10.1007/s00425-011-1522-9}, abstractNote={Different plant organelles have high internal stores of Ca(2+) compared to the cytoplasm and could play independent roles in stress responses or signal transduction. We used a GFP fusion with the C-domain of calreticulin, which shows low-affinity, high capacity Ca(2+) binding in the ER, as a calcium-binding peptide (CBP) to specifically increase stores in the ER and nucleus. Despite the presence of a signal sequence and KDEL retention sequence, our work and previous studies (Brandizzi et al. Plant Journal 34:269-281, 2003) demonstrated both ER and nuclear localization of GFP-CBP. Under normal conditions, GFP-CBP-expressing lines had ~25% more total Ca(2+) and higher levels of chlorophyll and seed yield than wild type and GFP controls. CBP-expressing plants also had better survival under intermittent drought or high salt treatments and increased root growth. One member of the CIPK (calcineurin B-like interacting protein kinase) gene family, CIPK6, was up-regulated in CBP-expressing plants, even under non-stress conditions. A null mutation in cipk6 abolished the increased stress tolerance of CBP-transgenic plants, as well as the CBP-mediated induction of two stress-associated genes, DREB1A and RD29A, under non-stress conditions. Although this suggested that it was the induction of CIPK6, rather than localized changes in Ca(2+), that resulted in increased survival under adverse conditions, CIPK6 induction still required Ca(2+). This work demonstrates that ER (or nuclear) Ca(2+) can directly participate in signal transduction to alter gene expression. The discovery of a method for increasing Ca(2+) levels without deleterious effects on plant growth may have practical applications.}, number={3}, journal={PLANTA}, author={Tsou, Pei-Lan and Lee, Sang Yoon and Allen, Nina Stromgren and Winter-Sederoff, Heike and Robertson, Dominique}, year={2012}, month={Mar}, pages={539–552} }
 @article{novaes_kirst_chiang_winter-sederoff_sederoff_2010, title={Lignin and Biomass: A Negative Correlation for Wood Formation and Lignin Content in Trees}, volume={154}, ISSN={["0032-0889"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-77957730551&partnerID=MN8TOARS}, DOI={10.1104/pp.110.161281}, abstractNote={Studies in populations of forest tree hybrids have shown a negative correlation of biomass growth (usually measured as wood volume) and lignin content ([Kirst et al., 2004][1]; [Novaes et al., 2009][2]). The control of growth and lignin appears to be highly regulated, implying that selection for}, number={2}, journal={PLANT PHYSIOLOGY}, author={Novaes, Evandro and Kirst, Matias and Chiang, Vincent and Winter-Sederoff, Heike and Sederoff, Ronald}, year={2010}, month={Oct}, pages={555–561} }
 @article{hardin_winter_huber_2004, title={Phosphorylation of the amino terminus of maize sucrose synthase in relation to membrane association and enzyme activity}, volume={134}, ISSN={["1532-2548"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-1942437647&partnerID=MN8TOARS}, DOI={10.1104/pp.103.036780}, abstractNote={Abstract}, number={4}, journal={PLANT PHYSIOLOGY}, author={Hardin, SC and Winter, H and Huber, SC}, year={2004}, month={Apr}, pages={1427–1438} }
 @misc{winter_huber_2000, title={Regulation of sucrose metabolism in higher plants: Localization and regulation of activity of key enzymes}, volume={19}, ISSN={["1549-7836"]}, DOI={10.1016/s0735-2689(01)80002-2}, abstractNote={Sucrose (Suc) plays a central role in plant growth and development. It is a major end product of photosynthesis and functions as a primary transport sugar and in some cases as a direct or indirect regulator of gene expression. Research during the last 2 decades has identified the pathways involved and which enzymes contribute to the control of flux. Availability of metabolites for Suc synthesis and ‘demand’ for products of sucrose degradation are important factors, but this review specifically focuses on the biosynthetic enzyme sucrose-phosphate synthase (SPS), and the degradative enzymes, sucrose synthase (SuSy), and the invertases. Recent progress has included the cloning of genes encoding these enzymes and the elucidation of posttranslational regulatory mechanisms. Protein phosphorylation is emerging as an important mechanism controlling SPS activity in response to various environmental and endogenous signals. In terms of Suc degradation, invertase-catalyzed hydrolysis generally has been associated with cell expansion, whereas SuSy-catalyzed metabolism has been linked with biosynthetic processes (e.g., cell wall or storage products). Recent results indicate that SuSy may be localized in multiple cellular compartments: (1) as a soluble enzyme in the cytosol (as traditionally assumed); (2) associated with the plasma membrane; and (3) associated with the actin cytoskel-eton. Phosphorylation of SuSy has been shown to occur and may be one of the factors controlling localization of the enzyme. The purpose of this review is to summarize some of the recent developments relating to regulation of activity and localization of key enzymes involved in sucrose metabolism in plants.}, number={1}, journal={CRITICAL REVIEWS IN PLANT SCIENCES}, author={Winter, H and Huber, SC}, year={2000}, pages={31–67} }
 @misc{winter_huber_2000, title={Regulation of sucrose metabolism in higher plants: Localization and regulation of activity of key enzymes}, volume={35}, ISSN={["1549-7798"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-0033829914&partnerID=MN8TOARS}, DOI={10.1080/10409230008984165}, abstractNote={ABSTRACT Sucrose (Sue) plays a central role in plant growth and development. It is a major end product of photosynthesis and functions as a primary transport sugar and in some cases as a direct or indirect regulator of gene expression. Research during the last 2 decades has identified the pathways involved and which enzymes contribute to the control of flux. Availability of metabolites for Sue synthesis and 'demand' for products of sucrose degradation are important factors, but this review specifically focuses on the biosynthetic enzyme sucrose-phosphate synthase (SPS), and the degradative enzymes, sucrose synthase (SuSy), and the invertases. Recent progress has included the cloning of genes encoding these enzymes and the elucidation of posttranslational regulatory mechanisms. Protein phosphorylation is emerging as an important mechanism controlling SPS activity in response to various environmental and endogenous signals. In terms of Sue degradation, invertase-catalyzed hydrolysis generally has been associated with cell expansion, whereas SuSy-catalyzed metabolism has been linked with biosynthetic processes (e.g., cell wall or storage products). Recent results indicate that SuSy may be localized in multiple cellular compartments: (1) as a soluble enzyme in the cytosol (as traditionally assumed); (2) associated with the plasma membrane; and (3) associated with the actin cytoskeleton. Phosphorylation of SuSy has been shown to occur and may be one of the factors controlling localization of the enzyme. The purpose of this review is to summarize some of the recent developments relating to regulation of activity and localization of key enzymes involved in sucrose metabolism in plants.}, number={4}, journal={CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY}, author={Winter, H and Huber, SC}, year={2000}, pages={253–289} }
 @article{kuzma_winter_storer_oresnik_atkins_layzell_1999, title={The site of oxygen limitation in soybean nodules}, volume={119}, ISSN={["1532-2548"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-0032838730&partnerID=MN8TOARS}, DOI={10.1104/pp.119.2.399}, abstractNote={Abstract}, number={2}, journal={PLANT PHYSIOLOGY}, author={Kuzma, MM and Winter, H and Storer, P and Oresnik, I and Atkins, CA and Layzell, DB}, year={1999}, month={Feb}, pages={399–407} }
 @article{collings_winter_wyatt_allen_1998, title={Growth dynamics and cytoskeleton organization during stem maturation and gravity-induced stem bending in Zea mays L.}, volume={207}, ISSN={["1432-2048"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-0032435367&partnerID=MN8TOARS}, DOI={10.1007/s004250050480}, abstractNote={Characterization of gravitropic bending in the maize stem pulvinus, a tissue that functions specifically in gravity responses, demonstrates that the pulvinus is an ideal system for studying gravitropism. Gravistimulation during the second of three developmental phases of the pulvinus induces a gradient of cell elongation across the non-growing cells of the pulvinus, with the most elongation occurring on the lower side. This cell elongation is spatially and temporally separated from normal internodal cell elongation. The three characterized growth phases in the pulvinus correspond closely to a specialized developmental sequence in which structural features typical of cells not fully matured are retained while cell maturation occurs in surrounding internodal and nodal tissue. For example, the lignification of supporting tissue and rearrangement of transverse microtubules to oblique that occur in the internode when cell elongation ceases are delayed for up to 10 d in the adjacent cells of the pulvinus, and only occurs as a pulvinus loses its capacity to respond to gravistimulation. Gravistimulation does not modify this developmental sequence. Neither wall lignification nor rearrangement of transverse microtubules occurs in the rapidly elongating lower side or non-responsive upper side of the pulvinus until the pulvinus loses the capacity to bend further. Gravistimulation does, however, lead to the formation of putative pit fields within the expanding cells of the pulvinus.}, number={2}, journal={PLANTA}, author={Collings, DA and Winter, H and Wyatt, SE and Allen, NS}, year={1998}, month={Dec}, pages={246–258} }
 @article{winter_huber_huber_1998, title={Identification of sucrose synthase as an actin-binding protein}, volume={430}, ISSN={["1873-3468"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-0032479338&partnerID=MN8TOARS}, DOI={10.1016/S0014-5793(98)00659-0}, abstractNote={Several lines of evidence indicate that sucrose synthase (SuSy) binds both G‐ and F‐actin: (i) presence of SuSy in the Triton X‐100‐insoluble fraction of microsomal membranes (i.e. crude cytoskeleton fraction); (ii) co‐immunoprecipitation of actin with anti‐SuSy monoclonal antibodies; (iii) association of SuSy with in situ phalloidin‐stabilized F‐actin filaments; and (iv) direct binding to F‐actin, polymerized in vitro. Aldolase, well known to interact with F‐actin, interfered with binding of SuSy, suggesting that a common or overlapping binding site may be involved. We postulate that some of the soluble SuSy in the cytosol may be associated with the actin cytoskeleton in vivo.}, number={3}, journal={FEBS LETTERS}, author={Winter, H and Huber, JL and Huber, SC}, year={1998}, month={Jul}, pages={205–208} }
 @article{collings_winter_allen_1997, title={Cytoskeletal organisation in gravistimulated maize stems}, volume={16}, number={1997}, journal={Current Topics in Plant Biochemistry and Physiology}, author={Collings, D. and Winter, H. and Allen, N.}, year={1997}, pages={88} }