M
Margaret L. Pierce
Researcher at Oklahoma State University–Stillwater
Publications - 28
Citations - 928
Margaret L. Pierce is an academic researcher from Oklahoma State University–Stillwater. The author has contributed to research in topics: Phytoalexin & Xanthomonas campestris. The author has an hindex of 16, co-authored 27 publications receiving 880 citations.
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Journal ArticleDOI
A global assembly of cotton ESTs.
Joshua A. Udall,Jordan M. Swanson,Karl Haller,Ryan A. Rapp,Michael E. Sparks,Jamie Hatfield,Yeisoo Yu,Yingru Wu,Caitriona Dowd,Aladdin B. Arpat,Brad Sickler,Thea A. Wilkins,Jin Ying Guo,Xiao-Ya Chen,Jodi A. Scheffler,Earl Taliercio,Ricky Turley,Helen G. McFadden,Paxton Payton,Natalya Klueva,Randell Allen,Deshui Zhang,Candace H. Haigler,Curtis G. Wilkerson,Jinfeng Suo,Stefan R. Schulze,Margaret L. Pierce,Margaret Essenberg,Hyeran Kim,Danny J. Llewellyn,Elizabeth S. Dennis,David Kudrna,Rod A. Wing,Andrew H. Paterson,Cari Soderlund,Jonathan F. Wendel +35 more
TL;DR: Because ESTs from diploid and allotetraploid Gossypium were combined in a single assembly, the assembly and associated information provide a framework for future investigation of cotton functional and evolutionary genomics.
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Problems encountered during the extraction, purification, and chromatography of pectic fragments, and some solutions to them
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Epidermal anthocyanin production as an indicator of bacterial blight resistance in cotton
TL;DR: The results indicate that anthocyanin production by cotton leaves in response to an unsuccessful challenge by the bacterium is a bacterial blight resistance response, but is not essential for resistance.
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Purification of (+)-δ-cadinene synthase, a sesquiterpene cyclase from bacteria-inoculated cotton foliar tissue
TL;DR: A sesquiterpene cyclase whose activity is induced in a glandless, bacterial blight-resistant line of cotton catalyses the conversion of (E,E)-farnesyl diphosphate to (+)-delta-cadinene, and Amino acid sequences of three tryptic peptides from the enzyme have been determined and are similar to known sequences in other terpenecyclases from plants.
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Detection and identification of rhamnogalacturonan lyase activity in intercellular spaces of expanding cotton cotyledons.
TL;DR: Rhamnogalacturonan lyase activity was the highest in rapidly expanding 3- to 4-day-old cotyledons and gradually decreased during the slow-down in expansion over the next 2-3 days and the activity was not induced by wounding or released into the apoplast by cell damage.