@article{wang_replogle_hussey_baum_wang_davis_mitchum_2011, title={Identification of potential host plant mimics of CLAVATA3/ESR (CLE)-like peptides from the plant-parasitic nematode Heterodera schachtii}, volume={12}, ISSN={["1364-3703"]}, DOI={10.1111/j.1364-3703.2010.00660.x}, abstractNote={SUMMARY}, number={2}, journal={MOLECULAR PLANT PATHOLOGY}, author={Wang, Jianying and Replogle, Amy and Hussey, Richard and Baum, Thomas and Wang, Xiaohong and Davis, Eric L. and Mitchum, Melissa G.}, year={2011}, month={Feb}, pages={177–186} }
 @article{wang_lee_replogle_joshi_korkin_hussey_baum_davis_wang_mitchum_2010, title={Dual roles for the variable domain in protein trafficking and host-specific recognition of Heterodera glycines CLE effector proteins}, volume={187}, ISSN={["1469-8137"]}, DOI={10.1111/j.1469-8137.2010.03300.x}, abstractNote={
            Featured paper: See Editorial p877
          }, number={4}, journal={NEW PHYTOLOGIST}, author={Wang, Jianying and Lee, Chris and Replogle, Amy and Joshi, Sneha and Korkin, Dmitry and Hussey, Richard and Baum, Thomas J. and Davis, Eric L. and Wang, Xiaohong and Mitchum, Melissa G.}, year={2010}, pages={1003–1017} }
 @article{sukno_mccuiston_wong_wang_thon_hussey_baum_davis_2007, title={Quantitative detection of double-stranded RNA-mediated gene silencing of parasitism genes in Heterodera glycines}, volume={39}, number={2}, journal={Journal of Nematology}, author={Sukno, S. A. and McCuiston, J. and Wong, M. Y. and Wang, X. H. and Thon, M. R. and Hussey, R. and Baum, T. and Davis, E.}, year={2007}, pages={145–152} }
 @article{mitchum_sukno_wang_shani_tsabary_shoseyov_davis_2004, title={The promoter of the Arabidopsis thaliana Cel1 endo-1,4-beta glucanase gene is differentially expressed in plant feeding cells induced by root-knot and cyst nematodes}, volume={5}, ISSN={["1364-3703"]}, DOI={10.1111/J.1364-3703.2004.00216.X}, abstractNote={SUMMARY}, number={3}, journal={MOLECULAR PLANT PATHOLOGY}, author={Mitchum, MG and Sukno, S and Wang, XH and Shani, Z and Tsabary, G and Shoseyov, O and Davis, EL}, year={2004}, month={May}, pages={175–181} }
 @article{de boer_mcdermott_wang_maier_qu_hussey_davis_baum_2002, title={The use of DNA microarrays for the developmental expression analysis of cDNAs from the oesophageal gland cell region of Heterodera glycines}, volume={3}, ISSN={["1364-3703"]}, DOI={10.1046/j.1364-3703.2002.00122.x}, abstractNote={Summary}, number={4}, journal={MOLECULAR PLANT PATHOLOGY}, author={De Boer, JM and McDermott, JP and Wang, XH and Maier, T and Qu, F and Hussey, RS and Davis, EL and Baum, TJ}, year={2002}, month={Jul}, pages={261–270} }
 @article{goellner_wang_davis_2001, title={Endo-beta-1,4-glucanase expression in compatible plant-nematode interactions}, volume={13}, ISSN={["1532-298X"]}, DOI={10.1105/tpc.13.10.2241}, number={10}, journal={PLANT CELL}, author={Goellner, M and Wang, XH and Davis, EL}, year={2001}, month={Oct}, pages={2241–2255} }
 @article{wang_allen_ding_goellner_maier_boer_baum_hussey_davis_2001, title={Signal peptide-selection of cDNA cloned directly from the esophageal gland cells of the soybean cyst nematode Heterodera glycines}, volume={14}, ISSN={["1943-7706"]}, DOI={10.1094/mpmi.2001.14.4.536}, abstractNote={ Secretions from the esophageal gland cells of plantparasitic nematodes play critical roles in the nematodeparasitic cycle. A novel method to isolate cDNA encoding putative nematode secretory proteins was developed that utilizes mRNA for reverse transcription-polymerase chain reaction derived from microaspiration of the esophageal gland cell contents of parasitic stages of the soybean cyst nematode Heterodera glycines. The resulting H. glycines gland cell cDNA was cloned into the pRK18 vector, and plasmid DNA was transformed into a mutated yeast host for specific selection of cDNA inserts that encode proteins with functional signal peptides. Of the 223 cDNA clones recovered from selection in yeast, 97% of the clones encoded a predicted signal peptide. Fourteen unique cDNA clones hybridized to genomic DNA of H. glycines on Southern blots and, among them, nine cDNA clones encoded putative extracellular proteins, as predicted by PSORT II computer analysis. Four cDNA clones hybridized to transcripts within the dorsal esophageal gland cell of parasitic stages of H. glycines, and in situ hybridization within H. glycines was not detected for eight cDNA clones. The protocol provides a direct means to isolate potential plant-parasitic nematode esophageal gland secretory protein genes. }, number={4}, journal={MOLECULAR PLANT-MICROBE INTERACTIONS}, author={Wang, XH and Allen, R and Ding, XF and Goellner, M and Maier, T and Boer, JM and Baum, TJ and Hussey, RS and Davis, EL}, year={2001}, month={Apr}, pages={536–544} }
 @article{ransom-hodgkins_brglez_wang_boss_2000, title={Calcium-regulated proteolysis of eEF1A}, volume={122}, ISSN={["0032-0889"]}, DOI={10.1104/pp.122.3.957}, abstractNote={Abstract}, number={3}, journal={PLANT PHYSIOLOGY}, author={Ransom-Hodgkins, WD and Brglez, I and Wang, XM and Boss, WF}, year={2000}, month={Mar}, pages={957–965} }
 @article{boer_yan_wang_smant_hussey_davis_baum_1999, title={Developmental expression of secretory beta-1,4-endoglucanases in the subventral esophageal glands of Heterodera glycines}, volume={12}, ISSN={["0894-0282"]}, DOI={10.1094/MPMI.1999.12.8.663}, abstractNote={Two β-1,4-endoglucanases (EGases), Hg-eng-1 and Hg-eng-2, were recently cloned from the soybean cyst nematode, Heterodera glycines, and their expression was shown in the subventral esophageal glands of hatched second-stage juveniles (J2). We examined the expression of these EGases in the subventral glands of all post-embryonic life stages of H. glycines by in situ hybridization and immunolocalization. The first detectable accumulation of EGase mRNAs occurred in the subventral glands of unhatched J2. EGase transcripts remained detectable in J2 after hatching and during subsequent root invasion. However, in late parasitic J2 and third-stage juveniles (J3), the percentage of individuals that showed EGase transcripts decreased. In female fourth-stage juveniles and adult females, EGase transcripts were no longer detected in the subventral glands. EGase hybridization signal reappeared in unhatched males coiled within the J3 cuticle, and transcripts were also present in the subventral glands of migratory adult males. Immunofluorescence labeling showed that EGase translation products are most abundantly present in the subventral glands of preparasitic J2, migratory parasitic J2, and adult males. The presence of EGases predominantly in the migratory stages suggests that the enzymes are used by the nematodes to soften the walls of root cells during penetration and intracellular migration.}, number={8}, journal={MOLECULAR PLANT-MICROBE INTERACTIONS}, author={Boer, JM and Yan, YT and Wang, XH and Smant, G and Hussey, RS and Davis, EL and Baum, TJ}, year={1999}, month={Aug}, pages={663–669} }
 @article{wang_meyers_yan_baum_smant_hussey_davis_1999, title={In planta localization of a beta-1,4-endoglucanase secreted by Heterodera glycines}, volume={12}, ISSN={["0894-0282"]}, DOI={10.1094/MPMI.1999.12.1.64}, abstractNote={ Polyclonal sera specific to β-1,4-endoglucanases (cellulases) synthesized in the subventral esophageal gland cells of the soybean cyst nematode, Heterodera glycines, were used to provide the first identification of a nematode esophageal gland protein that is secreted into host plant tissue. Sera generated to proteins encoded by Hg-eng-1 and Hg-eng-2 (endoglucanases) did not cross-react with soybean root proteins on Western blots (immunoblots) or in immunofluorescence microscopy of noninoculated (control) soybean root sections. In cross sections of soybean roots at 24 h after inoculation of roots with second-stage juveniles of H. glycines, HG-ENG-1 was localized within the nematode's subventral gland cells and was not detected in root tissue. HG-ENG-2 was localized within the subventral gland cells and was secreted from the juvenile's cortical tissue at 24 h after inoculation of roots with second-stage juveniles of H. glycines. HG-ENG-2 was localized along the juvenile's migratory path through the root cortex. }, number={1}, journal={MOLECULAR PLANT-MICROBE INTERACTIONS}, author={Wang, XH and Meyers, D and Yan, YT and Baum, T and Smant, G and Hussey, R and Davis, E}, year={1999}, month={Jan}, pages={64–67} }
 @article{smant_stokkermans_yan_boer_baum_wang_hussey_gommers_henrissat_davis_et al._1998, title={Endogenous cellulases in animals: Isolation of beta-1,4-endoglucanase genes from two species of plant-parasitic cyst nematodes}, volume={95}, ISSN={["0027-8424"]}, DOI={10.1073/pnas.95.9.4906}, abstractNote={
            β-1,4-Endoglucanases (EGases, EC
            3.2.1.4
            ) degrade polysaccharides possessing β-1,4-glucan backbones such as cellulose and xyloglucan and have been found among extremely variegated taxonomic groups. Although many animal species depend on cellulose as their main energy source, most omnivores and herbivores are unable to produce EGases endogenously. So far, all previously identified EGase genes involved in the digestive system of animals originate from symbiotic microorganisms. Here we report on the synthesis of EGases in the esophageal glands of the cyst nematodes
            Globodera rostochiensis
            and
            Heterodera glycines
            . From each of the nematode species, two cDNAs were characterized and hydrophobic cluster analysis revealed that the four catalytic domains belong to family 5 of the glycosyl hydrolases (EC 3.2.1, 3.2.2, and 3.2.3). These domains show 37–44% overall amino acid identity with EGases from the bacteria
            Erwinia chrysanthemi
            ,
            Clostridium acetobutylicum
            , and
            Bacillus subtilis
            . One EGase with a bacterial type of cellulose-binding domain was identified for each nematode species. The leucine-rich hydrophobic core of the signal peptide and the presence of a polyadenylated 3′ end precluded the EGases from being of bacterial origin. Cyst nematodes are obligatory plant parasites and the identified EGases presumably facilitate the intracellular migration through plant roots by partial cell wall degradation.
          }, number={9}, journal={PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA}, author={Smant, G and Stokkermans, JPWG and Yan, YT and Boer, JM and Baum, TJ and Wang, XH and Hussey, RS and Gommers, FJ and Henrissat, B and Davis, EL and et al.}, year={1998}, month={Apr}, pages={4906–4911} }