@misc{davis_yan_2003, title={Chemoreceptors in plant parasitic nematodes}, volume={6,521,438}, number={2003 Feb. 18}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Davis, E. L. and Yan, Y.-T.}, year={2003} }
 @article{yan_davis_2002, title={Characterisation of guanylyl cyclase genes in the soyabean cyst nematode Heterodera glycines}, volume={32}, ISSN={["1879-0135"]}, DOI={10.1016/S0020-7519(01)00315-0}, abstractNote={Parasitism by the soybean cyst nematode, Heterodera glycines, has become one of the major limiting factors in soybean production world-wide. A partial HG-gcy-1 cDNA clone was obtained by screening a H. glycines cDNA library with a probe derived from the HG-gcy1 genomic sequence, and HG-gcy-1 full-length cDNA was obtained by nested PCR and 5' rapid amplification of cDNA ends (5' RACE). Two additional, full-length guanylyl cyclase cDNA clones from H. glycines, named HG-gcy-2 and HG-gcy-3, were recovered directly by screening the H. glycines cDNA library with a probe derived from sequence of the HG-gcy-1 catalytic domain. The encoded proteins of all three HG-gcy genes had an extracellular ligand-binding domain, a single membrane-spanning domain, an intracellular protein kinase-like domain, and a guanylyl cyclase catalytic domain. The three HG-GCY proteins had conserved cysteine residues to form disulfide bridges within the extracellular domain similar to the predicted ligand-binding domains of other known membrane-bound guanylyl cyclases. mRNA in situ hybridisation detected the expression of HG-gcy-1 and HG-gcy-2 transcripts in specific and different sensory neurons within H. glycines specimens. HG-gcy-3 transcripts were not localised in H. glycines specimens by in situ hybridisation. The discovery of the three guanylyl cyclase genes in H. glycines is the first of its kind in a plant-parasitic nematode and may be representative of a conserved gene family used for chemosensory recognition in parasitic nematodes.}, number={1}, journal={INTERNATIONAL JOURNAL FOR PARASITOLOGY}, author={Yan, YT and Davis, EL}, year={2002}, month={Jan}, pages={65–72} }
 @article{yan_smant_davis_2001, title={Functional screening yields a new beta-1,4-endoglucanase gene from Heterodera glycines that may be the product of recent gene duplication}, volume={14}, ISSN={["1943-7706"]}, DOI={10.1094/MPMI.2001.14.1.63}, abstractNote={ Clones with secreted cellulolytic activity were identified when a cDNA library constructed from poly A(+) RNA of preparasitic second-stage juveniles of Heterodera glycines, the soybean cyst nematode, was expressed in the Escherichia coli SOLR strain and overlaid with a carboxymethylcellulose (CMC) substrate. Twenty CMC-degrading clones were analyzed, and all were either identical or strongly similar to a β-1,4-endoglucanase gene (HG-eng-2), previously isolated from H. glycines. A subgroup of identical “HG-eng-2-like” clones had considerable differences in the 5′ untranslated region compared with HG-eng-2 and were designated HG-eng-3. One H. glycines genomic clone contained HG-eng-2 and HG-eng-3 full-length genes, separated by a distance of approximately 8 kb, and a second genomic clone contained two copies of HG-eng-2, separated by approximately 6.5 kb, suggesting the presence of endoglucanase gene clusters in H. glycines. The HG-eng-2 and HG-eng-3 genes were in opposite transcriptional orientation, with considerable nucleotide differences in their 5′ flanking regions. The highly conserved nucleotide sequence in the introns and exons and their close proximity within the genome suggest that HG-eng-2 and HG-eng-3 are the products of recent gene duplication and inversion. }, number={1}, journal={MOLECULAR PLANT-MICROBE INTERACTIONS}, author={Yan, YT and Smant, G and Davis, E}, year={2001}, month={Jan}, pages={63–71} }
 @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} }
 @article{de boer_yan_smant_davis_baum_1998, title={In-situ hybridization to messenger RNA in Heterodera glycines}, volume={30}, number={3}, journal={Journal of Nematology}, author={De Boer, J. M. and Yan, Y. and Smant, G. and Davis, E. L. and Baum, T. J.}, year={1998}, pages={309–312} }
 @article{ito_yan_1998, title={Viscous scalar conservation law with nonlinear flux feedback and global attractors}, volume={227}, ISSN={["0022-247X"]}, DOI={10.1006/jmaa.1998.6016}, abstractNote={Abstract In this paper we study the forced viscous scalar conservation law on (0, 1) with the nonlinear flux feedback at the boundary. Global existence and uniqueness are established for L ∞ bounded initial conditions and forcing functions. Under an appropriate growth condition on the flux function and nonlinear dissipation at the boundary, we show the existence of an absorbing set that absorbs the whole space L ∞ (0, 1), and the existence of a compact global attractor in the L ∞ topology.}, number={1}, journal={JOURNAL OF MATHEMATICAL ANALYSIS AND APPLICATIONS}, author={Ito, K and Yan, Y}, year={1998}, month={Nov}, pages={271–299} }