Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Akkaladevi Narahari"'
Autor:
Machen, Alexandra J.1 amachen@kumc.edu, Akkaladevi, Narahari2 akkaladevin@missouri.edu, Trecazzi, Caleb1 ctrecazzi@kumc.edu, O'Neil, Pierce T.1 poneil@kumc.edu, Mukherjee, Srayanta1 srayanta@gmail.com, Qi, Yifei3, Dillard, Rebecca4 rdillard@gmail.com, Wonpil Im3 woi216@lehigh.edu, Gogol, Edward P.5 gogole@umkc.edu, White, Tommi A.2 whiteto@missouri.edu, Fisher, Mark T.1 mfisher1@kumc.edu
Publikováno v:
Toxins. Oct2017, Vol. 9 Issue 10, p298. 16p.
Autor:
Avadhesha Surolia, Bipin Singh, Akkaladevi Narahari, Musti J. Swamy, Kishore Babu Bobbili, Gopalakrishnan Bulusu
Publikováno v:
International journal of biological macromolecules. 137
CIA17 is a PP2-like, homodimeric lectin made up of 17 kDa subunits present in the phloem exudate of ivy gourd ( Coccinia indica ). Isothermal titration calorimetric (ITC) studies on the interaction of chitooligosaccharides [(GlcNAc) 2–6 ] showed th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f00fb936b91e3ec999b763281a7a06ec
https://pubmed.ncbi.nlm.nih.gov/31260764
https://pubmed.ncbi.nlm.nih.gov/31260764
Akademický článek
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Akademický článek
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Autor:
Kaushal Sharma, Musti J. Swamy, Avadhesha Surolia, Michael Mormann, Kishore Babu Bobbili, Akkaladevi Narahari, Gottfried Pohlentz
Publikováno v:
International journal of biological macromolecules. 108
Phloem protein-2 (PP2) is an abundant soluble protein in the sieve elements in plants. Its lectin property was reported in various species. The primary structure of a 17 kDa PP2 from Coccinia indica (Coccinia indica agglutinin, CIA17), determined by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3e1cda7bd17a3cfe8e958ef06ec23dc
https://pubmed.ncbi.nlm.nih.gov/29126937
https://pubmed.ncbi.nlm.nih.gov/29126937
Akademický článek
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Publikováno v:
Biochimie. 93:1676-1684
A new lectin has been purified to homogeneity from the phloem exudate of snake gourd (Trichosanthes anguina) by affinity chromatography on chitin. The snake gourd phloem lectin (SGPL) specifically binds chitooligosaccharides and their inhibitory pote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1df0893ee6b89b582d2a7201f6a7413
https://doi.org/10.1016/j.biochi.2011.05.032
https://doi.org/10.1016/j.biochi.2011.05.032
Autor:
Ritwik Samanta, Sanjeev P. Mahanta, Sauradip Chaudhuri, Pradeepta K. Panda, Akkaladevi Narahari
Publikováno v:
Inorganica Chimica Acta. 372:281-285
Calix[4]pyrrole bearing catechol-derived diether strap linked via alkyl chains has been synthesized and characterized for the first time. The strap with 1,2-diether link is providing a relatively constrained geometry on its side of the calix[4]pyrrol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d5499835ba95a76a812554d6b3e0abdb
https://doi.org/10.1016/j.ica.2011.02.004
https://doi.org/10.1016/j.ica.2011.02.004
Autor:
Musti J. Swamy, Pavan Kumar Nareddy, Hitesh Singla, Avadhesha Surolia, Akkaladevi Narahari, Gopalakrishnan Bulusu
Publikováno v:
The Journal of Physical Chemistry B. 115:4110-4117
The interaction of chitooligosaccharides [(GlcNAc)(2-6)] with pumpkin phloem exudate lectin (PPL) was investigated by isothermal titration calorimetry and computational methods. The dimeric PPL binds to (GlcNAc)(3-5) with binding constants of 1.26-1.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d799ded4905b3bfae35ffa5770c50a79
https://doi.org/10.1021/jp110468n
https://doi.org/10.1021/jp110468n
Autor:
Musti J. Swamy, Akkaladevi Narahari
Publikováno v:
Journal of Photochemistry and Photobiology B: Biology. 97:40-47
The exposure and accessibility of the tryptophan residues in the chitooligosaccharide-specific pumpkin (Cucurbita maxima) phloem exudate lectin (PPL) have been investigated by fluorescence spectroscopy. The emission lambda(max) of native PPL, seen at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::245795e11f5fd85cafb5483a8b35d535
https://doi.org/10.1016/j.jphotobiol.2009.07.008
https://doi.org/10.1016/j.jphotobiol.2009.07.008