Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Eric W. Odom"'
Publikováno v:
Comprehensive Glycoscience
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c289d17004a4ace701058e2c150ed663
https://doi.org/10.1016/b978-0-12-819475-1.00092-4
https://doi.org/10.1016/b978-0-12-819475-1.00092-4
Autor:
M. T. Elola, Eric W. Odom, Gerardo R. Vasta, Hafiz Ahmed, A. Snowden, Adam G. Marsh, Nilda E. Fink
Publikováno v:
Annals of the New York Academy of Sciences. 712:55-73
In recent years, the significant contributions from molecular research studies on animal lectins have elucidated structural aspects and provided clues not only to their evolution but also to their multiple biological functions. The experimental evide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::277436b5f5768cc09d8d05a3859a5be7
https://doi.org/10.1111/j.1749-6632.1994.tb33562.x
https://doi.org/10.1111/j.1749-6632.1994.tb33562.x
Publikováno v:
Journal of molecular biology. 401(2)
The plasma of the striped bass Morone saxatilis contains a fucose-specific lectin (MsaFBP32) that consists of two F-type carbohydrate recognition domains (CRDs) in tandem. The crystal structure of the complex of MsaFBP32 with l -fucose reported here
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::470b1629f6d4b653eda243f9819ba25e
https://pubmed.ncbi.nlm.nih.gov/20561530
https://pubmed.ncbi.nlm.nih.gov/20561530
Publikováno v:
Animal Lectins: A Functional View
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::81eca9d3e7e66fd4dd91b1384bc90633
https://doi.org/10.1201/9781420006971.ch31
https://doi.org/10.1201/9781420006971.ch31
Publikováno v:
Advances in experimental medicine and biology. 598
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d01d2510db540e01c810bee810f5b46d
https://pubmed.ncbi.nlm.nih.gov/17892226
https://pubmed.ncbi.nlm.nih.gov/17892226
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9780387717654
Lectins and other pattern recognition proteins are critical components of innate immune mechanisms in invertebrates and vertebrates. Unlike immunoglobulins, TCRs, and VLRs, which generate diversity in recognition by genetic recombination, lectins lik
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::077d271d551abd864fb57c02f5e4b4be
https://doi.org/10.1007/978-0-387-71767-8_27
https://doi.org/10.1007/978-0-387-71767-8_27
Publikováno v:
Comprehensive Glycoscience
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::68c394840733e91e1e66bea7fb0d17af
https://doi.org/10.1016/b978-044451967-2/00158-6
https://doi.org/10.1016/b978-044451967-2/00158-6
Autor:
Gigliola Benenati, Eric W. Odom, Nicolò Parrinello, Aiti Vizzini, Gerardo R. Vasta, Matteo Cammarata, Giuseppina Salerno
Publikováno v:
Biochimica et biophysica acta. 1770(1)
A novel fucose-binding lectin, designated SauFBP32, was purified by affinity chromatography on fucose-agarose, from the serum of the gilt head bream Sparus aurata. Electrophoretic mobility of the subunit revealed apparent molecular weights of 35 and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5666ef783c120a2db80af346f4488d96
https://pubmed.ncbi.nlm.nih.gov/17095163
https://pubmed.ncbi.nlm.nih.gov/17095163
Autor:
Gerardo R. Vasta, Eric W. Odom
Publikováno v:
The Journal of biological chemistry. 281(3)
Among other functions, lectins play an important role in the innate immune response of vertebrates and invertebrates by recognizing exposed glycans on the surface of potential pathogens. Despite the typically weak interaction of lectin domains with t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::730887ed7c5741d6e2af81146062c0bb
https://pubmed.ncbi.nlm.nih.gov/16251191
https://pubmed.ncbi.nlm.nih.gov/16251191
Publikováno v:
Current opinion in structural biology. 14(5)
During the past few years, substantial progress has been accomplished in the elucidation of the structural diversity of the lectin repertoires of invertebrates, protochordates and ectothermic vertebrates, providing particularly valuable information o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad5ec29e045526f82e6b5d0ae92e6076
https://pubmed.ncbi.nlm.nih.gov/15465324
https://pubmed.ncbi.nlm.nih.gov/15465324