Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Erminia Barboni"'
Publikováno v:
Biochemistry. 40:4859-4866
Galectin-3, a beta-galactoside binding protein, contains a C-terminal carbohydrate recognition domain (CRD) and an N-terminal domain that includes several repeats of a proline-tyrosine-glycine-rich motif. Earlier work based on a crystal structure of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c28e71bbb0f047d8e7ca3db29fbd93d5
https://doi.org/10.1021/bi002907f
https://doi.org/10.1021/bi002907f
Publikováno v:
Glycoconjugate Journal. 16:365-373
Galectin 3, a β-galactoside binding protein, contains a C-terminal carbohydrate recognition domain (CRD) and an N-terminal segment including multiple repeats of a proline/tyrosine/glycine-rich motif. Previous work has shown that galectin 3 but not t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8e489f2a18a347de0477cb870f5b8f71
https://doi.org/10.1023/a:1007004330048
https://doi.org/10.1023/a:1007004330048
Autor:
F. Bernardo Pliego Rivero, Ann Marie Gormley, P. John Seeley, Roger J. Morris, Marie-Catherine Tiveron, Frank Grosveld, Erminia Barboni
Publikováno v:
Nature. 355:745-748
THY-1, the smallest member of the immunoglobulin superfamily1, is a major cell-surface component expressed by several tissues2. The protein1carbohydrate3 and gene4 structures of this molecule are known, yet its function is not. It is highly expressed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae08f9e3e8adf99bee1815af070d9aa8
https://doi.org/10.1038/355745a0
https://doi.org/10.1038/355745a0
Publikováno v:
FEBS letters. 579(30)
Understanding the molecular mechanism of host-pathogen interactions is the basis for drug design and vaccine development. The fine composition of mycolic acids (MA), the major constituents of Mycobacterium tuberculosis (Mtb) cell envelope, as well as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d1f21c49a9ac50646f4b9610dcf7d8a
https://pubmed.ncbi.nlm.nih.gov/16310777
https://pubmed.ncbi.nlm.nih.gov/16310777
Publikováno v:
Glycobiology. 10(11)
A model structure (Henrick,K., Bawumia,S., Barboni,E.A.M., Mehul,B. and Hughes, R.C. (1998) Glycobiology:, 8, 45-57) of the carbohydrate recognition domain (CRD, amino acid residues 114-245) of hamster galectin-3 has been extended to include N-termin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b2436f2217cd82093929addceed1965
https://pubmed.ncbi.nlm.nih.gov/11087712
https://pubmed.ncbi.nlm.nih.gov/11087712
Publikováno v:
Glycobiology. 8(1)
A model of the carbohydrate recognition domain CRD, residues 111-245, of hamster galectin-3 has been made using homology modeling and dynamics minimization methods. The model is based on the known x-ray structures of bovine galectin-1 and human galec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4a2e734a313e7ff2b9e2a74713fd407
https://pubmed.ncbi.nlm.nih.gov/9451013
https://pubmed.ncbi.nlm.nih.gov/9451013
Publikováno v:
European journal of biochemistry. 49(1)
Pantothenoylcysteine-4′-phosphate decarboxylase has been purified 700-fold from horse liver by by an improved method. Enzyme activity was determined by measuring the amount of labeled CO2 produced from the labeled cysteine moiety of the substrate m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4de9874ec6f2c56e5447a9ca46024893
https://pubmed.ncbi.nlm.nih.gov/4459135
https://pubmed.ncbi.nlm.nih.gov/4459135
Autor:
Erminia Barboni, Maria Anna Rosei, A. Fiori, Carla Borri Voltattorni, Maria D'Erme, Alba Minelli
The effect of a number of inhibitors of L-aromatic amino acid decarboxylase activity on the absorption spectrum of the enzyme-bound coenzyme has been studied. It has been observed that the compounds tested, even if devoid of the amino function and th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4149685559c159baea08e6aad32caeb7
http://hdl.handle.net/11562/7431
http://hdl.handle.net/11562/7431
Publikováno v:
European journal of biochemistry. 14(1)
The addition of sodium sulfide to disulfide-containing proteins dissolved in 0.01 N NaOH produces an absorption in the range of 320–350 nm similar to that exhibited by cystine or cystamine treated under the same conditions. Proteins free of cystine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56455adf14e661c924762e5d810a10cd
https://pubmed.ncbi.nlm.nih.gov/5447431
https://pubmed.ncbi.nlm.nih.gov/5447431