Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Michel E Goldberg"'
Autor:
Gabriel L C Nunes, Alyne Simões, Fábio H Dyszy, Claudio S Shida, Maria A Juliano, Luiz Juliano, Tarsis F Gesteira, Helena B Nader, Gillian Murphy, Alain F Chaffotte, Michel E Goldberg, Ivarne L S Tersariol, Paulo C Almeida
Publikováno v:
PLoS ONE, Vol 6, Iss 6, p e21525 (2011)
Heparin has been shown to regulate human neutrophil elastase (HNE) activity. We have assessed the regulatory effect of heparin on Tissue Inhibitor of Metalloproteases-1 [TIMP-1] hydrolysis by HNE employing the recombinant form of TIMP-1 and correlate
Externí odkaz:
https://doaj.org/article/afc48b67b6e64ee1ad314b993234f385
Autor:
Jian-Hua Li, María Luisa Tasayco, Michel E. Goldberg, Roxana E. Georgescu, Alain F. Chaffotte
Publikováno v:
Biochemistry. 36:16040-16048
The disordered N- (1-73) and C- (74-108) fragments of oxidized Escherichia colithioredoxin (Trx) reconstitute the native structure upon association [Tasayco, M. L., & Chao, K. (1995) Proteins: Struct., Funct., Genet. 22, 41-44]. Kinetic measurements
Publikováno v:
Journal of Immunological Methods. 170:167-175
A reliable, convenient ELISA based method has been developed for measuring the dissociation rate constants of antigen/antibody complexes in solution. Its rationale is as follows: a solution containing the preformed antigen/antibody complex is diluted
Autor:
Michel E, Goldberg, Alain F, Chaffotte
Publikováno v:
Protein Science
Protein Science, Wiley, 2005, 14 (11), pp.2781-92. ⟨10.1110/ps.051678205⟩
Protein Science, 2005, 14 (11), pp.2781-92. ⟨10.1110/ps.051678205⟩
Protein Science, Wiley, 2005, 14 (11), pp.2781-92. ⟨10.1110/ps.051678205⟩
Protein Science, 2005, 14 (11), pp.2781-92. ⟨10.1110/ps.051678205⟩
Water from the solvent very strongly absorbs light in the frequency range of interest for studying protein structure by infrared (IR) spectroscopy. This renders handling of the observation cells painstaking and time consuming, and limits the reproduc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::7a473051b6b808e8511c1b617641646c
https://hal-pasteur.archives-ouvertes.fr/pasteur-00553614
https://hal-pasteur.archives-ouvertes.fr/pasteur-00553614
Autor:
Michel E, Goldberg
Publikováno v:
Medecine sciences : M/S. 21(6-7)
To probe the role of individual disulfide bonds in the folding kinetics of hen lysozyme, the variants with two mutations, C30A,C115A, C64A,C80A, and C76A,C94A, were constructed. The corresponding proteins, each lacking one disulfide bond, were produc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7395dbcf5e54280351a17d8322f8a15d
https://europepmc.org/articles/PMC2373558/
https://europepmc.org/articles/PMC2373558/
Publikováno v:
Protein science : a publication of the Protein Society. 8(12)
To investigate the role of some tertiary interactions, the disulfide bonds, in the early stages of refolding of hen lysozyme, we report the kinetics of reoxidation of denatured and reduced lysozyme under the same refolding conditions as those previou
Autor:
Yann Henry, Murielle Delepierre, Michel E. Goldberg, Cécile Wandersman, Nadia Izadi, Anne Lecroisey, Jean Haladjian
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 1997, 36 (23), pp.7050-7. ⟨10.1021/bi962577s⟩
Biochemistry, 1997, 36 (23), pp.7050-7. ⟨10.1021/bi962577s⟩
Biochemistry, American Chemical Society, 1997, 36 (23), pp.7050-7. ⟨10.1021/bi962577s⟩
Biochemistry, 1997, 36 (23), pp.7050-7. ⟨10.1021/bi962577s⟩
International audience; Many bacterial hemoproteins involved in heme acquisition have been isolated recently, comprising outer membrane receptors and extracellular heme-binding protein. The mechanisms by which these proteins extract heme have not bee
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b74cd3a37b27a641951251c94e914d8a
https://hal-pasteur.archives-ouvertes.fr/pasteur-00368062
https://hal-pasteur.archives-ouvertes.fr/pasteur-00368062
Publikováno v:
European Journal of Biochemistry
European Journal of Biochemistry, 1991, 201 (3), pp.681-93. ⟨10.1111/j.1432-1033.1991.tb16329.x⟩
European Journal of Biochemistry, Wiley, 1991, 201 (3), pp.681-93. ⟨10.1111/j.1432-1033.1991.tb16329.x⟩
European Journal of Biochemistry, 1991, 201 (3), pp.681-93. ⟨10.1111/j.1432-1033.1991.tb16329.x⟩
European Journal of Biochemistry, Wiley, 1991, 201 (3), pp.681-93. ⟨10.1111/j.1432-1033.1991.tb16329.x⟩
International audience; Two synthetic peptides from the beta 2 subunit of tryptophan synthase have been studied by 1H-NMR spectroscopy at 300 MHz. One peptide, His-Gly-Arg-Val-Gly-Ile-Tyr-Phe-Gly-Met-Lys (peptide 11; Ile, isoleucine) is antigenic and