Zobrazeno 1 - 10
of 57
pro vyhledávání: '"Claudi M. Cuchillo"'
Publikováno v:
Biochemistry. 50:7835-7841
Fifty years ago, the group of Tony Mathias and Bob Rabin at University College London deduced the first mechanism for catalysis by an enzyme, ribonuclease [Findlay, D., Herries, D. G., Mathias, A. P., Rabin, B. R., and Ross, C. A. (1961) Nature 190,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36737b383c63fef9c7b0aa5c119efcfa
https://doi.org/10.1021/bi201075b
https://doi.org/10.1021/bi201075b
Publikováno v:
Protein Science. 11:117-128
Bovine pancreatic ribonuclease (RNase A, EC 3.1.27.5) has been studied extensively (e.g., see D'Alessio and Riordan 1997; Raines 1998). However, fine kinetic analysis of its specificity has always been hampered by the enormous complexity of its subst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::718bd4107d872c7f2cc7d84b083bf25f
https://doi.org/10.1110/ps.13702
https://doi.org/10.1110/ps.13702
Publikováno v:
International Journal of Peptide and Protein Research. 16:241-244
The n.m.r. spectra of native S-peptide and of S-peptide II, a derivative obtained after reaction of bovine pancreatic ribonuclease A with 6-chloropurine riboside 5'-monophosphate, both in D2O and in urea-d4, were obtained with a 270 MHz Fourier trans
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c669e182ca705a1b2d0836b2a6e1ece9
https://doi.org/10.1111/j.1399-3011.1980.tb02582.x
https://doi.org/10.1111/j.1399-3011.1980.tb02582.x
Publikováno v:
ResearcherID
The titration curves of the C-2 histidine protons of bovine pancreatic ribonuclease A in the presence of several dideoxynucleoside monophosphates (dNpdN) were studied by means of proton nuclear magnetic resonance at 270 MHz in order to obtain informa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a628caef4a274a804776cbf9514877de
https://doi.org/10.1111/j.1399-3011.1988.tb00912.x
https://doi.org/10.1111/j.1399-3011.1988.tb00912.x
Autor:
Antoni Benito, Maria Vilanova, Montserrat Rodríguez, M.V. Nogués, Claudi M. Cuchillo, M. Moussaoui
Publikováno v:
Archives of Biochemistry and Biophysics. 471:191-197
Analyzing the pattern of oligonucleotide formation induced by HP-RNase cleavage shows that the enzyme does not act randomly and follows a more endonucleolytic pattern when compared to RNase A. The enzyme prefers the binding and cleavage of longer sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e8df53185a4e52cab6bf2d94c6ce35b
https://doi.org/10.1016/j.abb.2007.12.016
https://doi.org/10.1016/j.abb.2007.12.016
Publikováno v:
Cellular and Molecular Life Sciences. 65:324-337
Human eosinophil cationic protein (ECP)/ ribonuclease 3 (RNase 3) is a protein secreted from the secondary granules of activated eosinophils. Specific properties of ECP contribute to its cytotoxic activities associated with defense mechanisms. In thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82ea139da05084b050f195a6c89d6ee4
https://doi.org/10.1007/s00018-007-7499-7
https://doi.org/10.1007/s00018-007-7499-7
Autor:
Maria Vilanova, Víctor Buzón, Josep Cladera, Claudi M. Cuchillo, Marc Ribó, M. Victòria Nogués, Zoran Nikolovski, Mohammed Moussaoui
Publikováno v:
Protein Science. 15:2816-2827
Eosinophil cationic protein (ECP)/ribonuclease 3 is a member of the RNase A superfamily involved in inflammatory processes mediated by eosinophils. ECP is bactericidal, helminthotoxic, and cytotoxic to tracheal epithelium cells and to several mammali
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce44ee30405a2e39fe073e4e751ddb5b
https://doi.org/10.1110/ps.062196406
https://doi.org/10.1110/ps.062196406
Publikováno v:
Protein Science. 16:99-109
A general acid–base catalytic mechanism is responsible for the cleavage of the phosphodiester bonds of the RNA by ribonuclease A (RNase A). The main active site is formed by the amino acid residues His12, His119, and Lys41, and the process follows
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58c00c128ec68ff9dedbe38050358a3d
https://doi.org/10.1110/ps.062251707
https://doi.org/10.1110/ps.062251707
Autor:
M.V. Nogués, H.R Evans, Ester Boix, K.R. Acharya, Zoran Nikolovski, Claudi M. Cuchillo, C.G. Mohan
Publikováno v:
Biochemistry. 41:12100-12106
Eosinophil cationic protein (ECP) is a component of the eosinophil granule matrix. It shows marked toxicity against helminth parasites, bacteria single-stranded RNA viruses, and host epithelial cells. Secretion of human ECP is related to eosinophil-a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::43163cff665ae85746c7801910641a96
https://doi.org/10.1021/bi0264521
https://doi.org/10.1021/bi0264521
Publikováno v:
Cellular and Molecular Life Sciences (CMLS). 54:766-774
The enzymatic catalysis of polymeric substrates such as proteins, polysaccharides or nucleic acids requires precise alignment between the enzyme and the substrate regions flanking the region occupying the active site. In the case of ribonucleases, en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f2aafc96a3bf05ea69a98921650fc53
https://doi.org/10.1007/s000180050205
https://doi.org/10.1007/s000180050205