Zobrazeno 1 - 10
of 22
pro vyhledávání: '"José M. Fernández-Abalos"'
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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The production of the cellulase Cell from Streptomyces halstedii JM8 was studied in cells grown in the presence of glucose, cellobiose or microcrystalline cellulose (Avicel). Among these, glucose repressed expression while cellobiose and Avicel exert
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c310a1dc8eef255adad3e1fca367ceb8
https://doi.org/10.1111/j.1574-6968.1997.tb10469.x
https://doi.org/10.1111/j.1574-6968.1997.tb10469.x
Autor:
Ramón I. Santamaría, Valery L. Shnyrov, Alberto Ruiz-Arribas, José M. Fernández-Abalos, Javier De Las Rivas, Sonia Rodríguez, Margarita Díaz
Publikováno v:
FEMS Microbiology Letters. 240:237-243
Mutagenesis of the xylanase Xys1 of Streptomyces halstedii JM8 has been done by error prone PCR. Mutants with modified hydrolytic activity were isolated, the recombinant variant proteins purified and the catalytic activities of each one determined an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cabd2bfbd9658345c5480a0dcc4e8dbd
https://doi.org/10.1016/j.femsle.2004.09.032
https://doi.org/10.1016/j.femsle.2004.09.032
Autor:
John H. Doonan, José M. Fernández-Abalos, P. Lunness, H. Fox, Nick D. Read, Patrick C. Hickey
Publikováno v:
Molecular Microbiology. 45:1219-1230
Summary Mutation of bimG, the major protein phosphatase 1 gene in Aspergillus nidulans, causes multiple cell cycle and hyphal growth defects that are associated with overphosphorylation of subcellular components. We have used functional translational
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b3c067b18a8aae6e0ae91cfb427d736d
https://doi.org/10.1046/j.1365-2958.2002.03092.x
https://doi.org/10.1046/j.1365-2958.2002.03092.x
Publikováno v:
Microbiology. 145:2221-2227
The enhanced green fluorescent protein (EGFP) gene is a modified version of the green fluorescent protein gene of the jellyfish Aequorea victoria with a codon usage that corresponds well to that found in many GC-rich streptomycete genes. Here the use
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::139b245938b718b3eccfb488cdfe19a5
https://doi.org/10.1099/00221287-145-9-2221
https://doi.org/10.1099/00221287-145-9-2221
Autor:
Juan J. Calvete, Galina G. Zhadan, Victor P. Kutyshenko, Alberto Ruiz-Arribas, Enrique Villar, Ramón I. Santamaría, Manuel Cortijo, José M. Fernández-Abalos, Valery L. Shnyrov
Publikováno v:
European Journal of Biochemistry. 253:462-468
In a continuation of our earlier study [Ruiz-Arribas, A., Santamaria, R.I., Zhadan, G. G., Villar, E. & Shnyrov, V. L. (1994) Differential scanning calorimetric study of the thermal stability of xylanase from Streptomyces halstedii JM8, Biochemistry
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::006e19a3050641bbbc7a8642e1f8b5e8
https://doi.org/10.1046/j.1432-1327.1998.2530462.x
https://doi.org/10.1046/j.1432-1327.1998.2530462.x
Autor:
José M. Fernández-Abalos, Margarita Díaz, Juan Soliveri, José Luis Copa-Patiño, Ramón I. Santamaría
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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El pdf del artículo es el manuscrito de autor.-- et al.
Xylanases are very often modular enzymes composed of one or more catalytic domains and carbohydrate-binding modules (CBMs) connected by a flexible linker region. Usually, when these protei
Xylanases are very often modular enzymes composed of one or more catalytic domains and carbohydrate-binding modules (CBMs) connected by a flexible linker region. Usually, when these protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8efa2dbaf49293216febd94750e39515
https://pubmed.ncbi.nlm.nih.gov/21181427
https://pubmed.ncbi.nlm.nih.gov/21181427
Autor:
Librada M. Canedo Hernandez, José M. Fernández-Abalos, Ignacio Trujillano, Margarita Díaz, Ramón I. Santamaría, Julian Castro Rodriguez, Gloria Gonzalez Holgado
Publikováno v:
ChemInform. 33
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ff73d05c3483e351d4691373be8289b0
https://doi.org/10.1002/chin.200240192
https://doi.org/10.1002/chin.200240192
Autor:
Alberto, Hernández, José C, López, Ramón, Santamaría, Margarita, Díaz, José M, Fernández-Abalos, José L, Copa-Patiño, Juan, Soliveri
Publikováno v:
International microbiology : the official journal of the Spanish Society for Microbiology. 11(2)
A DNA fragment from the lignocellulolytic actinomycete Streptomyces avermitilis CECT 3339 was cloned using a DNA probe from the xylanase gene xysA of Streptomyces halstedii. The nucleotide sequence analysis revealed two potential ORFs, xyl30 and hd30
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::94a92da55bda5f84ff83f83238867238
https://pubmed.ncbi.nlm.nih.gov/18645964
https://pubmed.ncbi.nlm.nih.gov/18645964
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
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10 páginas, 8 figuras, 1 tabla.-- El pdf del artículo es la versión post-print.
The secreted protein pattern of Streptomyces lividans depends on the carbon source present in the culture media. One protein that shows the most dramatic change i
The secreted protein pattern of Streptomyces lividans depends on the carbon source present in the culture media. One protein that shows the most dramatic change i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d7b13f9fc2bbbf6f86ce6d69866b2e5
https://pubmed.ncbi.nlm.nih.gov/16079337
https://pubmed.ncbi.nlm.nih.gov/16079337
Publikováno v:
Gene. 351
The expression of xysA, a gene encoding for an endoxylanase from Streptomyces halstedii JM8, is repressed by glucose. In order to define the regions involved in its regulation, several deletions were made in the 475 bp xysA promoter and were studied
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff48779e355285e0cd6302b7d4fde82c
https://pubmed.ncbi.nlm.nih.gov/15850758
https://pubmed.ncbi.nlm.nih.gov/15850758