Search Results - "Matias, P M"

Environmental enrichment for captive stumptail macaques (Macaca arctoides) by Márquez-Arias, A., Santillán-Doherty, A.M., Arenas-Rosas, R.V., Gasca-Matías, M.P., Muñoz-Delgado, J.

“…Background  The behavior of animals is modified by captivity. Environmental enrichment (EE) is a program designed to enhance the welfare of confined animals by…”
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Roles of Escherichia coli ZinT in cobalt, mercury and cadmium resistance and structural insights into the metal binding mechanism by Colaço, H G, Santo, P E, Matias, P M, Bandeiras, T M, Vicente, J B

“…Escherichia coli ZinT is a metal binding protein involved in zinc homeostasis, with additional putative functions in the resistance against other metals…”
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Oxovanadium(IV) complexes with aromatic aldehydes by Costa Pessoa, J, Cavaco, I, Correia, I, Tomaz, I, Duarte, T, Matias, P.M

“…The synthesis, structure and spectroscopic properties of complexes with the formula [V IVO(dsal) 2(H 2O)], where Hdsal=salicylaldehyde, o-vanillin and…”
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Structure of Met30 variant of transthyretin and its amyloidogenic implications by Terry, C.J., Damas, A.M., Oliveira, P., Saraiva, M.J., Alves, I.L., Costa, P.P., Matias, P.M., Sakaki, Y., Blake, C.C.

“…Familial amyloidotic polyneuropathy (FAP) is an autosomal dominant hereditary type of lethal amyloidosis involving single (or double) amino acid substitutions…”
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Structural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutations by Matias, P M, Donner, P, Coelho, R, Thomaz, M, Peixoto, C, Macedo, S, Otto, N, Joschko, S, Scholz, P, Wegg, A, Bäsler, S, Schäfer, M, Egner, U, Carrondo, M A

“…The crystal structures of the human androgen receptor (hAR) and human progesterone receptor ligand-binding domains in complex with the same ligand metribolone…”
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Management of Stress Urinary Incontinence With Pelvic Floor Muscle Training for a Woman With Charcot-Marie-Tooth Disease: A Case Report by Ferreira, Letícia A., Fitz, Fátima F., Gimenez, Márcia M., Matias, Mayanni M.P., Bortolini, Maria A.T., Castro, Rodrigo A.

“…The purpose of this report is to describe the effects of pelvic floor muscle training (PFMT) in stress urinary incontinence (SUI) of a woman with…”
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The nature of the di-iron site in the bacterioferritin from Desulfovibrio desulfuricans by Carrondo, Maria A, Macedo, Sofia, Romão, Célia V, Mitchell, Edward, Matias, Pedro M, Liu, Ming Y, Xavier, António V, LeGall, Jean, Teixeira, Miguel, Lindley, Peter

“…The first crystal structure of a native di-iron center in an iron-storage protein (bacterio)ferritin is reported. The protein, isolated from the anaerobic…”
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Improving the oxygen tolerance in a highly active [NiFeSe] hydrogenase by Coito, A. M., Fourmond, V., Léger, C., Pereira, I. A. C., Matias, P. M.

“…Abstract only…”
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Preliminary crystallographic analysis of the oxidized form of a two mono‐nuclear iron centres protein from desulfovibrio desulfuricans ATCC 27774 by Coelho, Ana V., Matias, Pedro M., Carrondo, Maria A., Tavares, P., Moura, J. J. G., Moura, Isabel, Fülop, V., Hajdu, J., Le Gall, Jean

“…Crystals of the fully oxidized form of desulfoferrodoxin were obtained by vapor diffusion from a solution containing 20% PEG 4000, 0.1 M HEPES buffer, pH 7.5,…”
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Cytochrome c3 from Desulfovibrio gigas: Crystal structure at 1.8 Å resolution and evidence for a specific calcium‐binding site by Matias, Pedro M., Morais, José, Coelho, Ricardo, Carrondo, Maria Arménia, Wilson, Keith, Dauter, Zbigniew, Sieker, Larry

“…Crystals of the tetraheme cytochrome c3 from sulfate‐reducing bacteria Desulfovibrio gigas (Dg) (MW 13 kDa, 111 residues, four heme groups) were obtained and…”
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Redox-Bohr and other cooperativity effects in the nine-heme cytochrome C from Desulfovibrio desulfuricans ATCC 27774: crystallographic and modeling studies by Bento, Isabel, Teixeira, Vitor H, Baptista, António M, Soares, Cláudio M, Matias, Pedro M, Carrondo, Maria A

“…The nine-heme cytochrome c is a monomeric multiheme cytochrome found in Desulfovibrio desulfuricans ATCC 27774. The polypeptide chain comprises 296 residues…”
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Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough by Rodrigues, M. L., Oliveira, T., Matias, P. M., Martins, I. C., Valente, F. M. A., Pereira, I. A. C., Archer, M.

“…The cytochrome c nitrite reductase (cNiR) isolated from Desulfovibrio vulgaris Hildenborough is a membrane‐bound complex formed of NrfA and NrfH subunits. The…”
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The primary and three-dimensional structures of a nine-haem cytochrome c from Desulfovibrio desulfuricans ATCC 27774 reveal a new member of the Hmc family by Matias, Pedro M, Coelho, Ricardo, Pereira, Inês AC, Coelho, Ana V, Thompson, Andrew W, Sieker, Larry C, Gall, Jean Le, Carrondo, Maria Arménia

“…Background: Haem-containing proteins are directly involved in electron transfer as well as in enzymatic functions. The nine-haem cytochrome c (9Hcc),…”
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Conformational Component in the Coupled Transfer of Multiple Electrons and Protons in a Monomeric Tetraheme Cytochrome by Louro, Ricardo O., Bento, Isabel, Matias, Pedro M., Catarino, Teresa, Baptista, António M., Soares, Cláudio M., Carrondo, Maria Arménia, Turner, David L., Xavier, António V.

“…Cell metabolism relies on energy transduction usually performed by complex membrane-spanning proteins that couple different chemical processes, e.g. electron…”
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Three-Dimensional Structure of an Oncogene Protein: Catalytic Domain of Human c-H-ras p21 by De Vos, Abraham M., Tong, Liang, Milburn, Michael V., Matias, Pedro M., Jancarik, Jarmila, Noguchi, Shigeru, Nishimura, Susumu, Miura, Kazunobu, Ohtsuka, Eiko, Kim, Sung-Hou

“…The crystal structure at 2.7 Å resolution of the normal human c-H-ras oncogene protein lacking a flexible carboxyl-terminal 18 residue reveals that the protein…”
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Synthesis, anticonvulsant properties and pharmacokinetic profile of novel 10,11-dihydro-10-oxo-5H-dibenz/b,f/azepine-5-carboxamide derivatives by Learmonth, David A, Benes, Jan, Parada, António, Hainzl, Dominik, Beliaev, Alexander, Bonifácio, Maria João, Matias, Pedro M, Carrondo, Maria A, Garrett, José, Soares-da-Silva, Patrı́cio

“…A series of novel derivatives of oxcarbazepine ( 5), 10,11-dihydro-10-oxo-5H-dibenz/b,f/azepine-5-carboxamide was synthesised and evaluated for their…”
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Roles of Escherichia coli ZinT in cobalt, mercury and cadmium resistance and structural insights into the metal binding mechanismElectronic supplementary information (ESI) available: Table S1 - Effect of metals on ZinT thermal denaturation profiles tested by differential scanning fluorimetry. Table S2 - Metal concentrations supplemented into growth medium of ΔzinT and ΔgalT Escherichia coli strains. Table S3 - Crystallographic data collection and processing statistics. Table S4 - Final refinemen by Colaço, H. G, Santo, P. E, Matias, P. M, Bandeiras, T. M, Vicente, J. B

“…Escherichia coli ZinT is a metal binding protein involved in zinc homeostasis, with additional putative functions in the resistance against other metals…”
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Roles of Escherichia coliZinT in cobalt, mercury and cadmium resistance and structural insights into the metal binding mechanism by Colaco, H G, Santo, P E, Matias, P M, Bandeiras, T M, Vicente, J B

“…Escherichia coliZinT is a metal binding protein involved in zinc homeostasis, with additional putative functions in the resistance against other metals…”
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Structure analysis of cytochrome c3 from Desulfovibrio vulgaris Hildenborough at 1.9 A resolution by Matias, P M, Frazão, C, Morais, J, Coll, M, Carrondo, M A

“…The three-dimensional X-ray structure of cytochrome c3 from sulfate-reducing bacteria Desulfovibrio vulgaris Hildenborough (DvH) (M(r) 13 kDa, 107 residues, 4…”
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Structure determination of bacterioferritin from Desulfovibrio desulfuricans by the MAD method at the Fe K-edge by Coelho, Ana V., Macedo, Sofia, Matias, Pedro M., Thompson, Andrew W., LeGall, Jean, Carrondo, Maria Arménia

“…Bacterioferritins constitute a subfamily of heme ferritins, proteins involved in iron storage and homeostasis. The protein isolated from Desulfovibrio…”
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