about
Chromatographic behaviour of monoclonal antibodies against wild-type amidase from Pseudomonas aeruginosa on immobilized metal chelates.Optimization of microbial detoxification for an aquatic mercury-contaminated environment.Metabolomics for undergraduates: Identification and pathway assignment of mitochondrial metabolites.Preparation and physicochemical characterization of Ag nanoparticles biosynthesized by Lippia citriodora (Lemon Verbena).In vitro digestion, antioxidant and antiacetylcholinesterase activities of two species of Ruta: Ruta chalepensis and Ruta montana.Anaerobic reduction of a sulfonated azo dye, Congo Red, by sulfate-reducing bacteria.Measuring enzymatic activity of a recombinant amidase using Fourier transform infrared spectroscopy.Bioactivity studies and chemical profile of the antidiabetic plant Genista tenera.Characterization of monoclonal antibodies against altered (T103I) amidase from Pseudomonas aeruginosa.Isorhamnetin derivatives and piscidic acid for hypercholesterolemia: cholesterol permeability, HMG-CoA reductase inhibition, and docking studies.Glandular Trichomes and Biological Activities in Helichrysum italicum and H. stoechas, Two Asteraceae Species Growing Wild in Portugal.Application of Fourier transform infrared spectroscopy for monitoring hydrolysis and synthesis reactions catalyzed by a recombinant amidase.Interaction between Plectranthus barbatus herbal tea components and acetylcholinesterase: binding and activity studies.Function of Plectranthus barbatus herbal tea as neuronal acetylcholinesterase inhibitor.Kinetic properties of wild-type and altered recombinant amidases by the use of ion-selective electrode assay method.Isolation and characterization of mercury-resistant bacteria from sediments of Tagus Estuary (Portugal): implications for environmental and human health risk assessment.Application of empirical design methodologies to the study of the influence of reaction conditions and N-alpha-protecting group structure on the enzymatic X-Phe-Leu-NH(2) dipeptide synthesis in buffer/dimethylformamide solvents systems.Monoclonal antibodies recognize conformational epitopes on wild-type and recombinant mutant amidases from pseudomonas aeruginosa.The in vitro screening for acetylcholinesterase inhibition and antioxidant activity of medicinal plants from Portugal.Bifunctional phenolic-choline conjugates as anti-oxidants and acetylcholinesterase inhibitorsEffect of luteolin and apigenin on rosmarinic acid bioavailability in Caco-2 cell monolayersEvaluation of cholesterol absorption and biosynthesis by decoctions of Annona cherimola leavesAcetylcholinesterase inhibition, antioxidant activity and toxicity of Peumus boldus water extracts on HeLa and Caco-2 cell linesPhytochemical Characterization and Biological Evaluation of the Aqueous and Supercritical Fluid Extracts from Salvia sclareoides BrotDipeptide synthesis and separation in a reversed micellar membrane reactorBroad bean (Vicia faba L.) pods: a rich source of bioactive ingredients with antimicrobial, antioxidant, enzyme inhibitory, anti-diabetic and health-promoting propertiesImmobilized Metal Affinity Chromatography of Monoclonal Immunoglobulin M Against Mutant Amidase From Pseudomonas aeruginosaScreening of suitable immobilized metal chelates for adsorption of monoclonal antibodies against mutant amidase fromPseudomonas aeruginosaApplication of Factorial Design to the Optimization of Peroxidase Activity in Reverse Micelles of bis(2-ethylhexyl)Sodium Sulfosuccinate/ IsooctaneSynthesis of AcPheLeuNH2 by ?-chymotrypsin in TTAB reversed micelles: Application of response surface methodology to the optimization of the systemPeptide Synthesis by Microencapsulated ChymotrypsinImproved purification and properties of glucose dehydrogenase fromBacillus subtilis
P50
Q33825410-9E7B2435-ED30-4B96-8268-7342D1725F7EQ38604095-F3D9D40E-8AF1-4A80-A212-D4D4EF7D07F7Q40355677-B500ACB0-AFE2-4C3E-A55D-2526B0339364Q42959593-AE25EDDC-E331-4107-BBF8-34814F519396Q43029221-C9146222-87DE-4E18-857A-97222D07242AQ43985046-1A631909-2398-40B2-A381-CCFC1BA3D71AQ44641372-CF4E5D10-2915-4166-943E-4B6701BBE59EQ46186954-E083B547-B30A-49C4-A8AD-3CBCE321BB04Q46575349-EC91C8FD-79DA-4516-9E31-52C1D7CB94E4Q46646523-808F84B9-1C2D-4DC8-ACBE-351F0E0916BAQ46692519-B7F617A3-E0D0-4950-B1AE-6EEB5449A5EBQ46721755-34EA6969-2B22-4FE5-B12C-21CEE76A605FQ47379281-70FAC337-D83D-476D-8578-FF6BC5BF4F07Q49022359-FDD0C627-4298-40AB-BA2D-5B548AA8CF1AQ51174963-6369B3E2-4ADF-48DF-8717-1571CD498FEAQ51467672-1EF23951-F2A8-4996-9C0E-56EB5F56C64BQ52421675-A7BD543F-2ACC-492D-BB9F-22DA2B0ACE08Q52582596-79272B03-1186-4962-ABE9-EE96C8BE6715Q52805402-1EF42D8C-BA26-4E2F-AF73-FDD083A98773Q56933230-1163621C-BB98-4462-8250-C3C31CFD8B90Q58171867-3858EB8D-8DD1-4193-882C-EFAE24BA1348Q58171875-044A18CA-F653-4D27-8214-E51658548BD0Q58171882-DA42891B-AFFD-490F-B188-43D633A4F696Q58838073-A206432B-4F2D-4291-A1B5-A009E639A4F5Q58853472-AF34BEC0-7FEF-45CD-AF4F-917B129D8BEAQ61809208-F2C606C0-29A0-4A3E-B8C2-2163EB23C004Q61809432-801FE75A-1A91-4B7A-A3B1-37BC3C79FC7EQ61809458-3E43F2DF-BCB3-4E86-BDA5-00A14C5399C2Q61809524-7D5965EE-0385-43FC-A6AE-7BB120A1F81FQ61809569-3343D12E-23F6-48AF-B588-03D8E1B418F2Q61809601-4CCC2EB9-E912-4132-AE81-1AE9880F83BEQ61809631-DF01323A-20A5-4292-8820-84E807B82805
P50
description
hulumtuese
@sq
researcher
@en
ricercatrice
@it
wetenschapper
@nl
հետազոտող
@hy
name
Maria L. Serralheiro
@ast
Maria L. Serralheiro
@en
Maria L. Serralheiro
@es
Maria L. Serralheiro
@nl
Maria L. Serralheiro
@sl
type
label
Maria L. Serralheiro
@ast
Maria L. Serralheiro
@en
Maria L. Serralheiro
@es
Maria L. Serralheiro
@nl
Maria L. Serralheiro
@sl
prefLabel
Maria L. Serralheiro
@ast
Maria L. Serralheiro
@en
Maria L. Serralheiro
@es
Maria L. Serralheiro
@nl
Maria L. Serralheiro
@sl
P214
P1053
E-3407-2012
P106
P1153
6602688573
P21
P213
0000 0000 6921 5174
P214
P31
P3829
P496
0000-0001-7541-9613
P735
P7859
viaf-99713816