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Conserved amino acids near the carboxy terminus of bacterial tyrosyl-trna synthetase are involved in trna and tyr-amp bindingFEBS LETTERSFEBS LETT
(ELSEVIER SCIENCE PUBLISHERS B.V., 2017)
Role of the carboxyl terminus on the catalytic activity of protein kinase ck2 alpha subunitFEBS LETTERSFEBS LETT
(ELSEVIER SCIENCE PUBLISHERS B.V., 2017)
Effects of N-terminus Positive Charge on Invasive and Non-invasive Breast Cancer Cells
(Wiley-Blackwell, 2014)
The C-terminus of murine S100A9 inhibits hyperalgesia and edema induced by jararhagin
(Elsevier B.V., 2004-01-01)
The effect of a synthetic peptide (H-92-G(110)) identical to the C-terminus of murine S100A9 (mS100A9p) was investigated on hyperalgesia and edema induced by either jararhagin or papain in the rat paw. mS100A9p not only ...
Immunological profile of a Plasmodium vivax AMA-1 N-terminus peptide-carbon nanotube conjugate in an infected Plasmodium berghei mouse model
We have covalently conjugated an N-terminus Plasmodium vivax apical membrane antigen-1 (AMA-1) peptide to functionalized carbon nanotubes (f-CNT). Immunological characterization of this molecular conjugate revealed that ...
A degenerate primer allows amplification of part of the 3 '-terminus of three distinct carlavirus species
(Elsevier B.V., 2008-03-01)
Sequences of the coat protein amino acids of definitive and tentative species of carlaviruses deposited in GenBank were aligned and a region of seven amino acids (GLGVPTE) was found to be conserved. The corresponding ...
A degenerate primer allows amplification of part of the 3 '-terminus of three distinct carlavirus species
(Elsevier B.V., 2008-03-01)
Sequences of the coat protein amino acids of definitive and tentative species of carlaviruses deposited in GenBank were aligned and a region of seven amino acids (GLGVPTE) was found to be conserved. The corresponding ...
The N-terminal domain of Arabidopsis proline dehydrogenase affects enzymatic activity and protein oligomerization
(Elsevier France-Editions Scientifiques Medicales Elsevier, 2020-09)
Proline dehydrogenase (ProDH) is a flavoenzyme that catalyzes the oxidation of proline (Pro) into Δ1-pyrroline-5-carboxylate (P5C). In eukaryotes, ProDH coordinates with different Pro metabolism enzymes to control energy ...