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1.
Staphylococcus aureus Does Not Synthesize Arginine from Proline under Physiological Conditions.
J Bacteriol
; 204(6): e0001822, 2022 06 21.
Artículo
en Inglés
| MEDLINE | ID: mdl-35546540
2.
Highly soluble and stable 'insertion domain' of the capsid penton base protein provides complete protection against infections caused by fowl adenoviruses.
Microb Pathog
; 173(Pt A): 105835, 2022 Dec.
Artículo
en Inglés
| MEDLINE | ID: mdl-36265735
3.
Characterization of the highly immunogenic VP2 protrusion domain as a diagnostic antigen for members of Birnaviridae family.
Appl Microbiol Biotechnol
; 104(8): 3391-3402, 2020 Apr.
Artículo
en Inglés
| MEDLINE | ID: mdl-32088761
4.
C-Terminal Domain of the Human Zinc Transporter hZnT8 Is Structurally Indistinguishable from Its Disease Risk Variant (R325W).
Int J Mol Sci
; 21(3)2020 Jan 31.
Artículo
en Inglés
| MEDLINE | ID: mdl-32023808
5.
In silico designed Staphylococcus aureus B-cell multi-epitope vaccine did not elicit antibodies against target antigens suggesting multi-domain approach.
J Immunol Methods
; 504: 113264, 2022 05.
Artículo
en Inglés
| MEDLINE | ID: mdl-35341759
6.
Ftsh Sensitizes Methicillin-Resistant Staphylococcus aureus to ß-Lactam Antibiotics by Degrading YpfP, a Lipoteichoic Acid Synthesis Enzyme.
Antibiotics (Basel)
; 10(10)2021 Oct 01.
Artículo
en Inglés
| MEDLINE | ID: mdl-34680778
7.
Identification of potent epitopes on hexon capsid protein and their evaluation as vaccine candidates against infections caused by members of Adenoviridae family.
Vaccine
; 39(27): 3560-3564, 2021 06 16.
Artículo
en Inglés
| MEDLINE | ID: mdl-34030897
8.
In silico epitope prediction and immunogenic analysis for penton base epitope-focused vaccine against hydropericardium syndrome in chicken.
Virus Res
; 273: 197750, 2019 11.
Artículo
en Inglés
| MEDLINE | ID: mdl-31509776
9.
Overexpression and characterization of the 100K protein of Fowl adenovirus-4 as an antiviral target.
Virus Res
; 238: 218-225, 2017 06 15.
Artículo
en Inglés
| MEDLINE | ID: mdl-28666898
10.
Correction: Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production.
PLoS One
; 11(7): e0160128, 2016.
Artículo
en Inglés
| MEDLINE | ID: mdl-27442507
11.
Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production.
PLoS One
; 11(4): e0153436, 2016.
Artículo
en Inglés
| MEDLINE | ID: mdl-27093053
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