Structure and calcium binding activity of LipL32, the major surface antigen of pathogenic Leptospira sp. (2010)
- Authors:
- USP affiliated authors: FARAH, SHAKER CHUCK - IQ
- Unidades: IQ
- Subjects: LEPTOSPIROSE; BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Activity Report 2009: LNLS/Brazilian Synchrotron Light Laboratory
- ISSN: 1518-0204
- Volume/Número/Paginação/Ano: p. 71-77, 2010
-
ABNT
HAUK, Pricila; GUZZO, Cristiane Rodrigues; ROMAN RAMOS, Henrique; HO, Paulo Lee; FARAH, Chuck Shaker. Structure and calcium binding activity of LipL32, the major surface antigen of pathogenic Leptospira sp. Activity Report 2009: LNLS/Brazilian Synchrotron Light Laboratory, Campinas, p. 71-77, 2010. Disponível em: < http://www.lnls.br/ar2009/PDF/sh11.pdf >. -
APA
Hauk, P., Guzzo, C. R., Roman Ramos, H., Ho, P. L., & Farah, C. S. (2010). Structure and calcium binding activity of LipL32, the major surface antigen of pathogenic Leptospira sp. Activity Report 2009: LNLS/Brazilian Synchrotron Light Laboratory, 71-77. Recuperado de http://www.lnls.br/ar2009/PDF/sh11.pdf -
NLM
Hauk P, Guzzo CR, Roman Ramos H, Ho PL, Farah CS. Structure and calcium binding activity of LipL32, the major surface antigen of pathogenic Leptospira sp. [Internet]. Activity Report 2009: LNLS/Brazilian Synchrotron Light Laboratory. 2010 ; 71-77.Available from: http://www.lnls.br/ar2009/PDF/sh11.pdf -
Vancouver
Hauk P, Guzzo CR, Roman Ramos H, Ho PL, Farah CS. Structure and calcium binding activity of LipL32, the major surface antigen of pathogenic Leptospira sp. [Internet]. Activity Report 2009: LNLS/Brazilian Synchrotron Light Laboratory. 2010 ; 71-77.Available from: http://www.lnls.br/ar2009/PDF/sh11.pdf - Stability of troponin I and T investigated by a hydrophobic fluorescent probe
- Calcium binding to Leptospira outer membrane antigen LipL32 is not necessary for its interaction with plasma fibronectin, collagen type IV, and plasminogen
- Ca2+-induced rolling of tropomyosin in muscle thin filaments - The alpha- and beta-band hypothesis revisited
- High-throughput screening of Xanthomonas axonopodis pv citri targets for structural proteomics using NMR
- Deciphering the head-to-tail complex of 'alpha'-tropomyosin using double mutant cycles and molecular docking
- Analyses of protein-protein interactions involving Xanthomonas axonopodis pv citri RNA polimerase sigma factors
- Strategy for determining the binding site of tropomyosin on actin
- A tropomyosin mutant containing a intrinsic fluorescent probe may be used to study head-to-tail interaction thermodynamics
- New protein fold from Xanthomonas axonopodis pv citri YaeQ
- A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
