`Beta´-2-glycoprotein I induces leakage from cardioliopin-containing vesicles by a non-fusion mechanism: binding, bilayer unsteady, aggregation and leakage (1998)
- Authors:
- Autor USP: GURALNIK, HERNAN CHAIMOVICH - IQ
- Unidade: IQ
- Assunto: BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Publisher place: Philadelphia
- Date published: 1998
- Source:
- Título do periódico: Arthritis and Rheumatism
- Volume/Número/Paginação/Ano: v. 41, n. 9, p. S168, 1998
- Conference titles: National Scientific Meeting
-
ABNT
CELLI, C M; CUCURUL, E; CHARAVI, A; CHAIMOVICH GURALNIK, Hernan. `Beta´-2-glycoprotein I induces leakage from cardioliopin-containing vesicles by a non-fusion mechanism: binding, bilayer unsteady, aggregation and leakage. Arthritis and Rheumatism[S.l: s.n.], 1998. -
APA
Celli, C. M., Cucurul, E., Charavi, A., & Chaimovich Guralnik, H. (1998). `Beta´-2-glycoprotein I induces leakage from cardioliopin-containing vesicles by a non-fusion mechanism: binding, bilayer unsteady, aggregation and leakage. Arthritis and Rheumatism. Philadelphia. -
NLM
Celli CM, Cucurul E, Charavi A, Chaimovich Guralnik H. `Beta´-2-glycoprotein I induces leakage from cardioliopin-containing vesicles by a non-fusion mechanism: binding, bilayer unsteady, aggregation and leakage. Arthritis and Rheumatism. 1998 ; 41( 9): S168. -
Vancouver
Celli CM, Cucurul E, Charavi A, Chaimovich Guralnik H. `Beta´-2-glycoprotein I induces leakage from cardioliopin-containing vesicles by a non-fusion mechanism: binding, bilayer unsteady, aggregation and leakage. Arthritis and Rheumatism. 1998 ; 41( 9): S168. - Peg changes the fusion pattern in the case of unmodified fusogenic peptides
- Micelar and vesicular effects on reaction mechanisms
- Sera from patients with chronic chagas' disease may exhibit anti-cardiolipin activity
- Effect of the treatment with neuraminidase the behavior of alkaline phosphatase in micelles
- Entrevista com o Prof. Hernan Chaimovich
- Autonomia?
- Pesquisa a serviço do desenvolvimento
- Prefácio da 1ª edição
- Estrutura e reatividade em micelas
- Stability and activity modulation of chymotrypsin in AOT reserved micelles by protein-interface interaction of ALPHA-chymotrypsin with a negative interface leads to cooperative breakage of a salt bridge that keeps the catalytic active conformation [ILe (16) - Asp(194)]
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