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| Tang,Hongmin; Zhou,Peifu. |
| In this study, heat shock protein, Hspa5 was cloned, expressed and purified subsequently confirmed that it interacted with the tyrosinase (TYR) in vitro. Then, using the crystal structure of the homologous protein from the bacteria as a template, a homology model of human TYR was constructed. This model was further applied to investigate the molecular docking with Hspa5. The model showed that the interaction between the TYR and Hspa5 was mainly maintained by some hydrogen bonds in a quite low energy state. The results indicated that TYR was protected in different denaturation conditions by Hspa5. It was concluded that Hspa5 served as a molecular chaperone of TYR, which could help to better understand the molecule regulation mechanism of TRY in many kinds... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Molecular chaperone; Hspa5; Tyrosinase; Melanin; Melanosome. |
| Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000400547 |
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| Carolino,Sonia Madali Boseja; Vaez,Juliana Rocha; Irsigler,André Southernman Teixeira; Valente,Maria Anete S.; Rodrigues,Leonardo Augusto Zebral; Fontes,Elizabeth Pacheco Batista. |
| In contrast to yeast or mammalian counterpart, BiP (Binding Protein) from several plant species, such as maize, tobacco, Arabidopsis and soybean, is encoded by a multigene family. A systematic characterization and analysis of soybean BiP expression have provided evidence for the existence of multiple, complex regulatory mechanisms controlling plant BiP gene expression. In support of this observation, the soybean BiP gene family has been shown to exhibit organ-specific expression and differential regulation in response to abiotic stresses through distinct signaling pathways. As a member of the stress-regulated HSP70 family of protein, the elucidation of plant BiP function and regulation is likely to lead do new strategies to enhance crop tolerance to... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Endoplasmic reticulum; ER stressors; Grp78; Molecular chaperone; Unfolded protein response; Water stress. |
| Ano: 2003 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1677-04202003000200001 |
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