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1.
Microbiol Spectr ; 11(1): e0398722, 2023 02 14.
Artigo em Inglês | MEDLINE | ID: mdl-36625649

RESUMO

In this paper, a total of 26 pestalotioid isolates associated with different medicinal plants from southwest China and Thailand were studied. Based on morphological examinations and multigene analyses of three gene loci (ITS, tef1-α, and tub2), these 26 isolates represent 17 species distributed in three genera, including seven new species and eight new records. The concatenated three loci tree was used to infer the occurrence of sexual recombination within each pestalotioid genus through the pairwise homoplasy index (PHI) test implemented in SplitsTree. Further, simplifying the description of pestalotioid species is discussed, and a checklist for pestalotioid species associated with medicinal plants worldwide is provided. IMPORTANCE Pestalotioid species are an important fungal group, occurring commonly as plant pathogens, endophytes, and saprophytes. The study of pestalotioid species associated with medicinal plants is significant for agriculture, industry, and pharmaceutical industry but remains poorly studied. In this study, we report 17 pestalotioid species related to medicinal plants based on morphology and molecular analyses. Our study significantly enriches the species richness of pestalotioids and provides a basis for follow-up studies.


Assuntos
Plantas Medicinais , Filogenia , Tailândia , China , Endófitos
2.
Zhonghua Shao Shang Za Zhi ; 33(3): 190-192, 2017 Mar 20.
Artigo em Chinês | MEDLINE | ID: mdl-28316170

RESUMO

Previous studies have demonstrated that integrin-linked kinases (ILKs) are abundantly expressed in extracellular matrix (ECM) riche dermis, hair follicles, and basal cells of epidermis. ILKs are not only essential for the maintenance of skin structure, but also play important roles in wound healing. ILKs can promote the formation of granulation tissue by stimulating the proliferation of fibroblasts and secretion of ECM, accelerate wound contraction by inducing the differentiation of fibroblasts to myofibroblasts, and boost reepithelization by promoting proliferation, migration, and differentiation of keratinocytes and follicle epidermal stem cells.


Assuntos
Adesão Celular/fisiologia , Fibroblastos/fisiologia , Integrinas/metabolismo , Queratinócitos/metabolismo , Proteínas Serina-Treonina Quinases/metabolismo , Pele/metabolismo , Cicatrização/fisiologia , Animais , Diferenciação Celular , Movimento Celular , Derme/fisiologia , Epiderme , Células Epiteliais/fisiologia , Matriz Extracelular , Humanos , Pele/patologia , Células-Tronco/metabolismo
3.
Proc Natl Acad Sci U S A ; 93(5): 2065-70, 1996 Mar 05.
Artigo em Inglês | MEDLINE | ID: mdl-8700886

RESUMO

The kinetics of amyloid fibril formation by beta-amyloid peptide (Abeta) are typical of a nucleation-dependent polymerization mechanism. This type of mechanism suggests that the study of the interaction of Abeta with itself can provide some valuable insights into Alzheimer disease amyloidosis. Interaction of Abeta with itself was explored with the yeast two-hybrid system. Fusion proteins were created by linking the Abeta fragment to a LexA DNA-binding domain (bait) and also to a B42 transactivation domain (prey). Protein-protein interactions were measured by expression of these fusion proteins in Saccharomyces cerevisiae harboring lacZ (beta-galactosidase) and LEU2 (leucine utilization) genes under the control of LexA-dependent operators. This approach suggests that the Abeta molecule is capable of interacting with itself in vivo in the yeast cell nucleus. LexA protein fused to the Drosophila protein bicoid (LexA-bicoid) failed to interact with the B42 fragment fused to Abeta, indicating that the observed Abeta-Abeta interaction was specific. Specificity was further shown by the finding that no significant interaction was observed in yeast expressing LexA-Abeta bait when the B42 transactivation domain was fused to an Abeta fragment with Phe-Phe at residues 19 and 20 replaced by Thr-Thr (AbetaTT), a finding that is consistent with in vitro observations made by others. Moreover, when a peptide fragment bearing this substitution was mixed with native Abeta-(1-40), it inhibited formation of fibrils in vitro as examined by electron microscopy. The findings presented in this paper suggest that the two-hybrid system can be used to study the interaction of Abeta monomers and to define the peptide sequences that may be important in nucleation-dependent aggregation.


Assuntos
Peptídeos beta-Amiloides/metabolismo , Proteínas de Homeodomínio , Ligação Proteica , Transativadores , Doença de Alzheimer , Proteínas de Bactérias/metabolismo , Sequência de Bases , Primers do DNA/química , Proteínas de Drosophila , Escherichia coli , Humanos , Hormônios de Inseto/metabolismo , Substâncias Macromoleculares , Microscopia Eletrônica , Dados de Sequência Molecular , Proteínas Recombinantes de Fusão/metabolismo , Proteínas Recombinantes , Saccharomyces cerevisiae , Serina Endopeptidases/metabolismo
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