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Local heat-shock mediated multi-color labeling visualizing behaviors of enteric neural crest cells associated with division and neurogenesis in zebrafish gut.

08:00 EDT 8th April 2019 | BioPortfolio

Summary of "Local heat-shock mediated multi-color labeling visualizing behaviors of enteric neural crest cells associated with division and neurogenesis in zebrafish gut."

The enteric nervous system (ENS) is derived from enteric neural crest cells (ENCCs) that migrate into the gut. The zebrafish larva is a good model to study ENCC development due to its simplicity and transparency. However, little is known how individual ENCCs divide and become neurons.

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This article was published in the following journal.

Name: Developmental dynamics : an official publication of the American Association of Anatomists
ISSN: 1097-0177
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Medical and Biotech [MESH] Definitions

A family of heat-shock proteins that contain a 70 amino-acid consensus sequence known as the J domain. The J domain of HSP40 heat shock proteins interacts with HSP70 HEAT-SHOCK PROTEINS. HSP40 heat-shock proteins play a role in regulating the ADENOSINE TRIPHOSPHATASES activity of HSP70 heat-shock proteins.

Heat and cold stress-inducible, transcription factors that bind to inverted 5'-NGAAN-3' pentamer DNA sequences and are regulated by poly(ADP) ribosylation. They play essential roles as transcriptional activators of the HEAT-SHOCK RESPONSE by inducing expression of large classes of MOLECULAR CHAPERONES and heat-shock proteins. They also function in DNA REPAIR; transcriptional reactivation of latent HIV-1; and pre-mRNA processing and nuclear export of HSP70 HEAT-SHOCK PROTEINS during heat stress.

A subfamily of small heat-shock proteins that are closely related to ALPHA B-CRYSTALLIN. Hsp20 heat-shock proteins can undergo PHOSPHORYLATION by CYCLIC GMP-DEPENDENT PROTEIN KINASES.

Stress-inducible members of the heat-shock proteins 70 family. HSP72 heat shock proteins function with other MOLECULAR CHAPERONES to mediate PROTEIN FOLDING and to stabilize pre-existent proteins against aggregation.

A group of eukaryotic high-molecular mass heat-shock proteins that represent a subfamily of HSP70 HEAT-SHOCK PROTEINS. Hsp110 proteins prevent protein aggregation and can maintain denatured proteins in folding-competent states.

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