Civil Rights
Movements, leaders, victories and the continuing fight for equality.
q2K BHP
Black History Portal
THE BHP WIRE —
HIDDEN TRUTHS
What's New!
Explore the people, places, events, achievements, struggles and stories that shaped our journey.
Movements, leaders, victories and the continuing fight for equality.
Innovation, patents, science, technology and world-changing contributions.
Pioneers, champions, Negro Leagues, records, activism and excellence.
Meet the people whose lives, choices and achievements shaped the journey.
Black towns, communities, institutions and places where history happened.
Moments that changed communities, movements, institutions and the nation.
In August 1908, a white mob attacked Springfield, Illinois’s Black community, destroying homes and businesses and lynching two Black men. National outrage over the violence helped spur the movement that created the NAACP the following year.
MORE →Reflects the personal views, recollections, and perspective of the author, Mike Davis.
This is a personal recollection on the Move fire on May 13, 1985
| retinoic acid receptor alpha | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | RARA | ||||||
| NCBI gene | 5914 | ||||||
| HGNC | 9864 | ||||||
| OMIM | 180240 | ||||||
| RefSeq | NM_000964 | ||||||
| UniProt | P10276 | ||||||
| Other data | |||||||
| Locus | Chr. 17 q21.1 | ||||||
| |||||||
| retinoic acid receptor beta | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | RARB | ||||||
| NCBI gene | 5915 | ||||||
| HGNC | 9865 | ||||||
| OMIM | 180220 | ||||||
| RefSeq | NM_000965 | ||||||
| UniProt | P10826 | ||||||
| Other data | |||||||
| Locus | Chr. 3 p24 | ||||||
| |||||||
| retinoic acid receptor gamma | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | RARG | ||||||
| NCBI gene | 5916 | ||||||
| HGNC | 9866 | ||||||
| OMIM | 180190 | ||||||
| RefSeq | NM_000966 | ||||||
| UniProt | P13631 | ||||||
| Other data | |||||||
| Locus | Chr. 12 q13 | ||||||
| |||||||
The retinoic acid receptor (RAR) is a type of nuclear receptor which can also act as a ligand-activated transcription factor[1] that is activated by both all-trans retinoic acid and 9-cis retinoic acid, retinoid active derivatives of Vitamin A.[2] They are typically found within the nucleus.[3] There are three retinoic acid receptors (RAR), RAR-alpha, RAR-beta, and RAR-gamma, encoded by the RARA, RARB, RARG genes, respectively. Within each RAR subtype there are various isoforms differing in their N-terminal region A.[1] Multiple splice variants have been identified in human RARs: four for RARA, five for RARB, and two for RARG.[4] As with other type II nuclear receptors, RAR heterodimerizes with RXR and in the absence of ligand, the RAR/RXR dimer binds to hormone response elements known as retinoic acid response elements (RAREs) complexed with corepressor protein. Binding of agonist ligands to RAR results in dissociation of corepressor and recruitment of coactivator protein that, in turn, promotes transcription of the downstream target gene into mRNA and eventually protein. In addition, the expression of RAR genes is under epigenetic regulation by promoter methylation.[5] Both the length and magnitude of the retinoid response is dependent of the degradation of RARs and RXRs through the ubiquitin-proteasome.[3] This degradation can lead to elongation of the DNA transcription through disruption of the initiation complex or to end the response to facilitate further transcriptional programs.[3] RAR receptors are also known to exhibit many retinoid-independent effects as they bind to and regulate other nuclear receptor pathways, such as the estrogen receptor.[6]
RARs play a crucial role in embryonic development. Mice knockout studies of RARs revealed that knocking out RARs could fully replicate the spectrum of defects associated with fetal vitamin A deficiency syndrome, unveiling additional abnormalities beyond previously known vitamin A functions. Notably, double RAR mutants exhibited the most severe defects, including ocular and cardiovascular defects, indicating some level of redundancy among RARs. RXR/RAR heterodimers transmit retinoid signals in diverse ways to control the expression of networks of retinoic acid (RA) target genes. This process plays a crucial role in shaping both the axial and limb patterning during early embryo development, as well as influencing various aspects of organ formation in later stages of development.[7][8]
Source: Wikipedia. Article content is retrieved live through the MediaWiki API.
In genetics and molecular biology, a corepressor is a molecule that represses the expression of genes. In prokaryotes, corepressors are small molecules whereas in eukaryotes, corepressors are proteins. A corepressor does not directly bind to DNA, but instead indirectly regulates gene expression by binding to repressors. A corepressor downregulates (or represses) the expression of genes by binding to and activating a repressor transcription factor. The repressor in turn binds to a gene's operator sequence (segment of DNA to which a transcription factor binds to regulate gene expression), thereby blocking transcription of that gene.
BCL-6 corepressor is a protein that in humans is encoded by the BCOR gene.
The retinoic acid receptor (RAR) is a type of nuclear receptor which can also act as a ligand-activated transcription factor that is activated by both all-trans retinoic acid and 9-cis retinoic acid, retinoid active derivatives of Vitamin A. They are typically found within the nucleus. There are three retinoic acid receptors (RAR), RAR-alpha, RAR-beta, and RAR-gamma, encoded by the RARA, RARB, RARG genes, respectively. Within each RAR subtype there are various isoforms differing in their N-terminal region A. Multiple splice variants have been identified in human RARs: four for RARA, five for RARB, and two for RARG. As with other type II nuclear receptors, RAR heterodimerizes with RXR and in the absence of ligand, the RAR/RXR dimer binds to hormone response elements known as retinoic acid response elements (RAREs) complexed with corepressor protein. Binding of agonist ligands to RAR results in dissociation of corepressor and recruitment of coactivator protein that, in turn, promotes transcription of the downstream target gene into mRNA and eventually protein. In addition, the expression of RAR genes is under epigenetic regulation by promoter methylation. Both the length and magnitude of the retinoid response is dependent of the degradation of RARs and RXRs through the ubiquitin-proteasome. This degradation can lead to elongation of the DNA transcription through disruption of the initiation complex or to end the response to facilitate further transcriptional programs. RAR receptors are also known to exhibit many retinoid-independent effects as they bind to and regulate other nuclear receptor pathways, such as the estrogen receptor. RARs play a crucial role in embryonic development. Mice knockout studies of RARs revealed that knocking out RARs could fully replicate the spectrum of defects associated with fetal vitamin A deficiency syndrome, unveiling additional abnormalities beyond previously known vitamin A functions. Notably, double RAR mutants exhibited the most severe defects, including ocular and cardiovascular defects, indicating some level of redundancy among RARs. RXR/RAR heterodimers transmit retinoid signals in diverse ways to control the expression of networks of retinoic acid (RA) target genes. This process plays a crucial role in shaping both the axial and limb patterning during early embryo development, as well as influencing various aspects of organ formation in later stages of development.
REST corepressor 1 also known as CoREST is a protein that in humans is encoded by the RCOR1 gene.
Before the 1921 destruction of Tulsa’s Greenwood District, Black residents had created a remarkable center of business and community life. The district included stores, professional offices, entertainment venues and homes owned by Black citizens. Understanding Greenwood means learning what was built—not only what was burned.
MORE →Brown v. Board of Education in 1954.
