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THE JOURNEY THROUGH TIME

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MY'STORY

The MOVE Fire

This is a personal recollection on the Move fire on May 13, 1985 Philadelphia police fired thousands of rounds at the MOVE house, city officials approved dropping an explosive device on the roof, the resulting fire was allowed to burn, 11 people—including five children—died, and 61 homes were destroyed. Philadelphia City Council later called it a “brutal attack carried out by the City of Philadelphia on its own citizens” and acknowledged that no individual faced criminal consequences for the bombing. One timeline correction worth preserving for the BHP record: the major previous MOVE-police confrontation was August 8, 1978, about seven years before the bombing, not a year or two earlier. Officer James Ramp was killed, other police and firefighters were wounded, nine MOVE members were later convicted, and television cameras recorded police beating Delbert Africa during his arrest. The 1985 MOVE Commission later specifically criticized city planners for failing to adequately use lessons from that 1978 confrontation. And that actually strengthens the point you’re making: 1985 did not happen without precedent or institutional memory. There had already been a deadly confrontation with MOVE, years of conflict, negotiations and police involvement before Osage Avenue.

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BLACK FACTS
The Truths They Never Taught You...

Shirley Chisholm — Unbought and Unbossed

In 1968 Shirley Chisholm became the first Black woman elected to the United States Congress. In 1972 she launched a campaign for the Democratic presidential nomination, breaking another political barrier.

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Wikipedia

KIFC3

KIFC3
Identifiers
AliasesKIFC3, kinesin family member C3
External IDsOMIM: 604535; MGI: 109202; GeneCards: KIFC3
Available structures
PDBOrtholog search: PDBe RCSB
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)Chr 16: 57.76 – 57.86 MbChr 8: 95.83 – 95.93 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Kinesin-like protein KIFC3 is a protein that in humans is encoded by the KIFC3 gene.[5][6]


References

[edit]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000140859 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031788 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Hoang EH, Whitehead JL, Dose AC, Burnside B (Dec 1998). "Cloning of a novel C-terminal kinesin (KIFC3) that maps to human chromosome 16q13-q21 and thus is a candidate gene for Bardet-Biedl syndrome". Genomics. 52 (2): 219–22. doi:10.1006/geno.1998.5431. PMID 9782090.
  6. ^ "Entrez Gene: KIFC3 kinesin family member C3".

Further reading

[edit]
[edit]
  • Overview of all the structural information available in the PDB for UniProt: Q9BVG8 (Human Kinesin-like protein KIFC3) at the PDBe-KB.


Source: Wikipedia. Article content is retrieved live through the MediaWiki API.

Wikipedia

KIFC3

Kinesin-like protein KIFC3 is a protein that in humans is encoded by the KIFC3 gene.

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Wikipedia

Microtubule

Microtubules are biopolymers of tubulin that form part of the cytoskeleton to provide structure and shape to a eukaryotic cell. Microtubules can be as long as 50 micrometres, as wide as 23 to 27 nm and have an inner diameter between 11 and 15 nm. They are formed by the polymerization of a dimer of two globular proteins, alpha and beta tubulin into protofilaments that can then associate laterally to form a hollow tube, the microtubule. The most common form of a microtubule consists of 13 protofilaments in the tubular arrangement. Microtubules play an important role in a number of cellular processes. They are involved in maintaining the structure of the cell and, together with microfilaments and intermediate filaments, they form the cytoskeleton. They also make up the internal structure of cilia and flagella. They provide platforms for intracellular transport and are involved in a variety of cellular processes, including the movement of secretory vesicles, organelles, and intracellular macromolecular assemblies. They are also involved in cell division (by mitosis and meiosis) and are the main constituents of mitotic spindles, which are used to pull eukaryotic chromosomes apart. Microtubules are nucleated and organized by microtubule-organizing centres, such as the centrosome found in the center of many animal cells or the basal bodies of cilia and flagella, or the spindle pole bodies found in most fungi. There are many proteins that bind to microtubules, including the motor proteins dynein and kinesin, microtubule-severing proteins like katanin, and other proteins important for regulating microtubule dynamics. Recently an actin-like protein has been found in the gram-positive bacterium Bacillus thuringiensis, which forms a microtubule-like structure called a nanotubule, involved in plasmid segregation. Other bacterial microtubules have a ring of five protofilaments.

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Wikipedia

Keratin

Keratin () is one of a family of structural fibrous proteins also known as scleroproteins. It is the key structural material making up scales, hair, nails, feathers, horns, claws, hooves, and the outer layer of skin in tetrapod vertebrates. Keratin also protects epithelial cells from damage or stress. Keratin is extremely insoluble in water and organic solvents. Keratin monomers assemble into bundles to form intermediate filaments, which are tough and form strong unmineralized epidermal appendages found in reptiles, birds, amphibians, and mammals. Excessive keratinization participate in fortification of certain tissues such as in horns of cattle and rhinos, and armadillos' osteoderm. The only other biological matter known to approximate the toughness of keratinized tissue is chitin. Keratin comes in two types: the primitive, softer forms found in all vertebrates and the harder, derived forms found only among sauropsids (reptiles and birds).

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Wikipedia

Cytoskeleton

The cytoskeleton is a complex, dynamic network of interlinking protein filaments present in the cytoplasm of all cells, including those of bacteria and archaea. In eukaryotes, it extends from the cell nucleus to the cell membrane and is composed of similar proteins in the various organisms. It is composed of three main components: microfilaments, intermediate filaments, and microtubules, and these are all capable of rapid growth and/or disassembly depending on the cell's requirements. The cytoskeleton can perform many functions. Its primary function is to give the cell its shape and mechanical resistance to deformation, and through association with extracellular connective tissue and other cells it stabilizes entire tissues. The cytoskeleton can also contract, thereby deforming the cell and the cell's environment and allowing cells to migrate. Moreover, it is involved in many cell signaling pathways and in the uptake of extracellular material (endocytosis), the segregation of chromosomes during cellular division, the cytokinesis stage of cell division, as scaffolding to organize the contents of the cell in space and in intracellular transport (for example, the movement of vesicles and organelles within the cell) and can be a template for the construction of a cell wall. Furthermore, it can form specialized structures, such as flagella, cilia, lamellipodia and podosomes. The structure, function and dynamic behavior of the cytoskeleton can be very different, depending on organism and cell type. Even within one cell, the cytoskeleton can change through association with other proteins and the previous history of the network. A large-scale example of an action performed by the cytoskeleton is muscle contraction. This is carried out by groups of highly specialized cells working together. A main component in the cytoskeleton that helps show the true function of this muscle contraction is the microfilament. Microfilaments are composed of the most abundant cellular protein known as actin. During contraction of a muscle, within each muscle cell, myosin molecular motors collectively exert forces on parallel actin filaments. Muscle contraction starts from nerve impulses which then causes increased amounts of calcium to be released from the sarcoplasmic reticulum. Increases in calcium in the cytosol allows muscle contraction to begin with the help of two proteins, tropomyosin and troponin. Tropomyosin inhibits the interaction between actin and myosin, while troponin senses the increase in calcium and releases the inhibition. This action contracts the muscle cell, and through the synchronous process in many muscle cells, the entire muscle.

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TOPIC OF THE DAY

Greenwood / Black Wall Street

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.

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TRIVIA QUESTION OF THE DAY

Who was the first African-American woman millionaire in the United States?

Madam C.J. Walker