Simulations show how HIV sneaks into the nucleus of the cell
Because viruses have to hijack someone else's cell to replicate, they've gotten very good at it—inventing all sorts of tricks.
Jan 25, 2024
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Because viruses have to hijack someone else's cell to replicate, they've gotten very good at it—inventing all sorts of tricks.
Jan 25, 2024
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UNSW medical researcher Dr. David Jacques and his team have discovered how the human immunodeficiency virus (HIV) breaches the cell nucleus to establish infection, a finding that has implications beyond HIV biology.
Jan 24, 2024
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Several types of cancer are believed to be linked to alterations of macromolecular structures known as nuclear pore complexes (NPCs). These structures are embedded in the nuclear envelope, a membrane barrier that separates ...
Sep 15, 2023
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As heart cells mature in mice, the number of communication pathways called nuclear pores dramatically decreases, according to new research from University of Pittsburgh and UPMC scientists. While this might protect the organ ...
Oct 24, 2022
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Anita Göndör's group has identified a new mechanism underlying the pathological over-expression of cancer genes. The results, which are published in Nature Communications show that signals in the environment of the cancer ...
Jan 12, 2022
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Adenoviruses have a linchpin protein that stabilizes their DNA until it reaches the infected cell's nucleus. The protein then detaches from the viral genome, and the virus uncoats. Only then are the genes released into the ...
Dec 21, 2021
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Amyotrophic lateral sclerosis (ALS) is a rapidly progressive and fatal degenerative disease affecting the nerve cells in the brain and spinal cord responsible for controlling voluntary muscle movement. "Sporadic" or non-inherited ...
Jul 28, 2021
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Scientists at Sanford Burnham Prebys Medical Discovery Institute have shown that blocking the construction of nuclear pores complexes—large channels that control the flow of materials in and out of the cell nucleus—shrank ...
Sep 28, 2020
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Researchers have long sought to explain precisely how the most common genetic mutation linked to both amyotrophic lateral sclerosis (ALS) and frontotemporal dementia causes the death of nerve cells. Now, Johns Hopkins Medicine ...
Sep 3, 2020
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A multi-institutional study led by investigators at Massachusetts General Hospital (MGH) and Johns Hopkins School of Medicine has found how the abnormal form of tau that accumulates in the neurofibrillary tangles that characterize ...
Sep 5, 2018
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Nuclear pores are large protein complexes that cross the nuclear envelope, which is the double membrane surrounding the eukaryotic cell nucleus. There are about on average 2000 nuclear pore complexes in the nuclear envelope of a vertebrate cell, but it varies depending on cell type and throughout the life cycle. The proteins that make up the nuclear pore complex are known as nucleoporins. About half of the nucleoporins typically contain either an alpha solenoid or a beta-propeller fold, or in some cases both as separate structural domains. The other half show structural characteristics typical of "natively unfolded" proteins, i.e. they are highly flexible proteins that lack ordered secondary structure. These disordered proteins are the FG nucleoporins, so called because their amino-acid sequence contains many repeats of the peptide phenylalanine—glycine.
Nuclear pores allow the transport of water-soluble molecules across the nuclear envelope. This transport includes RNA and ribosomes moving from nucleus to the cytoplasm and proteins (such as DNA polymerase and lamins), carbohydrates, signal molecules and lipids moving into the nucleus. It is notable that the nuclear pore complex (NPC) can actively conduct 1000 translocations per complex per second. Although smaller molecules simply diffuse through the pores, larger molecules may be recognized by specific signal sequences and then be diffused with the help of nucleoporins into or out of the nucleus. This is known as the RAN cycle. Each of the eight protein subunits surrounding the actual pore (the outer ring) projects a spoke-shaped protein into the pore channel. The center of the pore often appears to contains a plug-like structure. It is yet unknown whether this corresponds to an actual plug or is merely cargo caught in transit.
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