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Teenage Mutant Ninja Turtles color classics
\"The Teenage Mutant Ninja Turtles are a mainstay of pop culture, and it all began with these comics by co-creators Peter Laird and Kevin Eastman. Go back to the very beginning with the Turtles' first encounter with the Foot Clan and their mysterious leader, the Shredder. This volume is perfect for fans to relive the glorious days of the Turtles' origins as well as an excellent place for new readers to see where the TMNT phenomenon began\"-- Back cover.
Book
The mutant files
Introduces the major characters from the \"Teenage Mutant Ninja Turtles\" television program, including Pete the Pigeon Man, the Rat King, the mutant squirrels known as Squirrelanoids, and the Turtles themselves.
Book
Skate like a ninja!
The Turtles team up with Mondo Gecko to catch some theives but whose side is Mondo really on?
Book
Show your colors!
Nickelodeon's Teenage Mutant Ninja Turtles introduce colors as they fight crime in New York City.
Book
Mutations of optineurin in amyotrophic lateral sclerosis
Optineurin defects in ALS
About 10% of cases of the motor neuron disease amyotrophic lateral sclerosis (ALS) are familial, but the small number of mutations so far identified account for only around 20–30% of the those cases. A new study of individuals from ALS-carrying families has now identified three different and previously unknown mutations of
OPTN
, the gene encoding optineurin.
OPTN
was earlier reported to be the causative gene of rare familial glaucoma. Optineurin's ability to inhibit activation of the regulatory protein NF-κB is lost in the mutant forms, suggesting that NF-κB inhibitors might be useful in ALS treatment.
Amyotrophic lateral sclerosis (ALS) is a disorder characterized by the degeneration of motor neurons. About 10% of cases are familial, but the mutations identified in these families account for only 20–30% of such cases. Here a new set of mutations in familial ALS is found — in the gene encoding optineurin. Given the effect of optineurin mutations on the NF-κB protein, it is suggested that inhibiting NF-κB might be useful in treating ALS.
Amyotrophic lateral sclerosis (ALS) has its onset in middle age and is a progressive disorder characterized by degeneration of motor neurons of the primary motor cortex, brainstem and spinal cord
1
. Most cases of ALS are sporadic, but about 10% are familial. Genes known to cause classic familial ALS (FALS) are superoxide dismutase 1 (
SOD1
)
2
,
ANG
encoding angiogenin
3
,
TARDP
encoding transactive response (TAR) DNA-binding protein TDP-43 (ref.
4
) and fused in sarcoma/translated in liposarcoma (
FUS
, also known as
TLS
)
5
,
6
. However, these genetic defects occur in only about 20–30% of cases of FALS, and most genes causing FALS are unknown. Here we show that there are mutations in the gene encoding optineurin (
OPTN
), earlier reported to be a causative gene of primary open-angle glaucoma (POAG)
7
, in patients with ALS. We found three types of mutation of
OPTN
: a homozygous deletion of exon 5, a homozygous Q398X nonsense mutation and a heterozygous E478G missense mutation within its ubiquitin-binding domain. Analysis of cell transfection showed that the nonsense and missense mutations of
OPTN
abolished the inhibition of activation of nuclear factor kappa B (NF-κB), and the E478G mutation revealed a cytoplasmic distribution different from that of the wild type or a POAG mutation. A case with the E478G mutation showed OPTN-immunoreactive cytoplasmic inclusions. Furthermore, TDP-43- or SOD1-positive inclusions of sporadic and
SOD1
cases of ALS were also noticeably immunolabelled by anti-OPTN antibodies. Our findings strongly suggest that OPTN is involved in the pathogenesis of ALS. They also indicate that NF-κB inhibitors could be used to treat ALS and that transgenic mice bearing various mutations of
OPTN
will be relevant in developing new drugs for this disorder.
Journal Article
Know your shapes!
\"Nickelodeon's Teenage Mutant Ninja Turtles introduce the concept of shapes as they fight aliens and slice pizza. Inspired by the successful Half-Shell Heroes toy line.\"--Amazon.com
Book
Allele-selective lowering of mutant HTT protein by HTT–LC3 linker compounds
Accumulation of mutant proteins is a major cause of many diseases (collectively called proteopathies), and lowering the level of these proteins can be useful for treatment of these diseases. We hypothesized that compounds that interact with both the autophagosome protein microtubule-associated protein 1A/1B light chain 3 (LC3)
1
and the disease-causing protein may target the latter for autophagic clearance. Mutant huntingtin protein (mHTT) contains an expanded polyglutamine (polyQ) tract and causes Huntington’s disease, an incurable neurodegenerative disorder
2
. Here, using small-molecule-microarray-based screening, we identified four compounds that interact with both LC3 and mHTT, but not with the wild-type HTT protein. Some of these compounds targeted mHTT to autophagosomes, reduced mHTT levels in an allele-selective manner, and rescued disease-relevant phenotypes in cells and in vivo in fly and mouse models of Huntington’s disease. We further show that these compounds interact with the expanded polyQ stretch and could lower the level of mutant ataxin-3 (ATXN3), another disease-causing protein with an expanded polyQ tract
3
. This study presents candidate compounds for lowering mHTT and potentially other disease-causing proteins with polyQ expansions, demonstrating the concept of lowering levels of disease-causing proteins using autophagosome-tethering compounds.
Compounds that interact with mutant huntingtin and an autophagosomal protein are able to reduce cellular levels of mutant huntingtin by targeting it for autophagic degradation, demonstrating an approach that may have potential for treating proteopathies.
Journal Article