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Remember, stock screeners are not the magic pill for selecting stocks. Nothing will ever replace good old-fashioned nose-to-the-grindstone research. However, screens can be a good place to start your research process as they can save time and narrow your options down to a more manageable group.
I can't tell ya how to find this, but I have found in one of my older Maximum CDs (from the powerware special issue) a software based tool for improving framerates in some systems. I occasionally play motocross madness, and I used to get a steady 130 FPS, but with this program activated it averaged 180 FPS, and wouldn't drop below about 155. Also at a few points it hit as high as 307 One track that's a user made one (I forget which one) the FPS held at 280. If anyone knows where this toy can be found please post it as I'm sure someone would like to have it. It's 247 K in size so it'd be an easy download.
See ya later all.
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Upload some images for this postI didn’t grow up eating a lot of fish, so for a long time I was really intimidated about cooking it. But it’s so easy! And quick! It’s weeknight gold! Cod was on sale at WF this week, so I wanted to try something new with it. Being a New England girl, I generally enjoy my cod deep fried in a beer batter and served alongside a pile of equally deep fried beer battered onion rings. But this is not vacation, unfortunately. And also, I don’t own a deep fryer. So I started poking around cookbooks and food blogs and found two that I wanted to try.
So tonight’s Not My Recipe is a combo. The fish recipe belongs to Genius Kitchen and the spinach cake from this recipe on Kit’s Coastal.
The fish came out *perfectly* — flakey and velvety. The fresh garlic/lemon/parsley dice to dress up the breadcrumbs (I subbed Panko) is such a powerful flavor pop. It’s classic for a reason. And the spinach was perfect, too. Nothing earth shatteringly new, but just classic and balanced and delicious. These are not my recipes, but I sure wish they were!of Johnnie's Passing
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Johnnie was born on July 8, 1941 and passed away on Saturday, April 7, 2018.
Johnnie was a resident of Woodway, Texas at the time of passing.
He joined the United States Army National Guard.
His family will host a memorial service at a later date. Memorial services will be held at a later date 1-888-579-7953 Code: 28181 Born: July 8, 1941 Death: April 7, 2018.TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress

The E3 ubiquitin ligase TRAIP associates with replication forks through direct interaction with PCNA, promoting checkpoint signaling and genome stability after replication stress.


Introduction
All cells are continuously exposed to a multitude of endogenously and exogenously generated genotoxic insults, which, if not sensed and processed correctly, can be life-threatening for organisms as they alter the content and organization of the genetic material (Hoeijmakers, 2001). To mitigate this danger, cells possess a multifaceted DNA damage response (DDR), a global network of pathways that coordinately impact diverse cellular processes to reestablish genome integrity, providing an important cellular barrier toward the onset of diseases such as cancer (Jackson and Bartek, 2009;Ciccia and Elledge, 2010). Signaling in the DDR is driven by regulated posttranslational modifications of numerous proteins within this network (Ciccia and Elledge, 2010). Cellular genomes are particularly vulnerable to perturbations to chromosomal DNA replication. A variety of obstacles, collectively referred to as "replication stress," can lead to slowing or stalling of replication fork progression, posing a threat to the fidelity of DNA replication and preservation of genome stability (Branzei and Foiani, 2010;Zeman and Cimprich, 2014). Major sources of replication stress include nucleotide shortage, unrepaired DNA lesions, and difficult-to-replicate genomic loci. A common consequence of a slowdown or block to DNA replication is the uncoupling of replicative polymerase and helicase movements, leading to the generation of extensive stretches of single-stranded DNA (ssDNA), which become rapidly bound by RPA (Byun et al., 2005). This serves as a signal for activation of the ATR kinase, a major effector of the response to replication stress (Zou and Elledge, 2003;Nam and Cortez, 2011). Upon its activation, ATR phosphorylates a plethora of substrates, facilitating stabilization of the replisome, inhibition of late origin firing, and arrest of the cell cycle (Zeman and Cimprich, 2014). These actions collectively provide an opportunity for cells to resolve the stress while minimizing the impact on the genome. Failure to rescue stalled replication forks may lead to fork collapse, giving rise to highly cytotoxic DNA doublestrand breaks (DSBs) and gross chromosomal instability (Branzei and Foiani, 2010). Indeed, a range of severe human diseases Cellular genomes are highly vulnerable to perturbations to chromosomal DNA replication. Proliferating cell nuclear antigen (PCNA), the processivity factor for DNA replication, plays a central role as a platform for recruitment of genome surveillance and DNA repair factors to replication forks, allowing cells to mitigate the threats to genome stability posed by replication stress. We identify the E3 ubiquitin ligase TRA IP as a new factor at active and stressed replication forks that directly interacts with PCNA via a conserved PCNA-interacting peptide (PIP) box motif. We show that TRA IP promotes ATR-dependent checkpoint signaling in human cells by facilitating the generation of RPA-bound single-stranded DNA regions upon replication stress in a manner that critically requires its E3 ligase activity and is potentiated by the PIP box. Consequently, loss of TRA IP function leads to enhanced chromosomal instability and decreased cell survival after replication stress. These findings establish TRA IP as a PCNA-binding ubiquitin ligase with an important role in protecting genome integrity after obstacles to DNA replication.
TRA IP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress are known to result from mutations in factors involved in replication stress responses (Zeman and Cimprich, 2014).
The sliding clamp proliferating cell nuclear antigen (PCNA) has an essential role as a processivity factor for eukaryotic DNA replication, providing the central scaffold for the dynamic and carefully controlled engagement of multiple factors with the replication machinery (Moldovan et al., 2007). PCNA also acts as a docking platform for recruitment of components of the DDR and replication surveillance mechanisms. Many of these factors interact with PCNA via a defined PCNA-interacting peptide (PIP) box motif. The regulated and highly coordinated interplay between PCNA and numerous effector proteins is a central step in pathways that respond to replication stress involving multilayered regulatory, posttranslational modification-driven mechanisms that impact PCNA and/or its partner proteins. Ubiquitin-dependent modification of PCNA by members of the RAD6 epistasis group has a key role in triggering DNA damage tolerance pathways that enable bypass of DNA lesions via translesion DNA synthesis or template switching (Hoege et al., 2002).
Although the pathways that respond to replication stress are critical for preventing genome instability and the onset of diseases such as cancer, our understanding of these processes and their regulation remains limited. Here, we used a proteomic strategy to search for new proteins that function in cellular responses to replication stress. We discovered that the E3 ubiquitin ligase TRA IP is a component of the replication fork that interacts directly with PCNA via a conserved PIP box and has an important role in promoting replication stress-induced signaling to protect genome stability in the face of such insults.

TRA IP associates with active and stalled replication forks
Using the CHR OMASS (chromatin mass spectrometry) method to monitor systems-wide protein recruitment to damaged chromatin templates undergoing DNA replication in Xenopus laevis egg extracts (Räschle et al., 2015), we identified the E3 ubiquitin ligase TRA IP (also known as TRIP or RNF206) as a factor showing prominent enrichment at DNA interstrand cross-linkcontaining chromatin, along with a large number of known DNA replication and repair factors (Fig. 1, A and B). In the Xenopus system, the enrichment of TRA IP at damaged chromatin was strongly suppressed in the presence of the replication inhibitor geminin ( Fig. 1 C), indicating that TRA IP accumulation is triggered by the encounter of damaged DNA by active replication forks. TRA IP has previously been implicated in NF-κB signaling, cell proliferation, and the spindle checkpoint (Chapard et al., 2012(Chapard et al.,, 2014. Recently, TRA IP was also suggested to regulate the translesion DNA synthesis polymerase polη when overexpressed (Wallace et al., 2014), but whether this represents a primary function of TRA IP in the DDR is not known. We therefore set out to explore the functional significance of its association with damaged DNA. To validate and corroborate our mass spectrometry data, we asked whether TRA IP is recruited to DNA damage sites in human cells. Initially, we used microlaser irradiation, which gives rise to a range of genotoxic insults. Under these conditions, ectopically expressed GFPtagged TRA IP was clearly recruited to damaged DNA, exhibiting a characteristic microfoci-like recruitment pattern typical of factors recruited directly to