I'm not against using solar electricity because it can be made affordable but this idea is equivalent to the backyard blast furnaces in Maoist China. It's a waste of time and only useful for status signaling to your eco-chic friends.
32 karma · joined November 21, 2015
I'm not against using solar electricity because it can be made affordable but this idea is equivalent to the backyard blast furnaces in Maoist China. It's a waste of time and only useful for status signaling to your eco-chic friends.
If I'm familiar with an application, I don't look at the keyboard. If I'm VERY familiar with an application, I don't even recall commands through their mnemonic, but through muscle memory.
For example, I've just switched to spacemacs from vim, and one of the first commands to learn is Ctrl+G, which is to exit from any menu. "Escape from menu" is not mapped into my brain as C-g, but as "pinky here and left index finger here." In contrast, when I want to change to next buffer, I think <SPC> b n, and not "thumb, right index finger on this button, then right index finger on this button" (although I'm sure that it will become muscle memory before long.)
HOWEVER, the nice thing about spacemacs is that you can press space and you see all possible commands pop up in the command buffer. This is a highly effective method for learning commands, and it is similar to how the "ribbon design" functioned in Microsoft Office 2007. This is where I think the E-ink keyboard could be most useful: in teaching keystrokes. It's essentially the same thing as looking down at the spacemacs command buffer, but you get to see the command pop up on your keyboard.
That being said, there are a lot of downsides to the whole idea. You're stuck with a very limited set of switch-and-layout combinations if you want an e-ink keyboard. Secondly, keyboards take a lot of abuse, and I don't know how much a replacement e-ink keycap costs, or where I'm going to get one (maybe this won't be such an issue, though). Finally, the glyph can only be represented as a glyph, and not as a detailed command like it can in a spacemacs buffer.
Cool product though; I'd get one if I had money to burn!
How would it do that? The phage can't synthesize latrotoxin itself, so it would need to instruct its bacterial host to produce it. Can bacteria even produce this toxin properly, with all proper post-translational modifications?
Secondly, how is it even obtaining the spider DNA when it infects the bacteria. I've heard of viruses packing extra nucleic acid from their hosts into their particulate forms when they replicate, but how does the spider DNA get into the bacteria so that this can happen?
In 2016, however, I think that a lot of people would have read CLRS, even if they haven't read ALL of it. It's used as the reference text by a lot of university courses on algorithms.
Chimeric Antigen Receptor therapy seems like more of a "game changer," given that it's a new therapeutic direction. This is just another monoclonal antibody.
From: Gettinger SN, Horn L, Gandhi L, et al. Overall Survival and Long-Term Safety of Nivolumab (Anti–Programmed Death 1 Antibody, BMS-936558, ONO-4538) in Patients With Previously Treated Advanced Non–Small-Cell Lung Cancer. Journal of Clinical Oncology. 2015;33(18):2004-2012. doi:10.1200/JCO.2014.58.3708.
Programmed death 1 (PD-1) is an immune checkpoint receptor expressed on activated T cells, which normally serves to dampen the immune response to protect against excessive inflammation and the development of autoimmunity. However, in the setting of malignancy, PD-1 signaling, driven primarily by adaptive expression of programmed death ligand 1 (PD-L1) within the tumor, inactivates primed T cells that recognize tumor-specific antigens, allowing tumor growth and metastasis. PD-1 pathway blockade with monoclonal antibodies offers a novel approach to restoring T cell–mediated antitumor immunity, with the potential for application across a broad population of patients with NSCLC.
From the article:
In a trial of more than 350 patients, published in the New England Journal of Medicine, 36% treated with the immunotherapy drug nivolumab were alive after one year compared with 17% who received chemotherapy.
That seems like a small improvement rather than a "game changer."
For example, say you created fusions between the cage mononmer and antibody Fv chains that bind two different proteins (A and B) and then you created fusions between the cage monomer and two different fluorescent proteins (GFP and RFP).
In bacteria strain 1, you express fusion A and fusion GFP so that you assemble cages that will show a green signal where-ever A is found (e.g., for fluorescent microscopy). Likewise, in bacterial strain 2, you expression fusions B and RFP so that you get a red signal where ever B is. You could use these as detectors in a western blot, for example. (Obviously there are better, established ways to detect proteins of interest in a western blot, but that's just a simple idea).
Another idea that I remember reading about was creating glucuronidase fusions to antibody fragments designed to bind cancer cells. The patient would then be administered the glucuronide of a cytotoxic drug, which is not toxic in its glucuronide form. The idea is that the antibody fusion protein would activate the drug so that it would be concentrated highly near the cancer cell and nowhere else.
1. It reminds me of the graphical view that is present in the IDA disassembler in which functions are broken into "boxes" wherever there is a jump in control flow. If you're disassembling a C function, for example, this generally means that a box corresponds to some block of code that is delimited by curly braces. The point here is that you don't have a box for every single assembly instruction, because that would be ridiculous. Rather, the function is broken down into several "clauses" that express complex ideas, and then each clause is described textually by several lines of code.
For example, if I want to express something like:
(lambda (x y) (/ (* 2 x) (+ x y)))
then it would be nice if I could draw a box with input terminals for x and y and then type in the expression, rather than having to create three boxes for each arithmetic operation. It would be faster to program this way, and the result would easier to read.2. Also, drawing inspiration from IDA's visual mode (as well as electronic circuit diagrams), lines should all travel at right angles. There should also be an auto layout mode which attempts to layout the graph so that there are a minimum number of edge crossings.
I don't really see the issue, here.
For example, say the pathogen develops a mutation so that the bacteriocin's binding domain no longer recognizes its bacterial target. Because the bacteriocin is a class of peptide, and not a small molecule, its (theoretically) rather simple to run a directed evolution program in order to discover a variant of the original bacteriocin that will bind the mutant strain. It would be far more difficult to do the same thing with some small molecule antibiotic, and you'd never be able to generate the number of derivatives of the small molecule that you could with a peptide.
Similarly, if the bacteria develops a mutation so that the active domain of the bacteriocin no longer works properly, you can run the same sort of directed evolution experiment.
Or, you could conceivably use a different binding domain altogether as was suggested in the article and in this thread.
As for the delivery of the antibiotic, it needs some way to come in contact with the pathogen. A topical wound that is infected with some form of staphylococcus, for example, could be treated with some sort of ointment. But relying on the body's circulatory system to deliver the drug, well that would seemingly be more difficult than just taking a pill.
At a cursory glance it seems like https://coronalabs.com/, but it's free, which is nice :).
Anyway, it is about using a class of bacteriocidal polypeptides, called bacteriocins, to treat bacterial infections in humans.
Because we have the technology to create custom polypeptide sequences, the allure is that we could design proteinaceous binding domains that are specific for some nasty pathogen. Through combinatorial chemical methods, you can generate millions of different of different peptides, and then select for the one that binds your bacterial target. Most current antibiotics are small molecules, and although you can screen chemical libraries for some antimicrobial property, you can't make millions or billions of derivatives of some candidate small molecule like you can with a peptide polymer. This could be a breakthrough method for the rapid development of antimicrobial agents.
However, there's a downside, and that is that large molecules have a more difficult time travelling through the body, specifically through tissues that have tight junctions between cells. It seems like these bacteriocins would have to be introduced intravenously (or maybe through the respiratory system, like ricin can be) as most peptides are hydrolyzed in the stomach. Even then, peptides don't easily diffuse through the blood brain barrier. I suppose they could be applied topically to treat MRSA.
I thought React was supposed to be used in tandem with a Flux-like component that stores the state of the application, thereby allowing the developer to adopt the functional reactive programming style.
Anyways, I think React will be short lived, because anyone who really wants to hop on the FRP bandwagon will pick up something like http://elm-lang.org in order to fully achieve Satori. I mean, if you're going to drink the Kool-aid, you might as well down the whole pitcher.