Why should you do this, especially in Sierra: -security/app-translocation-services-os-x-10-12/It is not strictly needed on Mac OS
App Translocation Services In OS X 10.12
I encountered this issue several years ago with the emulators BasiliskII and SheepShaver. I distribute regularly updated builds of these apps in zip archive from the emaculation.com site. Some users had the apps crash.It appeared to be a security feature in macOS that will not allow an app to run unless it has been intentionally installed by the user. The feature was introduced in macOS 10.12 (Sierra).My advice was then, and still is, to make a copy of the app in a different location, trash the original, and move the copy back to where the original was. It always works.
I ran into this issue with your apps in the past. I soon discovered that moving the app out of the folder it arrived in would stop the annoying translocation behaviour, just as mentioned in your postscript.
I've noticed something very peculiar with 10.12 that was not happening with 10.11 and before. An example app is PTHPasteboard. I've seen this with a couple others, but it doesn't seem to always happen.
Starting in OS X v10.12, you can no longer provide external code or data alongside your code-signed app in a zip archive or unsigned disk image. An app distributed outside the Mac App Store runs from a randomized path when it is launched and so cannot access such external resources.
I've downloaded and installed STS 3.8.2 on my Mac (10.12.1). Each time the STS.app file is launched, it creates a new org.springsource.sts_3.8.2.RELEASE_########_macosx_cocoa_x86_64 folder under the hidden .eclipse folder (the hashes are there because I have MANY of the same folder with the numbers in the hash area being the only difference). In doing so, the default workspace and all plugins I installed the last time it was running are wiped out (because they exist in the previous #### folder).
Since macOS Sierra does the app translocation again after every restart, Eclipse/STS doesn't know anything about the "old" configuration area anymore and creates a new one. As far as I can see, there is no way for Eclipse/STS to distinguish between a separate install and a newly translocated app... :-(
A) Move STS.app into a different location on your disc afterunpacking the tar.gz archive (using the Finder, not the commandline). If you move it to "Applications", for example, everythingworks as before (no app translocation happens in that case).
My friend [redacted] informed me that there is actually a new API for App Translocation in the 10.12 SDK: . I haven't tried that API yet; I still haven't attempted to build our apps using Xcode 8. But hopefully it should be useful in determining whether an app has been translocated. Once that condition has been detected, what's the solution? One approach would be to simply ask the user to move the app in Finder. It's also conceivable that the app could copy itself to /Applications, without the quarantine xattr, and relaunch itself from there. Again, this isn't something I've tested yet. I haven't had much time to explore Sierra, because we just got it yesterday, and I do need to sleep.
I hit this problem recently and moving the application in Finder did not stop the translocation.I noticed it by the forever rules in Little Snitch not working after close and relaunch of the application.Also by the Dock icon losing the link and showing a ? mark.
Now that I discovered this article, I downloaded DropDMG and selected signing in the preferences. The DMG can be downloaded and unpacked with no problems. You still got the question about the app is being downloaded from the internet, but the translocation does not occur.
App Translocation is applied to unsigned software packages (i.e. ZIP archives) that have been downloaded from the internet. To determine if something was downloaded (and thus is a candidate for translocation), the OS examines the com.apple.quarantine extended attribute. Using the xattr command, we can dump such attributes:
Extract the zip file to a folder of your choice. Double click on the application. Simple as.However, if you are using OSX 10.7.5 or later, please read the notes about "unsigned apps" below. In case of OpenArena 0.8.8, please also read the following section about it. Since OSX 10.12, things are more complex, and since 10.15, they are even worse.
Translocation (5;12)(q31-q33;p12-p13) is a recurring cytogeneticabnormality reported in patients with CMML, in particular those witheosinophilia.4 The t(5;12) translocation results in thefusion of the transmembrane and tyrosine kinase domains of theplatelet-derived growth factor receptor-B (PDGFR-B) gene onchromosome 5 with the amino-terminal domain of the TEL/ETV6 gene ofchromosome 12, a member of the ETS family of transcription factors.5,6The resultant aberrant tyrosine kinase activity of this hybrid proteinis potentially the transforming event in these cases of CMML.7-9The overall incidence of t(5;12) in CMML is unknown but is presumed tobe relatively rare. A retrospective analysis by Gunby, et al.demonstrated the translocation in only 1/27 patients with CMML.10Others have indicated only 40 to 50 known cases of CMML involvingt(5;12) or similar chromosomal abnormalities involving the PDGFR-B loci.11
Imatinib is a tyrosine kinase inhibitor with potent activity againstBCR-ABL in chronic myeloid leukemia. Imatinib also inhibits a number ofadditional tyrosine kinases including PDGFRA, PDGFRB, and c-kit,providing the basis for its use in CMML involving the t(5;12)translocation.12-14 Recently, Han, et al. reviewed 13 casesfrom the literature of myeloproliferative diseases with evidence ofPGDFR-B translocations treated with imatinib.11 An impressive number of complete responses were noted, encouraging further study of this agent in this CMML subgroup.
In summary, CMML associated with t(5;12) translocation is arelatively rare disorder. Responses to imatinib are variable, but thisagent offers a unique treatment alternative in a disease withrelatively few curative options in the elderly population. Therefore,identifying this translocation, especially in CMML patients presentingwith eosinophilia, should be a priority.
Merci de compléter votre article avec la méthodologie (si elle existe) pour contourner cette translocation des apps. Cela sera nettement plus intéressant que de rappeler ce qui existait déjà avant.
J'ai depuis peu acheté un mac et les trois procédures décrites ne marchent pas. J'ai macOS Sierra version 10.12.2. - Quand je fais un clic droit sur mon application + ouvrir dans le dossier "applications", cela m'affiche la même fenêtre que quand je clique simplement sur mon application - Je ne vois pas l'option dans les préférences système - La commande du terminal ne marche pas. "Permission denied". (je suis bien administrateur de mon mac)
Lysosomal changes and dysfunction are have profound implications for the development of numerous human diseases.9,10 The prevalence of neurodegenerative and cardiovascular diseases in the elderly was thought to be closely related to the decline in lysosomal function with age.9,11 In contrast, cancer cells upregulate their metabolism by modulating lysosomal quantity, composition, and activity to meet their needs for cell growth and proliferation.2,8 Besides, the translocation and abnormal secretion of lysosomes are conducive to the invasion and metastasis of cancer cells, and upregulated autophagy is considered a vital means by which cancer cells develop resistance to chemotherapy and radiotherapy.5,10,12,13 Growing attention has been paid to the role of lysosomes in immunity.14 The abnormal degradation of major histocompatibility complex (MHC) molecules and immune checkpoints by lysosomes in cancer cells, as well as the defects in selective autophagy of tumor-infiltrating T lymphocytes, together contribute to tumor immune escape.15,16,17 In the cells of patients with autoimmune diseases, changes in lysosomal biogenesis, acidification and cathepsin activity have also been confirmed, and such changes are thought to be closely related to disease activity and progression.18,19,20,21,22,23
Lysosomal biogenesis is a combination of cellular biosynthesis and endocytosis pathways (Fig. 3).6,28 The expression of lysosomal genes is triggered by the binding of transcription factors (TFs) of microphthalmia/transcription factor E (MiT/TFE) family to the coordinated lysosomal expression and regulation (CLEAR) elements.2,30,31 Among these TFs, transcription factor EB (TFEB) is the first and most thoroughly studied TF known to directly bind to the CLEAR element.2,30,31 Transient receptor potential mucolipin channel (TRPML1), calcineurin, protein phosphatase 2A (PP2A), and mammalian target of rapamycin complex 1 (mTORC1) jointly regulate the activation and nuclear translocation of TFEB by modulating its phosphorylation status.2,8,32,33,34 After being synthesized in endoplasmic reticulum (ER), lysosomal proteins are transported to trans-Golgi network (TGN) and then be secreted to plasma membrane for subsequent endocytosis, or transmitted directly to the endo-lysosomal system.28 Sorting events in endo-lysosomal system eventually cause these compartments to be rich in lysosomal membrane proteins and lysosomal hydrolases, which constitute the major components of lysosomes.8,28
The biogenesis of lysosomes. Lysosomal biogenesis is a combination of cellular biosynthesis and endocytosis pathways. TRPML1 channel, calcineurin, PP2A, and mTORC1 jointly regulate the biosynthesis of lysosomal proteins by modulating the activation and nuclear translocation of TFEB. PP2A, protein phosphatase 2A; mTORC1, mammalian target of rapamycin complex 1; TGN, trans-Golgi network; TFEB, transcription factor EB; CLEAR, coordinated lysosomal expression and regulation 2ff7e9595c
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