3,638 research outputs found
MUT-16 and orthologs contain a high degree of predicted disorder.
No full text(A) Graph comparing disorder tendency of C. elegans MUT-16 (isoform b, WP:CE40347) in red to orthologs in C. remanei (RP:RP48608) in light gray, C. briggsae (BP:CBP44329) in medium gray, and C. japonica (JA:JA63728) in dark gray using IUPRED and long disorder parameters (http://iupred.enzim.hu/). Scores above 0.5 indicate disorder. Residue positions correspond to the C. elegans MUT-16 sequence, but all proteins are similar in length. (B) Q, N, and P residues in C. elegans MUT-16 were counted in amino acid 100-mers, starting at position one, shifting 10 residues at a time, and displayed as stacked columns. Indicated residue positions are the mid-point of the 100-mer. (C) Schematic of known dependencies of Mutator foci formation. The requirements for localization of RRF-1, RDE-8, NYN-1, NYN-2, and SMUT-1 were not known prior to this work. (D, E) Diagram (D) and table (E) of MUT-16 deletions generated by CRISPR. Bars in (D) are drawn to scale relative to residue positions in (A,B).</p
Re-reading the sanctuary of mut in light of the new restorations
No full textThe restoration and conservation activities carried out by Istituto Centrale del Restauro on the wall paintings of the Temple of Mut has led to a better understanding of the iconography and the textual apparatus of the main sanctuary, B305.
The conservation work undertaken so far has allowed to make the east, west and south walls of the sanctuary B305 almost completely and clearly legible. The north wall is currently still under restoration, and the both the description of its iconography and the transcription of its texts will be presented soon
Es braucht schlicht Mut
No full textAuer M, Kreutz-Gers W, Kühl S. Es braucht schlicht Mut. Forschung & Lehre. 2025;(6):20-22
Toxic species Alexandrium minutum Halim bloom in Palma harbour (Majorca Island, march 1999), relarionshi
No full textAbstract not availabl
Study of materials, execution technique and deterioration processes at the Temple of Mut
No full textThe restoration activities on the mural paintings in the Temple of Mut were helped by the scientific study of their constituent materials and execution technique. The analysis also highlighted on-going and past deterioration processes, which altered the paintings visibility. The study was mostly focused on room B305 and, minorly, on room B303. From the micro-sampling, done by the restorers between 2014 and 2020, after a careful examination of surfaces, polished cross sections were prepared and analysed by optical microscopy (OM), under visible and UV light, and scanning electron microscopy with energy dispersive X-ray spectroscopy (SEM-EDS).
In cross sections where Egyptian blue might be found, visible induced luminescence (VIL) was also performed. Some micro-fragments were also analysed by micro-Fourier transform infrared spectroscopy (μ-FTIR). One mortar sample was also analysed by thermogravimetric analysis (TGA) to quantify its composition. Finally, binders in the pictorial layers were also tentatively characterized by gas chromatography-mass spectrometry (GC-MS)
The sedimentary characteristics of Dagpazari patch reef (Middle Miocene, Mut-Içel/Turkey)
No full textThis study aims to determine facies characteristics of the Dagpazari patch reef (Middle Miocene) located at 13 km north of the Mut (Içel) town. Mut (Içel) and nearby areas are geologically known as Mut Basin situated in the Central Taurides. In the Mut Basin, Middle Miocene time is represented by Mut and Köselerli formations. The Mut Formation comprises reef limestone and interfingers with the Köselerli Formation consisting of claystone, argillaceous limestone and marl. Dagpazari patch reef has a gentle and elongated dome shape. Its clongation extends in NW-SE direction. In the Dagpazari patch reef and its surroundings, five lithofacies and several subfacies have been delineated based mainly on reef geometry and also macro and micro facies features. This patch reef is approximately 15 m thick, 500 m in length and 200 m in width. These are; 1) Base facies (red algal wackestone-packstone, Dunham 1962; biomicrite, Folk 1962); 2) Reef core facies (coral-red algal framestone-bindstone, Embry and Klovan 1971; biolithite, Folk 1962); gastropodpelecypod wackestone-packstone, biomicrite; grainstone, biosparite); 3) Fore reef-flank facies (planktonic foraminiferal-red algal wackestone, biomicrite); 4) Back reef-flank facies (wackestone, biomicrite; local framestone-bindstone, biolithite); 5) Sealing facies (echinoid-intraclast packstone-grainstone, biointramicrite, biointrasparite). Reef core facies is easily separated from other reef facies by: i) presence of frame-building organisms (coral); ii) presence of binding organisms (red algae, bryozoa); and iii) diverse fauna. Reef-flank facies are separated from reef core facies due to their well-bedded appearance. The sealing facies truncates the other reef units with an erosional surface. Facies and frame-building organisms were highly affected by sea-level fluctuation during the Langhian. Grainstone (Dunham 1962) occurred where the environment is close to wave base; planktonic foraminiferal wackestone (Dunham 1962) deposited where the environment was relatively deep. In overall, the Dagpazari patch reef was deposited in shallow environment
Mut-tools:mutation testing for C/C++ programs
No full textMut-tools are used to inject mutations to C/C++ programs. Mutations are injected by an extended LLVM/Clang compiler (version 6.0) that modifies the source code representation of the program on the fly. All mutations of a translation unit (i.e., a source code file) are included into a single source code representation that is translated to an object binary file. We call this as the all mutants form of the translation unit. In earlier research similar representations are called as program schemata or conditional mutations. The modified source code representation exists only in the memory of the compilation process.As usual, an object binary file may represent an executable program (i.e., the program is composed of only one translation unit), or executable programs can be composed by link editing several binary object files together. In addition, libraries, both static and dynamic, can be built in the usual way. Ordinary object binary files and object binary files in the all mutants form can be mixed.The idea in the all mutants form is that if one of the mutations is activated at program start, then the all mutants form behaves exactly the same way as a mutant containing only the activated mutation. If none of the mutations is activated, the all mutants form behaves exactly the same way as the original program. This makes management of the mutants easy as there is only one binary version instead of thousands of different binary versions each of which represents one single mutant.Mut-tools are built on top of LLVM/Clang version 6.0. The main components are an LLVM/Clang plug-in module (`/usr/local/mut/lib/mutate.so') that injects mutations to the original C/C++ source code on the fly, and a run time library (`/usr/local/mut/lib/libmut.so') that is used to activate a specified mutant.The user level programs (in directory `/usr/local/mut/bin') mut-gen mut-list mut-runhide the usage of the main components from end users.The program `mut-gen' is used when a programmer wants to create binary object files in the all mutants form. The `mut-gen' program sets up the compilation environment so that the extended LLVM/Clang compiler injects mutants to the binary object file it creates.The mutations injected to a binary program can be listed with the program `mut-list'. A mutant can be activated with the program `mut-run'.A simple demonstration software can be found from the directory `/usr/local/mut/test/even'. The program takes one integer argument and prints whether the argument is even or odd. For demonstration purposes the source code is divided into two files (`main.cpp' and `even.cpp'). A simple makefile is provided, so the program `even' can be built with command mut-gen make evenMake sure that the directory `/usr/local/mut/bin' is in the PATH before any directory containing the Clang compiler (programs `clang' and `clang++').In general, if you can build some (C/C++) software with command mut-gen build-commandThe injected mutations can be listed with command mut-list -s evenA mutant selector is composed of three parts: source code file name, mutation location number, and mutation index within the mutation location. For instance the selector `even.cpp:2:1' is valid for `even' program.A mutant can be executed by activating the corresponding mutant selector at program start. This can be done with the `mut-run' program. For example test-case argsthen you can execute the test case with mutant `selector' activated with command for m in m"; mut-run -s "$m" ./even 3; doneIn the research the main focus was on how mutation tools for C/C++ software can be integrated into development and test execution environments. Hence the current version injects only binary and unary operator replacement mutations. The video shows how the all mutants form of the LLVM/Clang compiler infrastructure can be built with mut-tools, how the Clang unit test cases can be executed without activating any mutants, and how unit test cases can be executed with some mutants activated.For further information, usage experience, development suggestions, and comments please don't hesitate tocontact `[email protected]
Conformational regulation of pol V Mut.
No full textThe first step in pol V Mut regulatory pathway requires transfer of a molecule of RecA from the 3'-tip of a RecA* nucleoprotein filament to pol V (UmuD'2C) to form pol V Mut (UmuD'2C-RecA). Pol V Mut exists in 3 conformational states determined by the orientation of RecA on pol V. When first assembled pol V Mut (UmuD'2C-RecA) is catalytically inactive (State 1) and cannot bind to p/t DNA. A subsequent addition of ATP (or ATPγS) activates pol V Mut = UmuD'2C-RecA-ATP (State 2) due to ATP induced reorientation of RecA relative to UmuC, termed “ATP induced RecA switch”. Once activated, pol V Mut can bind to p/t DNA and synthesize DNA, including TLS (X denotes a DNA template lesion). Pol V Mut can either statically deactivate in the absence of DNA synthesis (State 3) with a rate of about 0.02/min at 37°C or deactivate dynamically (State 3) in the presence of DNA synthesis (0.023/min at 37°C). Deactivated pol V Mut can be activated (i.e., reactivated) via transfer of a “new” molecule of RecA from the 3'-tip of a RecA* nucleoprotein filament, in which the new RecA replaces the old RecA [11], followed by binding of ATP/ATPγS. Deactivated pol V Mut cannot be reactivated by binding to ATP or ATPγS. Both deactivation processes occur more rapidly at 37°C compared to at 30°C. Deactivation is inhibited in the presence of bound ATP and accelerated in the presence of bound p/t DNA – see text.</p
Stability and evolvability of 5-mut and 5-mut T987A stable variant.
No full textA: In a background that is further away from evolving OmpF+ (two mutations reverted compared to one mutation in 6-mut), the T987A mutation is still stabilizing. B: In the 5-mut background, T987A reduces evolvability to an even greater extent. Two sample t-test for unequal variance, N = 3 per genotype, **: P = 0.0069.</p
The basolateral expression of mUT-A3 in the mouse kidney
No full textFacilitative UT-A urea transporters play a central role in the urinary concentrating mechanism. There are three major UT-A isoforms found in the mouse kidney: mUT-A1, mUT-A2, and mUT-A3. The major aim of this study was to identify the location and function of mUT-A3. UT-A proteins were investigated using three novel mouse UT-A-targeted antibodies: ML446, MQ2, and ML194. ML446 detected mUT-A1 and mUT-A3. ML194 detected mUT-A1 and mUT-A2. Importantly, MQ2 was found to be selective for mUT-A3. MQ2 detected a 45- to 65-kDa signal in the mouse kidney inner medulla, which was deglycosylated to a 40-kDa protein band. Immunolocalization studies showed that mUT-A3 was strongly detected in the papillary tip, mainly in the basolateral regions of inner medullary collecting duct (IMCD) cells. Immunoblotting of subcellular fractions of inner medullary protein suggested that in mouse kidney mUT-A3 was present in plasma membranes. Consistent with this, immunoelectron microscopy demonstrated that mUT-A3 was predominantly localized at the basal plasma membrane domains of the IMCD cells in mouse kidney. Heterologous expression of mUT-A3-enhanced green fluorescent protein in Madin-Darby canine kidney cells showed that the protein localized to the basolateral membrane. In conclusion, our study indicates that mUT-A3 is a basolateral membrane transporter expressed in IMCD cells
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