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Porin

Porins are a class of membrane transport proteins found in the outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts.
They form water-filled channels that allow the passive diffusion of small hydrophilic molecules across the membrane.
Porins play a crucial role in cellular nutrient uptake, waste excretion, and signal transduction.
Understanding porin structure, function, and regulation is essential for developing antimicrobial therapies and engineering applications in biotechnology.
Researchers can leverge the PubCompare.ai platform to optimize their porin research protocols, effortlessly locate relevent literature, and identify the best products and methods for their studies.

Most cited protocols related to «Porin»

1
Quadruple Immunofluorescence Quantification of OXPHOS
Cited 19 times
Quadruple immunofluorescence was carried out on transverse muscle sections (10 μm) using antibodies detecting subunits of OXPHOS complexes (Supplementary Table S1). Complex I was detected using an antibody against subunit NDUFB823 (link), and Complex IV using an antibody to mtDNA encoded subunit I (COX-I). Mitochondrial mass was quantified using an antibody to porin, an outer mitochondrial membrane voltage-gated ion channel. Laminin, a basement membrane glycoprotein, was used to label the myofibre boundaries (Supplementary Table S1). Briefly, the sections were fixed in cold 4% paraformaldehyde (Sigma) for 3 min and permeabilised in a methanol (Fisher) gradient (10 min 70% methanol, 10 min 95% methanol, 20 min 100% methanol, 10 min 95%.methanol and 10 min 70% methanol). Non-specific protein interactions were blocked with 10% normal goat serum (Sigma) and incubated with the primary antibodies in a humidified chamber at 4 °C overnight (Supplementary Table S1). Following washes in TBST (Sigma), the sections were incubated with the secondary antibodies for 2 h at 4 °C and subsequently with streptavidin conjugated with Alexa 647 (Life Technologies) for 2 h at 4 °C (Supplementary Table S1). The sections were washed and mounted in Prolong Gold (Sigma). No-primary antibody controls, incubated only with anti-laminin antibody, were processed for each muscle sample.
Rocha M.C., Grady J.P., Grünewald A., Vincent A., Dobson P.F., Taylor R.W., Turnbull D.M, & Rygiel K.A. (2015). A novel immunofluorescent assay to investigate oxidative phosphorylation deficiency in mitochondrial myopathy: understanding mechanisms and improving diagnosis. Scientific Reports, 5, 15037.
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Publication 2015
Antibodies Antibodies, Anti-Idiotypic Cold Temperature DNA, Mitochondrial Fluorescent Antibody Technique Glycoproteins Goat Gold Immunoglobulins Ion Channel Laminin Membrane, Basement Membrane Glycoproteins Methanol Mitochondria Mitochondrial Membrane, Outer Muscle Tissue NADH Dehydrogenase Complex 1 Oxidase, Cytochrome-c paraform Porin Proteins Protein Subunits PTGS1 protein, human Serum Streptavidin
2
FeGenie: Automated Iron Metabolism Identification
Cited 12 times
FeGenie is implemented in Python 3, with three required dependencies: HMMER v. 3.2.1 (Johnson et al., 2010 (link)), BLASTp v. 2.7.1 (Madden, 2013 ), and Prodigal v. 2.6.3 (Hyatt et al., 2010 (link)). External installation of these dependencies is not required if FeGenie is configured using Conda2. There are two optional dependencies, which must be installed externally: R (R Core Team, 2013 ) and Rscript (R Core Team, 2013 ). R packages used in FeGenie include argparse (Davis, 2018 ), ggplot2 (Wickham, 2009 ), ggdendro (de Vries and Ripley, 2016 ), reshape (Wickham, 2007 (link)), reshape2 (Wickham, 2007 (link)), grid (R Core Team, 2013 ), ggpubr (Kassambara, 2017 ), tidyverse (Wickham, 2017 ), and Pvclust (Suzuki and Shimodaira, 2006 (link)); users need to install these packages independently using Rscript (detailed instructions on this are available within the FeGenie Wiki3). The overall workflow of FeGenie is outlined in Figure 3. User-provided input to this program includes a folder of genomes or metagenomes, which must all be in FASTA format, comprised of contigs or scaffolds. Users can also submit amino acid gene sequences in FASTA or GenBank format. First, Prodigal (Hyatt et al., 2010 (link)) is used to predict open-reading frames (ORFs). A custom library of profile HMMs (library described in section “HMM Development: Building and Calibrating HMMs”) is then queried against these ORFs using hmmsearch (Johnson et al., 2010 (link)), with custom bit score cutoffs for each HMM. Additionally, genes shown to be involved in dissimilatory iron reduction but lacking sufficient homologs in public repositories (precluding us from building reliable HMMs) are queried against the user-provided dataset using BLASTp (Madden, 2013 ) with a default e-value cutoff of 1E-10. These genes include the S-layer proteins implicated in iron reduction in Thermincola potens JR (Carlson et al., 2012 (link)), as well as porin-cytochrome encoding operons implicated in iron reduction in Geobacter spp. (Shi et al., 2014 (link)). The results of hmmsearch (Johnson et al., 2010 (link)) and BLAST (Madden, 2013 ) are then analyzed and candidate gene neighborhoods identified. Potential for dissimilatory iron oxidation and reduction is determined based on a set of rules that are summarized in Supplementary Table S3. Even though the sensitivity of each HMM has been calibrated against NCBI’s nr database (see section “HMM Development: Building and Calibrating HMMs” for details on the calibration process), we recommend that users take advantage of an optional cross-validation feature of the program that allows users to search each FeGenie-identified putative iron gene against a user chosen database of reference proteins (e.g., NCBI’s nr, RefSeq). Based on these analyses, FeGenie outputs the following files:
Garber A.I., Nealson K.H., Okamoto A., McAllister S.M., Chan C.S., Barco R.A, & Merino N. (2020). FeGenie: A Comprehensive Tool for the Identification of Iron Genes and Iron Gene Neighborhoods in Genome and Metagenome Assemblies. Frontiers in Microbiology, 11, 37.
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Publication 2020
Amino Acid Sequence Cytochromes DNA Library Genes Genome Geobacter Hypersensitivity Hypertelorism, Severe, With Midface Prominence, Myopia, Mental Retardation, And Bone Fragility Iron Metagenome Open Reading Frames Operon Porin Python S-layer proteins Thermincola potens
3
Structural Determination of CLC-ec1 Chloride Channel
Cited 8 times
CLC-ec1 and variants were expressed in E. coli, purified, and crystallized after complexation with a FAB fragment of antibody 10EC3/G4 (National Cell Culture Center), as previously described (Dutzler et al., 2003 (link)). Crystals were harvested after 1–3 weeks at 20°C and were frozen in liquid nitrogen. Crystallographic datasets were collected at the Swiss Light Source or the Advanced Photon Source, using radiation at the Br absorption edge (0.919 Å). Diffraction images were indexed and integrated in the HKL program, and electron density and anomalous difference maps were calculated in the CCP4 suite, after molecular replacement with PHASER and refinement with REFMAC5, using the wild-type CLC-ec1-FAB model (accession no. 1OTS) and twofold NCS restraints for the CLC homodimer. The refined model was also minimally rebuilt using sigmaa-weighted 2Fo-Fc and Fo-Fc maps in the COOT program. Model bias was suppressed by prime-and-switch density modification in the SOLVE/RESOLVE program within the PHENIX suite (Terwilliger, 2000 (link)).
CLC-ec1 ion transport functions were assayed by 36Cl− and H+ fluxes in liposomes and voltage-clamped currents in planar lipid bilayers as previously described (Accardi et al., 2004 (link); Accardi and Miller, 2004 (link)); in preparations used for lipid bilayer experiments, an anion-exchange chromatography step was used in lieu of gel filtration to remove outer membrane porins (Accardi and Miller, 2004 (link)). Figures were produced in PyMOL Molecular Graphics (DeLano Scientific, http://www.pymol.org).
Accardi A., Walden M., Nguitragool W., Jayaram H., Williams C, & Miller C. (2005). Separate Ion Pathways in a Cl−/H+ Exchanger. The Journal of General Physiology, 126(6), 563-570.
Publication 2005
Absorption, Radiation Anions Cell Culture Techniques Chromatography Crystallography Electrons Escherichia coli Freezing Gel Chromatography Immunoglobulins, Fab Ion Transport Light Lipid Bilayers Liposomes Microtubule-Associated Proteins Nitrogen Porin Tissue, Membrane
4
Purification of E. coli Chloride Channel
Cited 8 times
The DNA sequence encoding CLC-ec1, the protein product of E. coli gene b0155 (now designated clcA in the E. coli genome database) was inserted into the pASK-IBA2 vector (Sigma-Aldrich) between the XbaI and HindII sites (Maduke et al., 1999 (link)). Appended to a deletion of the last five residues of the natural CLC-ec1 sequence was a linker containing LysC and thrombin sites followed by a hexahistine tag, to yield the final COOH-terminal sequence …LARSKAAKGSGTLVPRGSGLEHHHHHH. Mutations E148A and E148Q were generated using standard two-step PCR.
CLC-ec1 was expressed after plasmid transformation into in an adventitiously generated variant strain of commercially available DE3 cells derived from Stratagene lot # 0420399. This strain, which we denote Por-No, was used because it produces the lowest amounts of contaminating outer membrane porins we have observed from many strains tested. For a typical 3 liter prep, cells from the transformation plates were inoculated into 2-liter baffled flasks, each containing 1 liter Terrific broth (Sambrook et al., 1989 ) with ampicillin (100 μg/ml) and grown at 37°C. When OD600 reached 1.6–1.9, cells were induced 3 h with 0.2 mg/L anhydrotetracycline. Cells were collected by centrifugation and stored overnight at 4°C. The next morning they were resuspended in 50 ml TrisCl, 100 mM NaCl, pH 7.5, and disrupted by sonication on ice in presence of leupeptin (20 μg/ml), pepstatin (20 μg/ml), and PMSF (∼0.2 mg/ml). All further operations were performed at room temperature. Protein was extracted for 2 h at room temperature with gentle shaking in presence of 50 mM DM, and the extract was centrifuged at 16,000 rpm for 45 min. The supernatant was loaded onto a 3-ml Cobalt column (BD Biosciences), at a flow rate of 2 ml/min, which had been washed previously with 5 vol of 40 mM TrisCl, 200 mM NaCl, 10 mM DM, pH 7.5 (WB). After washing with 10–15 vol of WB, nonspecifically bound proteins were eluted with 10 vol of WB containing 30 mM imidazole. The protein was then eluted with WB containing 400 mM imidazole and concentrated to a final volume of ∼0.5 ml in a centrifugal membrane concentrator. The hexahistidine tag was cleaved by digestion with LysC (0.5 U) for 1 h. The resulting product was diluted 20-fold in 10 mM DM and loaded on a 1 ml Poros HQ high-capacity anion exchange column preequilibrated with 10 volumes of 30 mM NaCl, 10 mM TrisCl, 10 mM DM, pH 7.5 (LoQ). The column was washed with 30 volumes of LoQ and the protein was eluted applying a salt gradient between LoQ and HiQ Buffers (300 mM NaCl, 10 mM TrisCl, 10 mM DM, pH 7.5), 30 ml each. The resulting CLC-ec1 peak was fractioned into 5 separate aliquots (2 ml each). Only the aliquots corresponding to the rising phase of the elution peak were concentrated and used for bilayer work.
Accardi A., Kolmakova-Partensky L., Williams C, & Miller C. (2004). Ionic Currents Mediated by a Prokaryotic Homologue of CLC Cl− Channels. The Journal of General Physiology, 123(2), 109-119.
Publication 2004
Ampicillin anhydrotetracycline Anions Buffers Cells Centrifugation Cloning Vectors Cobalt Cultured Cells Digestion DNA Sequence Escherichia coli Escherichia coli Proteins Genome His-His-His-His-His-His imidazole leupeptin Mutation pepstatin Plasmids Porin Proteins Sequence Deletion Sodium Chloride Strains Thrombin Tissue, Membrane
5
Immunoblotting of Native and Denatured Proteins
Cited 7 times
For immunoblotting of samples in blue native gels, protein complexes from 3–12% precast Bis–Tris Native PAGE gels (Life Technologies) were transferred to polyvinylidene difluoride membranes (Bio-Rad). For immunoblotting of denatured samples in whole tissue lysates, thoraxes were homogenized in radioimmunoprecipitation assay buffer (150-mM NaCl, 1% Triton X-100, 0.5% sodium deoxycholate, 0.1% SDS, and 50-mM Tris-HCl, pH 8) supplemented with Halt protease inhibitors (Pierce), resolved on mini-PROTEAN TGX stain-free gels from Bio-Rad, and transferred to polyvinylidene difluoride membranes. In both instances (native and nonnative gels), the membrane was subsequently blocked in 5% (wt/vol) nonfat dry milk in TBS for 30 min and incubated in the appropriate primary antibody dissolved in 2% BSA and 0.1% Tween 20 in TBS (TBST) overnight at 4°C. Following the overnight incubation, the blot was rinsed four times for 10 min each in 0.1% TBST, blocked for 30 min in 5% (wt/vol) nonfat dry milk in TBST, and incubated for 2 h with the appropriate HRP-conjugated secondary antibody dissolved in 2% BSA and 0.1% TBST. After incubation in the secondary antibody, samples were rinsed four times for 10 min each in 0.1% TBST. Immunoreactivity was detected by ECL and analyzed by a ChemiDoc Gel imaging system from Bio-Rad. Primary antibodies used were anti-NDUFS3 (Abcam, ab14711), anti-ATPsynβ (Life Technologies, A-21351), anti-VDAC1/Porin (Abcam, ab14734), anti–cytochrome C (Abcam, ab13575), anti-Hsp60 (Cell Signaling Technology, 4869S), anti-Hsp90 (Cell Signaling Technology, 4874S), and the rabbit polyclonal antibodies generated by Biomatik. Secondary antibodies used were goat anti-rabbit HRP (Pierce, PI31460) and goat anti-mouse HRP (Pierce, PI31430). There are major discrepancies between the migration behavior of membrane and soluble protein markers. Accordingly, estimating the sizes of membrane proteins such as OXPHOS complexes or AIs on blue native gels using standard soluble protein markers produces spurious results. Consequently, we chose not to estimate the sizes of proteins on blue native gels using standard protein markers. OXPHOS complexes and AIs were assessed based on their known constituent protein subunits.
Murari A., Rhooms S.K., Goparaju N.S., Villanueva M, & Owusu-Ansah E. (2020). An antibody toolbox to track complex I assembly defines AIF’s mitochondrial function. The Journal of Cell Biology, 219(10), e202001071.
Publication 2020
Antibodies Bistris Buffers Chest Cytochromes c Deoxycholic Acid, Monosodium Salt Gels Goat HSP90 Heat-Shock Proteins Immunoglobulins Membrane Proteins Milk, Cow's Mus Native Polyacrylamide Gel Electrophoresis polyvinylidene fluoride Porin Protease Inhibitors Proteins Protein Subunits Rabbits Radioimmunoprecipitation Assay Sodium Chloride Stains Tissue, Membrane Tissues Triton X-100 Tromethamine Tween 20 VDAC1 protein, human

Most recents protocols related to «Porin»

1
Vacuolar Isolation and GFP-Sch9 Analysis
Vacuoles of GFP-Sch9 expressing WT, pho85Δ, and fab1Δ cells were isolated as described before [130 (link)], with the exception of some minor changes. Yeast cultures were grown in YPD to approximately OD600nm 1. Cells were harvested, washed once, and resuspended in 0,03 M Tris-HCl pH 8,9 containing 10 mM DTT. After a 10 min incubation at 30°C, cells were incubated at 30°C in spheroplasting buffer (YP 0.2% glucose; 0.6 M sorbitol; 50 mM KPi; 0.1 mM pefabloc; 6U zymolyase/OD600nm unit) for at least 30 min. The collected spheroplastes are resuspended in 15% ficoll buffer (15% ficoll; 10 mM PIPES/KOH pH 6.8; 0.2 M sorbitol; 0.1 mM pefabloc, 0.1 μg/ml leupeptin, 10 μg/ml o-phenantrolin, 0.5 μg/ml pepstatin A), to which 50 μl of 0.4 mg/ml diethylaminoethyl (DEAE) dextran was added per 100 OD600nm units of cells. After 2 min incubation on ice, followed by 2 min at 30°C, the spheroplast suspension was transferred to a transparent SW41 tube (Beckman Coulter, Suarlée, Belgium). 8% ficoll buffer, 4% ficoll buffer and 0% ficoll buffer were pipetted carefully on top to create a discontinuous ficoll gradient. The samples were centrifuged for 90 min at 30’000 rpm in a SW41 rotor, at 4°C (Beckman Coulter, Suarlée, Belgium). After collecting the vacuolar fraction from the 0% - 4% ficoll interphase, vacuolar vesicles were further concentrated by diluting ½ in 10 mM PIPES/KOH pH 6.8 and centrifugation for 10 min at 5200g, 4°C. The purity of the isolated vacuolar vesicles was monitored by Western analysis, using Anti-Vph1 (Abcam, Cambridge, UK), anti-ATP6V1A (Abcam, Cambridge, UK), anti-Porin (Invitrogen, Thermo Fisher Scientific, Merelbeke, Belgium), anti-Pma1 (kindly provided by B. André), anti-Dpm1 (Invitrogen, Thermo Fisher Scientific, Merelbeke, Belgium). Total protein concentrations were measured with the Bradford method (Bio-Rad, Temse, Belgium). The obtained vacuolar vesicles were diluted to 0.1 μg/μl in 10 mM PIPES/KOH pH 6.8 and stained with 8 μM FM4-64 (Invitrogen, Thermo Fisher Scientific, Merelbeke, Belgium). GFP and FM4-64 signal intensity was measured with the Fluoroskan Ascent FL Microplate Fluorometer (Thermo Fisher Scientific, Merelbeke, Belgium), using a 485/518 filter pair and 530/645 filter pair respectively. The GFP ratio’s relative to FM4-64 or protein content in each sample was determined to serve as a measure of GFP-Sch9 abundance at the vacuolar membrane.
Deprez M.A., Caligaris M., Rosseels J., Hatakeyama R., Ghillebert R., Sampaio-Marques B., Mudholkar K., Eskes E., Meert E., Ungermann C., Ludovico P., Rospert S., De Virgilio C, & Winderickx J. (2023). The nutrient-responsive CDK Pho85 primes the Sch9 kinase for its activation by TORC1. PLOS Genetics, 19(2), e1010641.
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Publication 2023
Buffers Cells Centrifugation DEAE-Dextran Ficoll FM 4-64 Glucose Interphase leupeptin Pefabloc pepstatin piperazine-N,N'-bis(2-ethanesulfonic acid) Porin Proteins Sorbitol Spheroplasts Tissue, Membrane Tromethamine Vacuole Yeast, Dried zymolyase
2
Western Blotting for Proteomic Analysis
For Western blotting, samples were homogenized in RIPA buffer (150 mM NaCl, 50 mM Tris-HCl, 6 mM EDTA, 1% NP-40, 0.1% SDS, 0.5% deoxycholic acid, pH 8.0) containing inhibitors of proteases (Roche Diagnostics GmbH, Mannheim, Germany) and centrifuged for 10 min at 14,000× g at 4 °C. In all, 15–50 μg of protein lysates, determined by BCA assay (Invitrogen-ThermoFisher Scientific, Waltham, MA, USA) was denatured and separated by electrophoresis using 8–16% Tris-Glycine Mini Gels (Invitrogen-ThermoFisher Scientific, Waltham, MA, USA) and then electro-blotted onto PVDF membranes (Bio-Rad Laboratories Inc., Hercules, CA, USA). Membranes were blocked with TBS/0.1%-Tween20 (TTBS) containing 5% non-fat dry milk before overnight incubation with the specified antibodies. Peroxidase-conjugated anti-mouse and anti-rabbit secondary antibodies (Jackson ImmunoResearch, Laboratories Inc., Cambridge, UK) were added for 1 h at room temperature in the same buffer as used for the primary antibodies (2.5% non-fat dry milk in TTBS). Reactive bands were detected using Clarity MaxTM Western ECL Substrate (Bio-Rad Laboratories Inc., Hercules, CA, USA), according to the manufacturer’s instructions. Densitometry of Western blot bands was performed with the ImageJ software. Primary antibodies used for Western blotting analysis were as follows: REEP1 (Sigma-Aldrich, St. Louis, MO, USA, #SAB2101976; dilution 1:1000); total DRP1 (BD Transduction Laboratories, Oxford, UK, #611112; dilution 1:500); DRP1 Ser 637 (Byorbyt #orb127984; dilution 1:500). Immunodetection with porin antibody (MitoSciences, Eugene, OR, USA, #MSA05; dilution 1:5000) served as a loading control to normalize the bands intensity.
Naef V., Meschini M.C., Tessa A., Morani F., Corsinovi D., Ogi A., Marchese M., Ori M., Santorelli F.M, & Doccini S. (2023). Converging Role for REEP1/SPG31 in Oxidative Stress. International Journal of Molecular Sciences, 24(4), 3527.
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Publication 2023
Anti-Antibodies Antibodies Biological Assay Buffers Densitometry Deoxycholic Acid Diagnosis Edetic Acid Electrophoresis Gels Glycine Immunoglobulins Mice, House Milk, Cow's Nonidet P-40 Peroxidase polyvinylidene fluoride Porin Protease Inhibitors Proteins Rabbits Radioimmunoprecipitation Assay Sodium Chloride Technique, Dilution Tissue, Membrane Tromethamine Tween 20 Western Blot Western Blotting
3
Muscle Protein Extraction and Analysis
Homogenates for Western blot analyses were obtained from muscle. Tissues samples were homogenized in 10 vol of lysis buffer [10 mM Tris (pH 7.2), 150 mM NaCl, 1% Triton X-100, 0.1% SDS, 5 mM EDTA, 2 mM sodium orthovanadate, 50 mM NaF, 20 mM sodium pyrophosphate, and protease inhibitors mixture tablet (Roche)] with a mini-beadbeater (Biospec) twice for 30 s. Homogenates were rotated for 1 h at 4 °C in an orbital shaker and centrifuged at 16,000×g for 15 min at 4 °C. Supernatants were aliquoted and kept at −20 °C.
Proteins from total homogenates and the mitochondria isolation fraction were resolved in 10%, 12.5% or 15% acrylamide gels for SDS/PAGE and transferred to Immobilon membranes (Millipore). The following antibodies were used: Oxphos (abcam ab110413), ND2 (Proteintech 16879184), ATP6 (Millipore MABS1995), VDAC/Porin (Santa cruz 73614), Vinculin (Santa cruz 73614), LARS2 (Proteintech 17097-1-AP), TARS2 (Proteintech 15067-1-AP), NOS2 (Santa cruz sc-7271), NOS3 (BD Transduction 610296).
López-Soldado I., Torres A.G., Ventura R., Martínez-Ruiz I., Díaz-Ramos A., Planet E., Cooper D., Pazderska A., Wanic K., O'Hanlon D., O'Gorman D.J., Carbonell T., de Pouplana L.R., Nolan J.J., Zorzano A, & Hernández-Alvarez M.I. (2023). Decreased expression of mitochondrial aminoacyl-tRNA synthetases causes downregulation of OXPHOS subunits in type 2 diabetic muscle. Redox Biology, 61, 102630.
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Publication 2023
Acrylamide Antibodies Buffers Edetic Acid Gels Immobilon isolation Mitochondria Muscle Tissue Nitric Oxide Synthase Type II NOS3 protein, human Orthovanadate Porin Protease Inhibitors Proteins SDS-PAGE Sodium Sodium Chloride sodium pyrophosphate Tablet Tissue, Membrane Tissues Triton X-100 Tromethamine VCL protein, human Western Blot
4
Western Blot Analysis of OXPHOS Proteins
Protein isolation is described in the supplementary methods. Samples were prepared with 4× Laemmli Sample Buffer (Bio-Rad) and 30 µg protein loaded onto 12% hand-cast tris-glycine gels, transferred to a mini PVDF membrane with a Trans-Blot Turbo transfer system (Bio-Rad) using the standard 30 min protocol. Membranes were probed with antibodies to recognize components of the OXPHOS system: NDUFA9 (1:500, ab14713, Abcam), MTCO1 (1:500, ab14705, Abcam), porin/VDAC1 (1:1000, ab15895, Abcam), ATP5A (1:1000, ab14748, Abcam), and β-actin (1:2000, A1978, Sigma-Aldrich). Membranes were incubated with fluorescent secondary antibodies: IRDye 680RD Goat Anti-Rabbit and IRDye 800RD Goat Anti-Mouse (1:5000, 926-68071 and 926-32210 respectively, LI-COR Biosciences). Blots were imaged using a LI-COR Odyssey CLx imaging system and analyzed with LI-COR image studio.
Van Haute L., O’Connor E., Díaz-Maldonado H., Munro B., Polavarapu K., Hock D.H., Arunachal G., Athanasiou-Fragkouli A., Bardhan M., Barth M., Bonneau D., Brunetti-Pierri N., Cappuccio G., Caruana N.J., Dominik N., Goel H., Helman G., Houlden H., Lenaers G., Mention K., Murphy D., Nandeesh B., Olimpio C., Powell C.A., Preethish-Kumar V., Procaccio V., Rius R., Rebelo-Guiomar P., Simons C., Vengalil S., Zaki M.S., Ziegler A., Thorburn D.R., Stroud D.A., Maroofian R., Christodoulou J., Gustafsson C., Nalini A., Lochmüller H., Minczuk M, & Horvath R. (2023). TEFM variants impair mitochondrial transcription causing childhood-onset neurological disease. Nature Communications, 14, 1009.
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Publication 2023
Actins Antibodies CD3EAP protein, human Fluorescent Antibody Technique Gels Glycine Goat isolation Laemmli buffer Mice, House polyvinylidene fluoride Porin Proteins Rabbits Tissue, Membrane Tromethamine VDAC1 protein, human
5
Comprehensive Genomic Analysis of E. hormaechei
Long read sequencing data were assembled using the HGAP4 De Novo Assembly Application (Pacific Biosciences) with a minimum seed coverage of 30×. Short read trimmed sequences were assembled using SPAdes version 3.14 with read error correction enabled (48 (link)).
Accurate species identification was performed through Average Nucleotide Identity (ANI) testing. FastANI tool was used to generate a distance matrix of ECC isolates against Refseq complete E. hormaechei and E. cloacae genomes (Table S1) (49 (link)). Subsequently, the assembled genomes were uploaded and annotated with the RASTtk (http://rast.nmpdr.org). ResFinder 4.1 (https://cge.food.dtu.dk/services/ResFinder/) and the comprehensive antibiotic resistance database (CARD) were used to assess resistance determinants in all the isolates (50 (link), 51 (link)). Sequences of the omp35 and omp36 porin genes were extracted from the K. aerogenes genomes, and sequences were translated to detect nonsynonymous mutations using the translate webtool available at the Bioinformatics resource portal (https://web.expasy.org/translate/). Putative K-types and virulence determinants (yersiniabactin and colibactin) were inferred with the Kleborate and Kaptive (52 (link)).
Merhi G., Amayri S., Bitar I., Araj G.F, & Tokajian S. (2023). Whole Genome-Based Characterization of Multidrug Resistant Enterobacter and Klebsiella aerogenes Isolates from Lebanon. Microbiology Spectrum, 11(1), e02917-22.
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Publication 2023
Antibiotic Resistance, Microbial colibactin Enterobacter Genes Genome Mutation Nucleotides Porin Radioallergosorbent Test R Factors Virulence Factors yersiniabactin

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Porin by Abcam
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Porin is a lab equipment product. It is a membrane protein that forms large pores in the outer membrane of mitochondria, allowing the passage of small molecules and ions.
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Ab14705 is an immunohistochemistry and immunocytochemistry validated anti-EGFR antibody. It recognizes the epidermal growth factor receptor (EGFR) protein.
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Anti-Porin is a laboratory equipment product that functions as a protein. It is used in the study and analysis of bacterial cell membranes.
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VDAC1/Porin is a protein that forms a voltage-dependent anion channel in the outer mitochondrial membrane. It is involved in the regulation of metabolite transport across the mitochondrial membrane.
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Anti vdac1 porin by Abcam
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Anti-VDAC1/Porin is a primary antibody that recognizes the VDAC1 (Voltage-Dependent Anion Channel 1) protein, also known as Porin. VDAC1 is a mitochondrial outer membrane protein that functions as a channel, facilitating the exchange of metabolites, ions, and small molecules between the mitochondria and the cytosol.

More about "Porin"

Porins are a class of membrane transport proteins found in the outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts.
These water-filled channels allow the passive diffusion of small hydrophilic molecules across the membrane, playing a crucial role in cellular nutrient uptake, waste excretion, and signal transduction.
Understanding porin structure, function, and regulation is essential for developing antimicrobial therapies and engineering applications in biotechnology.
Researchers can leverage the PubCompare.ai platform to optimize their porin research protocols, effortlssly locate relevant literature, and identify the best products and methods for their studies.
The platform's AI-driven comparisons and intelligent tools can help researchers take their porin research to new heights, enabling them to discover the power of this versatile protein.
Synonyms and related terms include β-barrel proteins, outer membrane proteins (OMPs), voltage-dependent anion channels (VDACs), and mitochondrial porins.
Abbreviations like OMP and VDAC are commonly used in the field.
Key subtopics include porin structure and topology, transport mechanisms, regulation, and applications in areas such as antibiotics, bioremediation, and biosensors.
Researchers can also explore related resources like Ab15895 (anti-β-actin antibody), Ab14705 (anti-porin antibody), Ab14734 (anti-VDAC1/porin antibody), and the Odyssey Infrared Imaging System for Western blot analysis of porin proteins.
PVDF membranes are commonly used for protein transfer and detection in porin research.
By leveraging these tools and resources, scientists can advance their understanding and applications of this important class of membrane proteins.