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APT
APT
APT (Advance Persistent Threat) refers to a sophisticated, long-term cyberattack aimed at specific organizations or individuals.
These attacks are typically carried out by well-resourced and highly skilled adversaries, such as nation-states or advanced hacker groups.
APTs often involve stealthy infiltration, lateral movement within a network, and the extraction of sensitive data over an extended period.
They employ a wide range of techniques, including social engineering, malware, and exploits, to remain undetected and maintain persistent access.
Understanding the characteristics and mitigation strategies of APTs is crucial for enhancing cybersecurity and protecting against these advanced, targeted threats.
These attacks are typically carried out by well-resourced and highly skilled adversaries, such as nation-states or advanced hacker groups.
APTs often involve stealthy infiltration, lateral movement within a network, and the extraction of sensitive data over an extended period.
They employ a wide range of techniques, including social engineering, malware, and exploits, to remain undetected and maintain persistent access.
Understanding the characteristics and mitigation strategies of APTs is crucial for enhancing cybersecurity and protecting against these advanced, targeted threats.
Most cited protocols related to «APT»
Acrylamide
APT
Electrophoresis
Exoglycosidases
Homo sapiens
Mannose
Polysaccharides
Sialic Acids
Ammonium Hydroxide
APT
Bath
Glucose
Neoplasm Metastasis
Silver
Silver Nitrate
Sodium Hydroxide
Teflon
Various sources of plant cell wall polysaccharides were used for the characterisation of LM27 and LM28 using ELISAs. These included tamarind xyloglucan (100403, Megazyme International), maize xylan (McCartney et al. 2005 (link)), birchwood xylan (X0502, Sigma-Aldrich), rye arabinoxylan (20601b, Megazyme International) and oat spelt xylan (95590, Sigma-Aldrich). Individual xylan-derived aldouronic acid oligosaccharides were a kind gift from Sanna Koutaniemi (Koutaniemi et al. 2012 (link)), and a mixture of aldouronic acids (tri:tetra:penta—2:2:1) was obtained from Megazyme.
The Arabidopsis thaliana triple mutant in gxm1gxm2gxm3 was generated by crossing single mutants prepared in Li et al. (2013 (link)). The insertion lines are SALK_087114 (gxm1, At1g33800), SALK_084669 (gxm2, At4g09990) and SALK_050883 (gxm3, At1g09610). Plants from the triple mutant line were grown for 6 weeks, and 5-cm of basal inflorescence stem was harvested. The alcohol-insoluble residue (AIR) was obtained and pre-treated with alkali and digested with a GH11 xylanase as described (Mortimer et al. 2010 (link)). After GH11 digestion, resulting sugars were derivatised by 9-aminopyrene-1, 4, 6-trisulfonate (APTS) and analysed by DNA sequencer-Assisted Saccharide analysis in high throughput, DASH (Li et al. (2013 (link)). GH11 products of stem AIR digestion were deuteropermethylated and analysed by MALDI-TOF-Mass Spectrometry as described (Tryfona et al. 2010 (link)).
The Arabidopsis thaliana triple mutant in gxm1gxm2gxm3 was generated by crossing single mutants prepared in Li et al. (2013 (link)). The insertion lines are SALK_087114 (gxm1, At1g33800), SALK_084669 (gxm2, At4g09990) and SALK_050883 (gxm3, At1g09610). Plants from the triple mutant line were grown for 6 weeks, and 5-cm of basal inflorescence stem was harvested. The alcohol-insoluble residue (AIR) was obtained and pre-treated with alkali and digested with a GH11 xylanase as described (Mortimer et al. 2010 (link)). After GH11 digestion, resulting sugars were derivatised by 9-aminopyrene-1, 4, 6-trisulfonate (APTS) and analysed by DNA sequencer-Assisted Saccharide analysis in high throughput, DASH (Li et al. (2013 (link)). GH11 products of stem AIR digestion were deuteropermethylated and analysed by MALDI-TOF-Mass Spectrometry as described (Tryfona et al. 2010 (link)).
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Acids
Alcohols
Alkalies
APT
Arabidopsis thalianas
arabinoxylan
Carbohydrates
Cell Wall
Digestion
Enzyme-Linked Immunosorbent Assay
Ethanol
Inflorescence
Maize
Mass Spectrometry
natural heparin pentasaccharide
Oligosaccharides
Plants
Polysaccharides
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Stem, Plant
Sugars
Tamarindus indica
Tetragonopterus
Triticum spelta
Xylanase A
Xylans
xyloglucan
Safety analyses were based on the all-patients-treated set (APTS), comprising all randomized patients who took at least one dose of study medication. Efficacy analyses were based on a modified intention-to-treat set – the full-analysis set (FAS), comprising all patients in the APTS who had at least one valid post-baseline assessment of the primary efficacy variable (the DSST and the RAVLT [acquisition and delayed recall]).
The primary efficacy analysis was the change from baseline to week 8 in the composite z-score defined as the equally weighted sum of the z-scores in the DSST and RAVLT, thus assessing a broad range of cognitive domains, including executive function, attention, processing speed, and learning and memory. The DSST score was assigned a weight of 0.5, and the two subtest scores of the RAVLT (acquisition [learning] and delayed recall [memory]) were each assigned a weight of 0.25. The composite z-score is used for the first time in this study and is based on post-hoc analysis of the vortioxetine study of elderly patients with MDD (Katona et al., 2012 (link)). Based on a Missing-at-Random assumption, these analyses were performed using all available data from all patients in the FAS. The model included treatment and center as fixed factors. The baseline composite z-score was used as a covariate. Interactions between visit and treatment and baseline composite z-score were also included in the model. An unstructured covariance structure was used to model the within-patient variation. For endpoints that occurred after the pre-specified statistical testing procedure was stopped or that were outside the testing procedure, nominal p-values with no adjustment for multiplicity were reported. The phrasing ‘separation from placebo’ is used to describe findings with p < 0.05. Efficacy analyses that were not multiplicity-controlled were considered secondary. For details of the testing hierarchy and descriptions of key secondary and secondary analyses, multiple regression analyses [path analysis] and post-hoc sub-group analyses, see the Supplementary Material.
The sample size calculation was based on an overall significance level of 5% by having 2.5% within each dose in order to adjust for multiplicity. For the primary endpoint (composite z-score), the treatment difference to placebo for each vortioxetine dose at week 8 was assumed to be 0.25, based on the results with elderly patients (Katona et al., 2012 (link)). A total of 600 patients (200 per arm) were needed for the mixed model for repeated measures (MMRM) using all available data to provide a power of ≈90% for finding at least one dose significant, and a power of ≈85% for finding a specific dose significant, assuming a 20% withdrawal rate.
The primary efficacy analysis was the change from baseline to week 8 in the composite z-score defined as the equally weighted sum of the z-scores in the DSST and RAVLT, thus assessing a broad range of cognitive domains, including executive function, attention, processing speed, and learning and memory. The DSST score was assigned a weight of 0.5, and the two subtest scores of the RAVLT (acquisition [learning] and delayed recall [memory]) were each assigned a weight of 0.25. The composite z-score is used for the first time in this study and is based on post-hoc analysis of the vortioxetine study of elderly patients with MDD (Katona et al., 2012 (link)). Based on a Missing-at-Random assumption, these analyses were performed using all available data from all patients in the FAS. The model included treatment and center as fixed factors. The baseline composite z-score was used as a covariate. Interactions between visit and treatment and baseline composite z-score were also included in the model. An unstructured covariance structure was used to model the within-patient variation. For endpoints that occurred after the pre-specified statistical testing procedure was stopped or that were outside the testing procedure, nominal p-values with no adjustment for multiplicity were reported. The phrasing ‘separation from placebo’ is used to describe findings with p < 0.05. Efficacy analyses that were not multiplicity-controlled were considered secondary. For details of the testing hierarchy and descriptions of key secondary and secondary analyses, multiple regression analyses [path analysis] and post-hoc sub-group analyses, see the Supplementary Material.
The sample size calculation was based on an overall significance level of 5% by having 2.5% within each dose in order to adjust for multiplicity. For the primary endpoint (composite z-score), the treatment difference to placebo for each vortioxetine dose at week 8 was assumed to be 0.25, based on the results with elderly patients (Katona et al., 2012 (link)). A total of 600 patients (200 per arm) were needed for the mixed model for repeated measures (MMRM) using all available data to provide a power of ≈90% for finding at least one dose significant, and a power of ≈85% for finding a specific dose significant, assuming a 20% withdrawal rate.
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Aged
APT
Attention
Cognition
Executive Function
Memory
Mental Recall
Patients
Placebos
Safety
Vortioxetine
Most recents protocols related to «APT»
Human milk samples for HMO analysis were obtained by manual milk expression by the mother into a clean plastic container. The samples were kept cool until homogenization by the study team. They were then split into 1–2 mL portions and stored at −20°C. All aliquots were stored at −20°C at the study site until shipment on dry ice to the ETH Zurich, Switzerland. For the HMO composition analysis reported here, the HM samples were transported on dry ice to the glycoanalytical laboratory (glyXera GmbH, Magdeburg, Germany). The qualitative and quantitative HMO composition of each individual HM sample was determined with the glyXboxCE™ system (glyXera GmbH, Magdeburg, Germany) based on multiplexed capillary gel electrophoresis with laser-induced fluorescence detection (xCGE-LIF).73 (link) In accordance with the glyXera GmbH kit protocol (KIT-glyX-OS.P-APTS, glyXera GmbH, Magdeburg, Germany), the pure HM samples were diluted 1:100, spiked with an internal standard (IS) (oligosaccharide (OS) quantification standard solution, OS-A5-N-1 mL-01; part of the KIT-glyX-Quant-DP5, all from glyXera GmbH, Magdeburg, Germany) and treated with a denaturation solution. The free OS were labeled with 8-aminopyrene-1,3,6-trisulfonic acid (APTS), purified and determined with the glyXbox™ system. All measurements included the addition of a migration time alignment standard (glyXalign4; STD-glyXalign-4-S, glyXera GmbH) to the sample. Finally, glyXtoolGUI™ software (Beta v0.8.11, glyXera GmbH, Magdeburg, Germany) was used for the processing and analysis of the HMO Fingerprints data (normalized electropherograms). The limit of quantification (LOQ) was determined from the signal-to-noise ratio (SNR) of each HMO Fingerprint calculated as described by Ullsten et al.74 (link) The LOQ was defined as an SNR of 10 and the limit of detection (LOD) was defined as an SNR of 3. The respective noise for each sample was determined after migration time alignment of the unsmoothed data in the late migration time range (approximation range = degree of polymerization (DP) 18< DP<20). Peaks with intensities below the LOQ but above the LOD were picked. All peaks ≥LOQ were considered and their IS-normalized peak areas were calculated (as percentages relative to the peak area of the IS [% IS] (= nPA)). All peaks ≥LOD but 75 (link) All HM samples were assigned to a maternal secretor and Lewis (Se/Le) phenotype (HM groups I–IV) based on the presence or absence of specific α1-2- and/or α1-4-fucosylated HMOs, as previously described.73 (link) The assignment of maternal secretor status was based on the presence of 2’-fucosyllactose (2’-FL), difucosyllactose (DFL), and lacto-N-fucopentaose (LNFP) I, and the determination of Lewis status was based on the presence of LNFP II and lacto-N-difucohexaose (LNDFH) II. Differences in HMO abundance between maternal secretor status and HM types were assessed with Mann-Whitney tests or Kruskal-Wallis tests followed by post-hoc Dunn’s test, respectively, with adjustment for false discovery rate (FDR) by the Benjamini-Hochberg mechanism (FDR<0.05).
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Acids
APT
Dry Ice
Electrophoresis, Capillary
Fluorescence
lacto-N-fucopentaose I
lacto-N-fucopentaose II
Milk
Milk, Human
Mothers
Oligosaccharides
Phenotype
Polymerization
Ten glucoside hydrolases were screened regarding their ability to digest APTS-labeled maltodextrins and dextrans under different reaction conditions, i.e., buffers. Tested glucoside hydrolases were: α-amylase II-A (0.15 U/μL), α-amylase IX-A (1 U/μL), α-amylase XIII-A (1 U/μL), α-glucosidase (1 U/μL), β-amylase (1 U/μL), oligo-1,6-glucosidase (1 U/μL), oligo-α-(1,4-1,6)-glucosidase (1 U/μL), GAP (0.17 U/μL and 0.017 U/μL), DxPsp (0.5 U/μL), and DxChe (activity unknown). Overall, the pH ranges and optima for the tested enzymes’ activities varied from acidic (pH 3) to neutral (pH 6.9) conditions according to the manufacturer’s information. To exclude the loss of acid labile sialic acids from N-glycans, we tested six digestion buffers in less acidic to neutral range: WS0049 (pH 6.6), WS0095 (pH 5), WS0122 (pH 6), disodium phosphate-citrate buffer at pH 5 and 7, and potassium phosphate buffer at pH 6.
The reaction setup was as follows: All ten glucoside hydrolases were tested in time series from 10 min up to overnight incubation. For each sampling time point, APTS-labeled maltodextrins or dextrans were formulated in 9 μL 1X digestion buffer. To each sampling time point, 1 μL of glucoside hydrolase solution was added and thoroughly mixed. The reaction mixture was incubated at 37 °C for 10 min, 30 min, 1 h, 4 h, or overnight (18 h). The reaction was stopped by the addition of 90 μL 89% ACNaq (v/v) and drying in a vacuum centrifuge. Samples were subsequently stored at −20 °C and formulated in Washing Solution I (part of the glyXprepCE™ kit) for sample purification. As a negative control, 9 μL of buffered APTS-labeled sample were treated similar without addition of glucoside hydrolase solution.
To deplete the enzymes and salts from the reaction mixture before xCGE-LIF analysis, an adapted sample purification using the glyXprepCE™ kit was performed. After application of the APTS-labeled sample, washing was performed four times with Washing Solution I before elution. The result of the enzyme reaction was monitored by xCGE-LIF on a glyXboxCE™ system.
The reaction setup was as follows: All ten glucoside hydrolases were tested in time series from 10 min up to overnight incubation. For each sampling time point, APTS-labeled maltodextrins or dextrans were formulated in 9 μL 1X digestion buffer. To each sampling time point, 1 μL of glucoside hydrolase solution was added and thoroughly mixed. The reaction mixture was incubated at 37 °C for 10 min, 30 min, 1 h, 4 h, or overnight (18 h). The reaction was stopped by the addition of 90 μL 89% ACNaq (v/v) and drying in a vacuum centrifuge. Samples were subsequently stored at −20 °C and formulated in Washing Solution I (part of the glyXprepCE™ kit) for sample purification. As a negative control, 9 μL of buffered APTS-labeled sample were treated similar without addition of glucoside hydrolase solution.
To deplete the enzymes and salts from the reaction mixture before xCGE-LIF analysis, an adapted sample purification using the glyXprepCE™ kit was performed. After application of the APTS-labeled sample, washing was performed four times with Washing Solution I before elution. The result of the enzyme reaction was monitored by xCGE-LIF on a glyXboxCE™ system.
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Acids
Adjustment Disorders
alpha Glucosidase
Amylase
APT
Citrate
Dextrans
Digestion
enzyme activity
Enzymes
Glucosidase
Glucosides
Hydrolase
maltodextrin
Oligonucleotides
Polysaccharides
potassium phosphate
Salts
Sialic Acids
sodium phosphate, dibasic
Vacuum
Possible side reactions of selected enzymes (GAP, DxChe, DxPsp and β-amylase) with N-glycans were evaluated using APTS-labeled N-glycans derived from bovine standard glycoproteins ribonuclease B, fetuin, and IgG. Specifically, activity on galactose, N-acetylglucosamine, mannose, fucose and sialic acid residues was monitored. All enzyme reactions were performed as described in Section 4.4 . using disodium phosphate-citrate buffer at pH 5 as the digestion buffer.
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Acetylglucosamine
alpha-Fetoproteins
Amylase
APT
Bos taurus
Buffers
Citrate
Digestion
Enzymes
Fucose
Galactose
Glycoproteins
Mannose
N-Acetylneuraminic Acid
Polysaccharides
ribonuclease B
sodium phosphate, dibasic
To evaluate the performance of non-enzymatic approaches for OSI depletion and the progress of enzyme reactions, glyXboxCE™ (glyXera, Magdeburg, Germany) was used, including the sample preparation kit glyXprepCE™. Briefly, bovine ribonuclease B, fetuin, and IgG as standard glycoproteins and stem cell lysates were dissolved in PBS and de-N-glycosylated by peptide-N-glycosidase F according to the kit instructions. Maltodextrins and dextrans were dissolved in ultrapure water. Maltodextrins, dextrans, and released N-glycans were labeled with APTS and purified by hydrophilic interaction chromatography (HILIC) in solid phase extraction (SPE) mode as described in the kit instructions. APTS-labeled analytes were analyzed with xCGE-LIF using glyXboxCE™. Obtained data was processed using glyXtoolCE™ (glyXera GmbH, Magdeburg, Germany) [73 ]. The software performed a migration time alignment of electropherograms to an internal standard, resulting in aligned N-glycan fingerprints. Peaks with a signal-to-noise ratio >10 were picked, and relative peak intensities were calculated based on peak height normalization. N-glycan structures were determined with the glyXtoolCE™ integrated N-glycan database and confirmed with exoglycosidase digests (see Supplementary Methods ).
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alpha-Fetoproteins
APT
Cattle
Chromatography
Dextrans
Endo-beta-N-Acetylglucosaminidase F
Enzymes
Exoglycosidases
Glycoproteins
Hydrophilic Interactions
maltodextrin
Polysaccharides
ribonuclease B
Solid Phase Extraction
Stem Cells
APTS-labeled N-glycans from standard glycoproteins (see Section 4.5 ) spiked with APTS-labeled maltodextrins or dextrans, and several stem-cell-derived N-glycan samples containing OSIs, were treated with GAP or DxChe as described in Section 4.4 . using disodium phosphate-citrate buffer at pH 5 for 30 min.
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APT
Buffers
Citrates
Dextrans
Glycoproteins
maltodextrin
Polysaccharides
sodium phosphate, dibasic
Stem Cells
Top products related to «APT»
Sourced in United States
The GlycanAssure APTS Kit is a product designed for the fluorescent labeling of glycans. It utilizes the APTS (8-Aminopyrene-1,3,6-trisulfonic acid) reagent to label glycans, enabling their detection and analysis.
Sourced in United States, Germany, United Kingdom, Spain, France, Australia, Italy, Poland, Malaysia, Ireland, Japan, India
3-aminopropyltriethoxysilane is a bifunctional organosilane compound. It contains both an amino group and three ethoxy groups. This molecule can be used as a coupling agent in various applications, facilitating the bonding between inorganic and organic materials.
Sourced in United States, Japan, United Kingdom
The 3500xL Genetic Analyzer is a capillary electrophoresis instrument designed for DNA sequencing and genetic analysis. It features 8 capillaries and can process multiple samples simultaneously. The system utilizes laser-induced fluorescence detection for accurate and sensitive DNA fragment analysis.
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Hydrochloric acid is a commonly used laboratory reagent. It is a clear, colorless, and highly corrosive liquid with a pungent odor. Hydrochloric acid is an aqueous solution of hydrogen chloride gas.
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Ethanol is a clear, colorless liquid chemical compound commonly used in laboratory settings. It is a key component in various scientific applications, serving as a solvent, disinfectant, and fuel source. Ethanol has a molecular formula of C2H6O and a range of industrial and research uses.
Sourced in United States, Germany, Japan, China, India, United Kingdom, Switzerland
The ABI 3500 Genetic Analyzer is a capillary electrophoresis instrument designed for DNA sequencing and fragment analysis applications. It utilizes laser-induced fluorescence detection and a 24-capillary array to provide high-throughput analysis of genetic samples.
Sourced in United States, Canada, United Kingdom
Peptide-N-glycosidase F (PNGase F) is an enzyme that cleaves the linkage between the asparagine residue and the first N-acetylglucosamine of high-mannose, hybrid, and complex oligosaccharides from glycoproteins.
GlycanAssure Data Analysis Software Version 2.0 is a software application developed by Thermo Fisher Scientific for the analysis of glycan data. The software provides tools for processing, visualizing, and interpreting glycan data obtained from various analytical techniques.
Sourced in Germany
Arthrobacter ureafaciens sialidase is an enzyme derived from the bacterium Arthrobacter ureafaciens. It is used in laboratory settings for the cleavage of sialic acid residues from glycoconjugates.
Sourced in United States, Japan, Germany, Canada, United Kingdom, Italy
The 3500 Genetic Analyzer is a capillary electrophoresis instrument designed for DNA sequencing and fragment analysis. It utilizes laser-induced fluorescence detection to analyze DNA samples. The instrument is capable of generating high-quality genetic data for a variety of applications.
More about "APT"
Advanced Persistent Threats (APTs) are a sophisticated and stealthy form of cyber attack that target specific organizations or individuals.
These attacks are typically carried out by well-resourced and highly skilled adversaries, such as nation-states or advanced hacker groups.
APTs often involve a prolonged and methodical approach, including infiltration, lateral movement within a network, and the extraction of sensitive data over an extended period.
The characteristics of APTs include the use of a wide range of techniques, such as social engineering, malware, and exploits, to remain undetected and maintain persistent access.
Understanding the mitigation strategies for APTs is crucial for enhancing cybersecurity and protecting against these advanced, targeted threats.
The GlycanAssure APTS Kit, for example, provides a comprehensive solution for the analysis of N-glycans, which can be an important aspect of APT detection and response.
The kit utilizes tools like 3-aminopropyltriethoxysilane, the 3500xL Genetic Analyzer, and Peptide-N-glycosidase F (PNGase F) to facilitate the preparation, separation, and analysis of glycans.
The GlycanAssure Data Analysis Software Version 2.0 further enables researchers to interpret the data and gain insights into the glycosylation patterns that may be associated with APT activities.
Additionally, the ABI 3500 Genetic Analyzer and the 3500 Genetic Analyzer are widely used in the field of molecular biology and genetics, which can be relevant to the investigation and mitigation of APTs.
These instruments, combined with the use of Hydrochloric acid, Ethanol, and Arthrobacter ureafaciens sialidase, provide a powerful set of tools for researchers and cybersecurity professionals to analyze and understand the complex biological and technological aspects of APTs.
These attacks are typically carried out by well-resourced and highly skilled adversaries, such as nation-states or advanced hacker groups.
APTs often involve a prolonged and methodical approach, including infiltration, lateral movement within a network, and the extraction of sensitive data over an extended period.
The characteristics of APTs include the use of a wide range of techniques, such as social engineering, malware, and exploits, to remain undetected and maintain persistent access.
Understanding the mitigation strategies for APTs is crucial for enhancing cybersecurity and protecting against these advanced, targeted threats.
The GlycanAssure APTS Kit, for example, provides a comprehensive solution for the analysis of N-glycans, which can be an important aspect of APT detection and response.
The kit utilizes tools like 3-aminopropyltriethoxysilane, the 3500xL Genetic Analyzer, and Peptide-N-glycosidase F (PNGase F) to facilitate the preparation, separation, and analysis of glycans.
The GlycanAssure Data Analysis Software Version 2.0 further enables researchers to interpret the data and gain insights into the glycosylation patterns that may be associated with APT activities.
Additionally, the ABI 3500 Genetic Analyzer and the 3500 Genetic Analyzer are widely used in the field of molecular biology and genetics, which can be relevant to the investigation and mitigation of APTs.
These instruments, combined with the use of Hydrochloric acid, Ethanol, and Arthrobacter ureafaciens sialidase, provide a powerful set of tools for researchers and cybersecurity professionals to analyze and understand the complex biological and technological aspects of APTs.