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Article ; Online: A MALDI-TOF MS method for the simultaneous and quantitative analysis of neutral and sialylated glycans of CHO-expressed glycoproteins.

Tep, Samnang / Hincapie, Marina / Hancock, William S

2012 Volume 347, Issue 1, Page(s) 121–129

Abstract: The development of a MALDI-TOF MS method for the quantitative analysis of the glycosylation of CHO-expressed biotherapeutic glycoproteins shall be presented. The method utilizes a well-established chemistry, reductive amination of glycans, to derivatize ... ...

Abstract	The development of a MALDI-TOF MS method for the quantitative analysis of the glycosylation of CHO-expressed biotherapeutic glycoproteins shall be presented. The method utilizes a well-established chemistry, reductive amination of glycans, to derivatize glycans with either a light analog ((12)C(7) anthranilic acid) or a heavy analog ((13)C(7) anthranilic acid) to allow for the direct comparison of the alternately-labeled glycans by MALDI-TOF MS. The method allows for the simultaneous analysis of neutral and sialylated glycans and displays a linear dynamic range over two orders of magnitude with sub-picomolar sensitivity. Additionally, because the glycans are derivatized with anthranilic acid, which is a very sensitive fluorophore, the glycans can be analyzed by chromatography with fluorescence detection. The need for this type of method is highlighted by the biotechnology/biopharmaceutical industry's continuous drive towards fully understanding process control. By providing this type of quantitative data, glycosylation changes of the expressed protein can be easily observed thereby helping to further advance the understanding of a major aspect of the biopharmaceutical process.
MeSH term(s)	Animals ; Bioreactors ; CHO Cells ; Cricetinae ; Cricetulus ; Gene Expression ; Glycoproteins/chemistry ; Glycoproteins/genetics ; N-Acetylneuraminic Acid/chemistry ; Polysaccharides/chemistry ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods ; Time Factors
Chemical Substances	Glycoproteins ; Polysaccharides ; N-Acetylneuraminic Acid (GZP2782OP0)
Language	English
Publishing date	2012-01-10
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1435-7
ISSN	1873-426X ; 0008-6215
ISSN (online)	1873-426X
ISSN	0008-6215
DOI	10.1016/j.carres.2011.10.005
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Article ; Online: The characterization and quantitation of glycomic changes in CHO cells during a bioreactor campaign.

Tep, Samnang / Hincapie, Marina / Hancock, William S

Biotechnology and bioengineering

2012 Volume 109, Issue 12, Page(s) 3007–3017

Abstract: Within the biotechnology industry there is a continuous drive to better and more fully understand the biopharmaceutical process in order to achieve better process control. A method to monitor and quantitate glycomic changes that occur in CHO cells during ...

Abstract	Within the biotechnology industry there is a continuous drive to better and more fully understand the biopharmaceutical process in order to achieve better process control. A method to monitor and quantitate glycomic changes that occur in CHO cells during a bioreactor campaign could help to address this. The goal of the method presented here is to provide data that may help to understand the changes in glycosylation that are occurring, within the cell, to proteins other than the expressed biotherapeutic. The method involves the lysing of cells to gain access to intracellular proteins. The expressed biotherapeutic is specifically removed by affinity chromatography, while the remaining proteins are subjected to deglycosylation by treatment with PNGase F. The released glycans are derivatized with isotopic tags, and quantitative analysis by MALDI-TOF MS is performed. The MALDI-TOF MS method allows for the simultaneous analysis of both neutral and sialylated glycans, displays a linear dynamic range over two orders of magnitude for both neutral and sialylated glycans and achieves sub-picomolar sensitivity. This method may yield valuable information that gives further insight into the inner-workings of CHO cells, potentially taking another step towards fully understanding and controlling the biopharmaceutical process.
MeSH term(s)	Animals ; Bioreactors ; CHO Cells ; Cricetinae ; Cricetulus ; Electrophoresis, Polyacrylamide Gel ; Glycomics/methods ; Glycoproteins/analysis ; Glycoproteins/metabolism ; Glycosylation ; Isotope Labeling ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase/analysis ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase/metabolism ; Polysaccharides/analysis ; Polysaccharides/metabolism ; Reproducibility of Results ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Staphylococcal Protein A/analysis ; Staphylococcal Protein A/metabolism ; ortho-Aminobenzoates/chemistry ; ortho-Aminobenzoates/metabolism
Chemical Substances	Glycoproteins ; Polysaccharides ; Staphylococcal Protein A ; ortho-Aminobenzoates ; anthranilic acid (0YS975XI6W) ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase (EC 3.5.1.52)
Language	English
Publishing date	2012-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	280318-5
ISSN	1097-0290 ; 0006-3592
ISSN (online)	1097-0290
ISSN	0006-3592
DOI	10.1002/bit.24590
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Article ; Online: A general approach for the purification and quantitative glycomic analysis of human plasma.

Tep, Samnang / Hincapie, Marina / Hancock, William S

Analytical and bioanalytical chemistry

2012 Volume 402, Issue 9, Page(s) 2687–2700

Abstract: The development of a general method for the purification and quantitative glycomic analysis of human plasma samples to characterize global glycosylation changes shall be presented. The method involves multiple steps, including the depletion of plasma via ...

Abstract	The development of a general method for the purification and quantitative glycomic analysis of human plasma samples to characterize global glycosylation changes shall be presented. The method involves multiple steps, including the depletion of plasma via multi-affinity chromatography to remove high abundant proteins, the enrichment of the lower abundant glycoproteins via multi-lectin affinity chromatography, the isotopic derivatization of released glycans, and quantitative analysis by MALDI-TOF MS. Isotopic derivatization of glycans is accomplished using the well-established chemistry of reductive amination to derivatize glycans with either a light analog ((12)C anthranilic acid) or a heavy analog ((13)C(7) anthranilic acid), which allows for the direct comparison of the alternately labeled glycans by MALDI-TOF MS. The method displays a tenfold linear dynamic range for both neutral and sialylated glycans with sub-picomolar sensitivity. Additionally, by using anthranilic acid, a very sensitive fluorophore, as the derivatization reagent, the glycans can be analyzed by chromatography with fluorescence detection. The utility of this methodology is highlighted by the many diseases and disorders that are known to either show or be the result of changes in glycosylation. A method that provides a generic approach for sample preparation and quantitative data will help to further advance the field of glycomics.
MeSH term(s)	Blood Proteins/analysis ; Blood Proteins/isolation & purification ; Blood Proteins/metabolism ; Chromatography/methods ; Glycomics/methods ; Glycoproteins/blood ; Glycoproteins/isolation & purification ; Glycoproteins/metabolism ; Glycosylation ; Humans ; Mass Spectrometry/methods ; Polysaccharides/analysis ; Polysaccharides/metabolism
Chemical Substances	Blood Proteins ; Glycoproteins ; Polysaccharides
Language	English
Publishing date	2012-03
Publishing country	Germany
Document type	Evaluation Studies ; Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	201093-8
ISSN	1618-2650 ; 0016-1152 ; 0372-7920
ISSN (online)	1618-2650
ISSN	0016-1152 ; 0372-7920
DOI	10.1007/s00216-012-5712-5
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Article: Modeling the Kinetics of Lipid-Nanoparticle- Mediated Delivery of Multiple siRNAs to Evaluate the Effect on Competition for Ago2.

Mihaila, Radu / Ruhela, Dipali / Galinski, Beverly / Card, Ananda / Cancilla, Mark / Shadel, Timothy / Kang, Jing / Tep, Samnang / Wei, Jie / Haas, R Matthew / Caldwell, Jeremy / Flanagan, W Michael / Kuklin, Nelly / Cherkaev, Elena / Ason, Brandon

Molecular therapy. Nucleic acids

2019 Volume 16, Page(s) 367–377

Abstract: Drug combinations can improve the control of diseases involving redundant and highly regulated pathways. Validating a multi-target therapy early in drug development remains difficult. Small interfering RNAs (siRNAs) are routinely used to selectively ... ...

Abstract	Drug combinations can improve the control of diseases involving redundant and highly regulated pathways. Validating a multi-target therapy early in drug development remains difficult. Small interfering RNAs (siRNAs) are routinely used to selectively silence a target of interest. Owing to the ease of design and synthesis, siRNAs hold promise for combination therapies. Combining siRNAs against multiple targets remains an attractive approach to interrogating highly regulated pathways. Currently, questions remain regarding how broadly such an approach can be applied, since siRNAs have been shown to compete with one another for binding to Argonaute2 (Ago2), the protein responsible for initiating siRNA-mediated mRNA degradation. Mathematical modeling, coupled with in vitro and in vivo experiments, led us to conclude that endosomal escape kinetics had the highest impact on Ago2 depletion by competing lipid-nanoparticle (LNP)-formulated siRNAs. This, in turn, affected the level of competition observed between them. A future application of this model would be to optimize delivery of desired siRNA combinations in vitro to attenuate competition and maximize the combined therapeutic effect.
Language	English
Publishing date	2019-03-23
Publishing country	United States
Document type	Journal Article
ZDB-ID	2662631-7
ISSN	2162-2531
ISSN	2162-2531
DOI	10.1016/j.omtn.2019.03.004
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Article ; Online: Small-molecule inhibition of glycogen synthase 1 for the treatment of Pompe disease and other glycogen storage disorders.

Ullman, Julie C / Mellem, Kevin T / Xi, Yannan / Ramanan, Vyas / Merritt, Hanne / Choy, Rebeca / Gujral, Tarunmeet / Young, Lyndsay E A / Blake, Kerrigan / Tep, Samnang / Homburger, Julian R / O'Regan, Adam / Ganesh, Sandya / Wong, Perryn / Satterfield, Terrence F / Lin, Baiwei / Situ, Eva / Yu, Cecile / Espanol, Bryan /

Sarwaikar, Richa / Fastman, Nathan / Tzitzilonis, Christos / Lee, Patrick / Reiton, Daniel / Morton, Vivian / Santiago, Pam / Won, Walter / Powers, Hannah / Cummings, Beryl B / Hoek, Maarten / Graham, Robert R / Chandriani, Sanjay J / Bainer, Russell / DePaoli-Roach, Anna A / Roach, Peter J / Hurley, Thomas D / Sun, Ramon C / Gentry, Matthew S / Sinz, Christopher / Dick, Ryan A / Noonberg, Sarah B / Beattie, David T / Morgans, David J / Green, Eric M

Science translational medicine

2024 Volume 16, Issue 730, Page(s) eadf1691

Abstract: Glycogen synthase 1 (GYS1), the rate-limiting enzyme in muscle glycogen synthesis, plays a central role in energy homeostasis and has been proposed as a therapeutic target in multiple glycogen storage diseases. Despite decades of investigation, there are ...

Abstract	Glycogen synthase 1 (GYS1), the rate-limiting enzyme in muscle glycogen synthesis, plays a central role in energy homeostasis and has been proposed as a therapeutic target in multiple glycogen storage diseases. Despite decades of investigation, there are no known potent, selective small-molecule inhibitors of this enzyme. Here, we report the preclinical characterization of MZ-101, a small molecule that potently inhibits GYS1 in vitro and in vivo without inhibiting GYS2, a related isoform essential for synthesizing liver glycogen. Chronic treatment with MZ-101 depleted muscle glycogen and was well tolerated in mice. Pompe disease, a glycogen storage disease caused by mutations in acid α glucosidase (GAA), results in pathological accumulation of glycogen and consequent autophagolysosomal abnormalities, metabolic dysregulation, and muscle atrophy. Enzyme replacement therapy (ERT) with recombinant GAA is the only approved treatment for Pompe disease, but it requires frequent infusions, and efficacy is limited by suboptimal skeletal muscle distribution. In a mouse model of Pompe disease, chronic oral administration of MZ-101 alone reduced glycogen buildup in skeletal muscle with comparable efficacy to ERT. In addition, treatment with MZ-101 in combination with ERT had an additive effect and could normalize muscle glycogen concentrations. Biochemical, metabolomic, and transcriptomic analyses of muscle tissue demonstrated that lowering of glycogen concentrations with MZ-101, alone or in combination with ERT, corrected the cellular pathology in this mouse model. These data suggest that substrate reduction therapy with GYS1 inhibition may be a promising therapeutic approach for Pompe disease and other glycogen storage diseases.
MeSH term(s)	Mice ; Animals ; Glycogen Storage Disease Type II/drug therapy ; Glycogen Synthase/metabolism ; Glycogen Synthase/pharmacology ; Mice, Knockout ; Glycogen/metabolism ; Muscle, Skeletal/metabolism ; Enzyme Replacement Therapy/methods
Chemical Substances	Glycogen Synthase (EC 2.4.1.11) ; Glycogen (9005-79-2)
Language	English
Publishing date	2024-01-17
Publishing country	United States
Document type	Journal Article
ZDB-ID	2518854-9
ISSN	1946-6242 ; 1946-6234
ISSN (online)	1946-6242
ISSN	1946-6234
DOI	10.1126/scitranslmed.adf1691
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Article: A comparison of three techniques for quantitative carbohydrate analysis used in characterization of therapeutic antibodies.

Siemiatkoski, Joseph / Lyubarskaya, Yelena / Houde, Damian / Tep, Samnang / Mhatre, Rohin

Carbohydrate research

2006 Volume 341, Issue 3, Page(s) 410–419

Abstract: A comparison of three techniques for quantitative analysis of galactosylation present on immunoglobulins is described. ESIMS, MALDI-TOF MS, and anion-exchange chromatography with fluorescence detection were evaluated in terms of repeatability, limit of ... ...

Abstract	A comparison of three techniques for quantitative analysis of galactosylation present on immunoglobulins is described. ESIMS, MALDI-TOF MS, and anion-exchange chromatography with fluorescence detection were evaluated in terms of repeatability, limit of quantitation, selectivity, and linearity. A recombinant monoclonal IgG was enzymatically modified in vitro to produce essentially completely galactosylated and degalactosylated forms of the immunoglobulin. Samples of known galactosylation levels were prepared by mixing the modified forms with the native form of the immunoglobulin. Good repeatability and linearity were demonstrated for all three assays (RSDs<1.0%, correlation coefficients>0.99). Differences in selectivity, sensitivity, and other performance aspects of the three techniques are also discussed in this paper.
MeSH term(s)	Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/metabolism ; Carbohydrate Sequence ; Carbohydrates/analysis ; Chromatography, High Pressure Liquid/methods ; Chromatography, Ion Exchange/methods ; Fluorescence ; Glycosylation ; Immunoglobulins/analysis ; Molecular Sequence Data ; N-Acetyllactosamine Synthase/metabolism ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase/metabolism ; Protein Processing, Post-Translational ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Spectrometry, Mass, Electrospray Ionization ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods ; Streptococcus pneumoniae/enzymology
Chemical Substances	Antibodies, Monoclonal ; Carbohydrates ; Immunoglobulins ; Recombinant Proteins ; N-Acetyllactosamine Synthase (EC 2.4.1.90) ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase (EC 3.5.1.52)
Language	English
Publishing date	2006-02-27
Publishing country	Netherlands
Document type	Comparative Study ; Journal Article
ZDB-ID	1435-7
ISSN	1873-426X ; 0008-6215
ISSN (online)	1873-426X
ISSN	0008-6215
DOI	10.1016/j.carres.2005.11.024
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Article ; Online: Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles--part 1: separation-based methods.

Reusch, Dietmar / Haberger, Markus / Maier, Bernd / Maier, Maria / Kloseck, Ronny / Zimmermann, Boris / Hook, Michaela / Szabo, Zoltan / Tep, Samnang / Wegstein, Jo / Alt, Nadja / Bulau, Patrick / Wuhrer, Manfred

mAbs

2015 Volume 7, Issue 1, Page(s) 167–179

Abstract: Immunoglobulin G (IgG) crystallizable fragment (Fc) glycosylation is crucial for antibody effector functions, such as antibody-dependent cell-mediated cytotoxicity, and for their pharmacokinetic and pharmacodynamics behavior. To monitor the Fc- ... ...

Abstract	Immunoglobulin G (IgG) crystallizable fragment (Fc) glycosylation is crucial for antibody effector functions, such as antibody-dependent cell-mediated cytotoxicity, and for their pharmacokinetic and pharmacodynamics behavior. To monitor the Fc-glycosylation in bioprocess development, as well as product characterization and release analytics, reliable techniques for glycosylation analysis are needed. A wide range of analytical methods has found its way into these applications. In this study, a comprehensive comparison was performed of separation-based methods for Fc-glycosylation profiling of an IgG biopharmaceutical. A therapeutic antibody reference material was analyzed 6-fold on 2 different days, and the methods were compared for precision, accuracy, throughput and other features; special emphasis was placed on the detection of sialic acid-containing glycans. Seven, non-mass spectrometric methods were compared; the methods utilized liquid chromatography-based separation of fluorescent-labeled glycans, capillary electrophoresis-based separation of fluorescent-labeled glycans, or high-performance anion exchange chromatography with pulsed amperometric detection. Hydrophilic interaction liquid chromatography-ultra high performance liquid chromatography of 2-aminobenzamide (2-AB)-labeled glycans was used as a reference method. All of the methods showed excellent precision and accuracy; some differences were observed, particularly with regard to the detection and quantitation of minor glycan species, such as sialylated glycans.
MeSH term(s)	Animals ; Antibodies, Monoclonal/chemistry ; CHO Cells ; Chromatography, High Pressure Liquid ; Cricetinae ; Cricetulus ; Glycosylation ; Immunoglobulin Fc Fragments/chemistry ; Mass Spectrometry
Chemical Substances	Antibodies, Monoclonal ; Immunoglobulin Fc Fragments
Language	English
Publishing date	2015
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1942-0870
ISSN (online)	1942-0870
DOI	10.4161/19420862.2014.986000
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Article: Imidazopyridine-Based Fatty Acid Synthase Inhibitors That Show Anti-HCV Activity and in Vivo Target Modulation.

Oslob, Johan D / Johnson, Russell J / Cai, Haiying / Feng, Shirley Q / Hu, Lily / Kosaka, Yuko / Lai, Julie / Sivaraja, Mohanram / Tep, Samnang / Yang, Hanbiao / Zaharia, Cristiana A / Evanchik, Marc J / McDowell, Robert S

ACS medicinal chemistry letters

2012 Volume 4, Issue 1, Page(s) 113–117

Abstract: Potent imidazopyridine-based inhibitors of fatty acid synthase (FASN) are described. The compounds are shown to have antiviral (HCV replicon) activities that track with their biochemical activities. The most potent analogue (compound 19) also inhibits ... ...

Abstract	Potent imidazopyridine-based inhibitors of fatty acid synthase (FASN) are described. The compounds are shown to have antiviral (HCV replicon) activities that track with their biochemical activities. The most potent analogue (compound 19) also inhibits rat FASN and inhibits de novo palmitate synthesis in vitro (cell-based) as well as in vivo.
Language	English
Publishing date	2012-12-02
Publishing country	United States
Document type	Journal Article
ISSN	1948-5875
ISSN	1948-5875
DOI	10.1021/ml300335r
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Article ; Online: Rescue of Mtp siRNA-induced hepatic steatosis by DGAT2 siRNA silencing.

Tep, Samnang / Mihaila, Radu / Freeman, Alexander / Pickering, Victoria / Huynh, Felicia / Tadin-Strapps, Marija / Stracks, Allison / Hubbard, Brian / Caldwell, Jeremy / Flanagan, W Michael / Kuklin, Nelly A / Ason, Brandon

Journal of lipid research

2012 Volume 53, Issue 5, Page(s) 859–867

Abstract: Microsomal triglyceride transfer protein (Mtp) inhibitors represent a novel therapeutic approach to lower circulating LDL cholesterol, although therapeutic development has been hindered by the observed increase in hepatic triglycerides and liver ... ...

Abstract	Microsomal triglyceride transfer protein (Mtp) inhibitors represent a novel therapeutic approach to lower circulating LDL cholesterol, although therapeutic development has been hindered by the observed increase in hepatic triglycerides and liver steatosis following treatment. Here, we used small interfering RNAs (siRNA) targeting Mtp to achieve target-specific silencing to study this phenomenon and to determine to what extent liver steatosis is induced by changes in Mtp expression. We observed that Mtp silencing led to a decrease in many genes involved in hepatic triglyceride synthesis. Given the role of diacylglycerol O-acyltransferase 2 (Dgat2) in regulating hepatic triglyceride synthesis, we then evaluated whether target-specific silencing of both Dgat2 and Mtp were sufficient to attenuate Mtp silencing-induced liver steatosis. We showed that the simultaneous inhibition of Dgat2 and Mtp led to a decrease in plasma cholesterol and a reduction in the accumulation of hepatic triglycerides caused by the inhibition of Mtp. Collectively, these findings provide a proof-of-principle for a triglyceride synthesis/Mtp inhibitor combination and represent a potentially novel approach for therapeutic development in which targeting multiple pathways can achieve the desired response.
MeSH term(s)	Animals ; Apolipoproteins B/deficiency ; Apolipoproteins B/genetics ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cholesterol/blood ; Diacylglycerol O-Acyltransferase/deficiency ; Diacylglycerol O-Acyltransferase/genetics ; Fatty Liver/blood ; Fatty Liver/enzymology ; Fatty Liver/genetics ; Fatty Liver/metabolism ; Gene Silencing ; Liver/metabolism ; Male ; Mice ; RNA, Small Interfering/genetics ; Triglycerides/metabolism
Chemical Substances	Apolipoproteins B ; Carrier Proteins ; RNA, Small Interfering ; Triglycerides ; microsomal triglyceride transfer protein ; Cholesterol (97C5T2UQ7J) ; DGAT2 protein, mouse (EC 2.3.1.20) ; Diacylglycerol O-Acyltransferase (EC 2.3.1.20)
Language	English
Publishing date	2012-02-21
Publishing country	United States
Document type	Journal Article
ZDB-ID	80154-9
ISSN	1539-7262 ; 0022-2275
ISSN (online)	1539-7262
ISSN	0022-2275
DOI	10.1194/jlr.M021063
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Article ; Online: Multi-site N-Glycan mapping study 2: UHPLC.

Szekrényes, Ákos / Park, SungAe Suhr / Cosgrave, Eoin / Jones, Aled / Haxo, Ted / Kimzey, Michael / Pourkaveh, Shiva / Szabó, Zoltán / Sosic, Zoran / Feng, Peng / Sejwal, Preeti / Dent, Kelsey / Michels, David / Freckleton, Gordon / Qian, Jun / Lancaster, Catherine / Duffy, Toni / Schwartz, Melissa / Luo, Jiann-Kae /

van Dyck, Jonathan / Leung, Pui-King / Olajos, Marcell / Kowle, Ronald / Gao, Kai / Wang, Wenbo / Wegstein, Jo / Tep, Samnang / Domokos, Apolka / Váradi, Csaba / Guttman, András

Electrophoresis

2018 Volume 39, Issue 7, Page(s) 998–1005

Abstract: In the first part of this publication, the results from an international study evaluating the precision (i.e., repeatability and reproducibility) of N-glycosylation analysis using capillary electrophoresis of APTS-labeled N-glycans were presented. The ... ...

Abstract	In the first part of this publication, the results from an international study evaluating the precision (i.e., repeatability and reproducibility) of N-glycosylation analysis using capillary electrophoresis of APTS-labeled N-glycans were presented. The corresponding results from ultra-high performance liquid chromatography (UHPLC) with fluorescence detection are presented here from 12 participating sites. All participants used the same lot of samples, reagents, and columns to perform the assays. Elution time, peak area and peak area percent values were determined for all peaks ≥0.1% peak area, and statistical analysis was performed following ISO 5725-2 guideline principles. The results demonstrated adequate reproducibility, within any given site as well across all sites, indicating that standard UHPLC-based N-glycan analysis platforms are appropriate for general use.
MeSH term(s)	Benzamides/chemistry ; Binding Sites ; Chromatography, High Pressure Liquid/methods ; Electrophoresis, Capillary/methods ; Fluorescent Dyes/chemistry ; Glycosylation ; Humans ; Limit of Detection ; Polysaccharides/analysis ; Reproducibility of Results ; Spectrometry, Fluorescence/methods
Chemical Substances	Benzamides ; Fluorescent Dyes ; Polysaccharides
Language	English
Publishing date	2018-02-06
Publishing country	Germany
Document type	Journal Article
ZDB-ID	619001-7
ISSN	1522-2683 ; 0173-0835
ISSN (online)	1522-2683
ISSN	0173-0835
DOI	10.1002/elps.201700463
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