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Article: SLAPSHOT reveals rapid dynamics of extracellularly exposed proteome in response to calcium-activated plasma membrane phospholipid scrambling.

Tuomivaara, Sami T / Teo, Chin Fen / Jan, Yuh Nung / Jan, Lily Y / Wiita, Arun P

bioRxiv : the preprint server for biology

2023

Abstract: To facilitate our understanding of the often rapid and nuanced dynamics of extracellularly exposed proteomes during signaling events, it is important to devise robust workflows affording fast time resolution without biases and confounding factors. Here, ... ...

Abstract	To facilitate our understanding of the often rapid and nuanced dynamics of extracellularly exposed proteomes during signaling events, it is important to devise robust workflows affording fast time resolution without biases and confounding factors. Here, we present
Language	English
Publishing date	2023-03-26
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.03.26.534250
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Article ; Online: PDADMAC/Alginate-Coated Gold Nanorod For Eradication of Staphylococcus Aureus Biofilms.

Manimaran, Malarmugila / Teo, Yin Yin / Kah, James Chen Yong / Beishenaliev, Adilet / Loke, Yean Leng / Foo, Yiing Yee / Ng, Shiow-Fern / Chee, Chin Fei / Chin, Sek Peng / Faruqu, Farid Nazer / Chang, Chia-Yu / Misran, Misni / Chung, Lip Yong / Leo, Bey Fen / Chiou, Shih-Hwa / Chang, Chia-Ching / Tay, Sun Tee / Kiew, Lik Voon

International journal of nanomedicine

2024 Volume 19, Page(s) 3697–3714

Abstract: Introduction: Over 75% of clinical microbiological infections are caused by bacterial biofilms that grow on wounds or implantable medical devices. This work describes the development of a new poly(diallyldimethylammonium chloride) (PDADMAC)/alginate- ... ...

Abstract	Introduction: Over 75% of clinical microbiological infections are caused by bacterial biofilms that grow on wounds or implantable medical devices. This work describes the development of a new poly(diallyldimethylammonium chloride) (PDADMAC)/alginate-coated gold nanorod (GNR/Alg/PDADMAC) that effectively disintegrates the biofilms of Methods: GNR was synthesised via seed-mediated growth method, and the resulting nanoparticles were coated first with Alg and then PDADMAC. FTIR, zeta potential, transmission electron microscopy, and UV-Vis spectrophotometry analysis were performed to characterise the nanoparticles. The efficacy and speed of the non-coated GNR and GNR/Alg/PDADMAC in disintegrating Results: The synthesised GNR/Alg/PDADMAC (mean length: 55.71 ± 1.15 nm, mean width: 23.70 ± 1.13 nm, aspect ratio: 2.35) was biocompatible and potent in eradicating preformed biofilms of methicillin-resistant (MRSA) and methicillin-susceptible Conclusion: These findings support the potential application of GNR/Alg/PDADMAC as an alternative agent to conventional antiseptics and antibiotics for the eradication of medically important MRSA and MSSA biofilms.
MeSH term(s)	Biofilms/drug effects ; Gold/chemistry ; Gold/pharmacology ; Quaternary Ammonium Compounds/chemistry ; Quaternary Ammonium Compounds/pharmacology ; Alginates/chemistry ; Alginates/pharmacology ; Nanotubes/chemistry ; Animals ; Mice ; Staphylococcus aureus/drug effects ; Staphylococcus aureus/physiology ; Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/chemistry ; Polyethylenes/chemistry ; Polyethylenes/pharmacology ; Staphylococcal Infections/drug therapy ; Methicillin-Resistant Staphylococcus aureus/drug effects ; Methicillin-Resistant Staphylococcus aureus/physiology ; Cell Line ; Microbial Sensitivity Tests ; Metal Nanoparticles/chemistry
Chemical Substances	Gold (7440-57-5) ; Quaternary Ammonium Compounds ; Alginates ; Anti-Bacterial Agents ; poly-N,N-dimethyl-N,N-diallylammonium chloride (26062-79-3) ; Polyethylenes
Language	English
Publishing date	2024-04-23
Publishing country	New Zealand
Document type	Journal Article
ZDB-ID	2364941-0
ISSN	1178-2013 ; 1176-9114
ISSN (online)	1178-2013
ISSN	1176-9114
DOI	10.2147/IJN.S452085
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Article ; Online: Metabolic labeling of glycans with isotopic glucose for quantitative glycomics in yeast.

Kim, Ji-Yeon / Joo, Woo Hong / Shin, Dong-Soo / Lee, Yong-Ill / Teo, Chin Fen / Lim, Jae-Min

Analytical biochemistry

2021 Volume 621, Page(s) 114152

Abstract: Changes in glycan levels could directly affect the biochemical properties of glycoproteins and thus influence their physiological functions. In order to decode the correlation of glycan prevalence with their physiological contribution, many mass ... ...

Abstract	Changes in glycan levels could directly affect the biochemical properties of glycoproteins and thus influence their physiological functions. In order to decode the correlation of glycan prevalence with their physiological contribution, many mass spectrometry (MS) and stable isotope labeling-based methods have been developed for the relative quantification of glycans. In this study, we expand the quantitative glycomic toolbox with the addition of optimized Metabolic Isotope Labeling of Polysaccharides with Isotopic Glucose (MILPIG) approach in baker's yeast (Saccharomyces cerevisiae). We demonstrate that culturing baker's yeast in the presence of carbon-13 labeled glucose (1-
MeSH term(s)	Calibration ; Carbon Isotopes/metabolism ; Cell Culture Techniques/methods ; Glucose/chemistry ; Glycoconjugates/analysis ; Glycoconjugates/biosynthesis ; Glycoconjugates/chemistry ; Glycomics/methods ; Glycosylation ; Isotope Labeling/methods ; Mass Spectrometry ; Polysaccharides/analysis ; Polysaccharides/biosynthesis ; Polysaccharides/chemistry ; Reproducibility of Results ; Saccharomyces cerevisiae/chemistry ; Saccharomyces cerevisiae/metabolism
Chemical Substances	Carbon Isotopes ; Glycoconjugates ; Polysaccharides ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2021-03-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1016/j.ab.2021.114152
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Article ; Online: Monitoring protein O-linked β-N-acetylglucosamine status via metabolic labeling and copper-free click chemistry.

Teo, Chin Fen / Wells, Lance

Analytical biochemistry

2014 Volume 464, Page(s) 70–72

Abstract: O-Linked β-N-acetylglucosamine (O-GlcNAc) modification found on the serine and threonine residues of intracellular proteins is an inducible post-translational modification that regulates numerous biological processes. In combination with other cell ... ...

Abstract	O-Linked β-N-acetylglucosamine (O-GlcNAc) modification found on the serine and threonine residues of intracellular proteins is an inducible post-translational modification that regulates numerous biological processes. In combination with other cell biological and biochemical approaches, a robust and streamlined strategy for detecting the number and stoichiometry of O-GlcNAc modification can provide valuable insights for decoding the functions of O-GlcNAc at the molecular level. Here, we report an optimized workflow for evaluating the O-GlcNAc status of proteins using a combination of metabolic labeling and click chemistry-based mass tagging. This method is strategically complementary to the chemoenzymatic-based mass-tagging method.
MeSH term(s)	Acetylglucosamine/metabolism ; Click Chemistry ; Copper/chemistry
Chemical Substances	Copper (789U1901C5) ; Acetylglucosamine (V956696549)
Language	English
Publishing date	2014-07-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1016/j.ab.2014.06.010
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Article: Metabolic labeling of glycans with isotopic glucose for quantitative glycomics in yeast

Kim, Ji-Yeon / Joo, Woo Hong / Shin, Dong-Soo / Lee, Yong-Ill / Teo, Chin Fen / Lim, Jae-Min

Analytical biochemistry. 2021 May 15, v. 621

2021

Abstract	Changes in glycan levels could directly affect the biochemical properties of glycoproteins and thus influence their physiological functions. In order to decode the correlation of glycan prevalence with their physiological contribution, many mass spectrometry (MS) and stable isotope labeling-based methods have been developed for the relative quantification of glycans. In this study, we expand the quantitative glycomic toolbox with the addition of optimized Metabolic Isotope Labeling of Polysaccharides with Isotopic Glucose (MILPIG) approach in baker's yeast (Saccharomyces cerevisiae). We demonstrate that culturing baker's yeast in the presence of carbon-13 labeled glucose (1–¹³C₁) leads to effective incorporation of carbon-13 to both N-linked and O-linked glycans. We established that metabolic incorporation of isotope-labeled glucose at a concentration of 5 mg/mL for three days is required for an accurate quantitative analysis with optimal isotopic cluster distribution of glycans. To validate the robustness of the method, we performed the analysis by 1:1 mixing of normal and isotope-labeled glycans, and obtained excellent linear calibration curves from various analytes. Finally, we quantitated the inhibitory effect of tunicamycin, a N-linked glycosylation inhibitor, to glycan expression profile in yeast.
Keywords	Saccharomyces cerevisiae ; bakers yeast ; chemical species ; glucose ; glycomics ; glycoproteins ; glycosylation ; isotope labeling ; mass spectrometry ; polysaccharides ; quantitative analysis ; stable isotopes ; tunicamycin
Language	English
Dates of publication	2021-0515
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1016/j.ab.2021.114152
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Article: Expanding the use of salivary cortisol as a non-invasive outpatient test in the dynamic evaluation of suspected adrenal insufficiency.

Tan, Sarah Ying Tse / Tan, Hong Chang / Zhu, Ling / Loh, Lih Ming / Lim, Dawn Shao Ting / Swee, Du Soon / Chan, Yoke Ling / Lim, Huee Boon / Ling, Shiau Lee / Ou, En Jun / Teo, Wynn Ee / Zhang, Xiao Ping / Goh, Hui Fen / Kek, Peng Chin

Endocrine connections

2023 Volume 12, Issue 4

Abstract: Background: Adrenal insufficiency (AI) is potentially life-threatening, and accurate diagnosis is crucial. The first-line diagnostic test, the adrenocorticotrophic hormone (ACTH) stimulation test, measures serum total cortisol. However, this is affected ...

Abstract	Background: Adrenal insufficiency (AI) is potentially life-threatening, and accurate diagnosis is crucial. The first-line diagnostic test, the adrenocorticotrophic hormone (ACTH) stimulation test, measures serum total cortisol. However, this is affected in states of altered albumin or cortisol-binding globulin levels, limiting reliability. Salivary cortisol reflects free bioactive cortisol levels and is a promising alternative. However, few studies are available, and heterogenous methodologies limit applicability. Methods: This study prospectively recruited 42 outpatients undergoing evaluation for AI, excluding participants with altered cortisol-binding states. Serum (immunoassay) and salivary (liquid chromatography tandem mass spectrometry) cortisol levels were sampled at baseline, 30 min, and 60 min following 250 µg synacthen administration. AI was defined as a peak serum cortisol level <500 nmol/L in accordance with guidelines. Results: The study recruited 21 (50%) participants with AI and 21 without AI. There were no significant differences in baseline characteristics, blood pressure, or sodium levels between groups. Following synacthen stimulation, serum and salivary cortisol levels showed good correlation at all timepoints (R2 = 0.74, P < 0.001), at peak levels (R2 = 0.72, P < 0.001), and at 60 min (R2 = 0.72, P < 0.001). A salivary cortisol cut-off of 16.0 nmol/L had a sensitivity of 90.5% and a specificity of 76.2% for the diagnosis of AI. Conclusion: This study demonstrates a good correlation between serum and salivary cortisol levels during the 250 µg synacthen test. A peak salivary cortisol cut-off of 16.0 nmol/L can be used for the diagnosis of AI. It is a less invasive alternative to evaluate patients with suspected AI. Its potential utility in the diagnosis of AI in patients with altered cortisol-binding states should be further studied.
Language	English
Publishing date	2023-03-28
Publishing country	England
Document type	Journal Article
ZDB-ID	2668428-7
ISSN	2049-3614
ISSN	2049-3614
DOI	10.1530/EC-23-0004
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Article ; Online: Thermoregulation via Temperature-Dependent PGD

Wang, Tongfei A / Teo, Chin Fen / Åkerblom, Malin / Chen, Chao / Tynan-La Fontaine, Marena / Greiner, Vanille Juliette / Diaz, Aaron / McManus, Michael T / Jan, Yuh Nung / Jan, Lily Y

Neuron

2019 Volume 103, Issue 2, Page(s) 349

Language	English
Publishing date	2019-07-18
Publishing country	United States
Document type	Published Erratum
ZDB-ID	808167-0
ISSN	1097-4199 ; 0896-6273
ISSN (online)	1097-4199
ISSN	0896-6273
DOI	10.1016/j.neuron.2019.06.026
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Zs.A 2496: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Dissecting PUGNAc-mediated inhibition of the pro-survival action of insulin.

Teo, Chin Fen / El-Karim, Enas Gad / Wells, Lance

Glycobiology

2016 Volume 26, Issue 11, Page(s) 1198–1208

Abstract: Previous studies utilizing PUGNAc, the most widely used β-N-acetylglucosaminidase (OGA) inhibitor to increase global O-N-acetylglucosamine (GlcNAc) levels, have reported a variety of effects including insulin resistance as a direct result of elevated O- ... ...

Abstract	Previous studies utilizing PUGNAc, the most widely used β-N-acetylglucosaminidase (OGA) inhibitor to increase global O-N-acetylglucosamine (GlcNAc) levels, have reported a variety of effects including insulin resistance as a direct result of elevated O-GlcNAc levels. The notion of OGA inhibition causing insulin resistance was not replicated in studies in which elevated global O-GlcNAc levels were achieved using two other OGA inhibitors. Related to insulin action, work by others has suggested that O-GlcNAc elevation may inhibit the anti-apoptotic action of insulin. Thus, we examined the pro-survival action of insulin upon serum deprivation in the presence of PUGNAc as well as two selective OGA inhibitors (GlcNAcstatin-g and Thiamet-G), and a selective lysosomal hexosaminidase inhibitor (INJ2). We established that PUGNAc inhibits the pro-survival action of insulin but this effect is not recapitulated by the selective OGA inhibitors suggesting that elevation in O-GlcNAc levels alone is not responsible for PUGNAc's effect on the anti-apoptotic action of insulin. Further, we demonstrate that a selective hexosaminidase A/B (HexA/B) inhibitor does not impact insulin action suggesting that PUGNAc's effect is not due to inhibition of lysosomal hexosaminidase. Finally, we tested a combination of selective OGA and lysosomal hexosaminidase inhibitors but were not able to recapitulate the inhibition of insulin action generated by PUGNAc alone. These results strongly suggest that the defect in insulin action upon PUGNAc treatment does not derive from its inhibition of OGA or HexA/B, and that there is an unknown target of PUGNAc that is the likely culprit in inhibiting the protective effect of insulin from apoptosis.
Language	English
Publishing date	2016-11
Publishing country	England
Document type	Journal Article
ZDB-ID	1067689-2
ISSN	1460-2423 ; 0959-6658
ISSN (online)	1460-2423
ISSN	0959-6658
DOI	10.1093/glycob/cww043
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Article: Monitoring protein O-linked β-N-acetylglucosamine status via metabolic labeling and copper-free click chemistry

Teo, Chin Fen / Wells, Lance

Analytical biochemistry. 2014 Nov. 01, v. 464

2014

Abstract	O-Linked β-N-acetylglucosamine (O-GlcNAc) modification found on the serine and threonine residues of intracellular proteins is an inducible post-translational modification that regulates numerous biological processes. In combination with other cell biological and biochemical approaches, a robust and streamlined strategy for detecting the number and stoichiometry of O-GlcNAc modification can provide valuable insights for decoding the functions of O-GlcNAc at the molecular level. Here, we report an optimized workflow for evaluating the O-GlcNAc status of proteins using a combination of metabolic labeling and click chemistry-based mass tagging. This method is strategically complementary to the chemoenzymatic-based mass-tagging method.
Keywords	monitoring ; post-translational modification ; proteins ; serine ; stoichiometry ; threonine
Language	English
Dates of publication	2014-1101
Size	p. 70-72.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1016/j.ab.2014.06.010
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Article ; Online: Kv1.1 channels regulate early postnatal neurogenesis in mouse hippocampus via the TrkB signaling pathway.

Chou, Shu-Min / Li, Ke-Xin / Huang, Ming-Yueh / Chen, Chao / Lin King, Yuan-Hung / Li, Grant Guangnan / Zhou, Wei / Teo, Chin Fen / Jan, Yuh Nung / Jan, Lily Yeh / Yang, Shi-Bing

eLife

2021 Volume 10

Abstract: In the postnatal brain, neurogenesis occurs only within a few regions, such as the hippocampal sub-granular zone (SGZ). Postnatal neurogenesis is tightly regulated by factors that balance stem cell renewal with differentiation, and it gives rise to ... ...

Abstract	In the postnatal brain, neurogenesis occurs only within a few regions, such as the hippocampal sub-granular zone (SGZ). Postnatal neurogenesis is tightly regulated by factors that balance stem cell renewal with differentiation, and it gives rise to neurons that participate in learning and memory formation. The Kv1.1 channel, a voltage-gated potassium channel, was previously shown to suppress postnatal neurogenesis in the SGZ in a cell-autonomous manner. In this study, we have clarified the physiological and molecular mechanisms underlying Kv1.1-dependent postnatal neurogenesis. First, we discovered that the membrane potential of neural progenitor cells is highly dynamic during development. We further established a multinomial logistic regression model for cell-type classification based on the biophysical characteristics and corresponding cell markers. We found that the loss of Kv1.1 channel activity causes significant depolarization of type 2b neural progenitor cells. This depolarization is associated with increased tropomyosin receptor kinase B (TrkB) signaling and proliferation of neural progenitor cells; suppressing TrkB signaling reduces the extent of postnatal neurogenesis. Thus, our study defines the role of the Kv1.1 potassium channel in regulating the proliferation of postnatal neural progenitor cells in mouse hippocampus.
MeSH term(s)	Animals ; Animals, Newborn ; Cell Proliferation ; Gene Expression Regulation, Developmental ; Hippocampus/cytology ; Hippocampus/metabolism ; In Vitro Techniques ; Kv1.1 Potassium Channel/genetics ; Kv1.1 Potassium Channel/metabolism ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; Membrane Potentials ; Mice, Inbred ICR ; Mice, Knockout ; Neural Stem Cells/metabolism ; Neurogenesis ; Neurons/metabolism ; Protein-Tyrosine Kinases/genetics ; Protein-Tyrosine Kinases/metabolism ; Signal Transduction ; Mice
Chemical Substances	Kcna1 protein, mouse ; Membrane Glycoproteins ; Kv1.1 Potassium Channel (147173-20-4) ; Ntrk2 protein, mouse (EC 2.7.10.1) ; Protein-Tyrosine Kinases (EC 2.7.10.1)
Language	English
Publishing date	2021-05-21
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.58779
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