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2021 ◽  
Author(s):  
Watcharapong Hongjamrassilp ◽  
Daniel T Blumstein

Abstract An increase in ecotourism adversely impacts many animals and contributes to biodiversity loss. To mitigate these impacts, we illustrate the application of a conservation behavior framework towards the development of a sustainable ecotourism management plan. In Ubon Ratchathani, Thailand, thousands of tourists annually come to see a unique mass migration of shrimps on land (referred to as “shrimp parading”). Preliminary work suggests that this tourism has negatively impacted the shrimps. To reduce tourism-related impacts we studied: (1) the decisions shrimps make when parading, and (2) how shrimps respond to different light intensities and colors. We created an artificial stream and tested the conditions that influence parading by experimentally varying the presence of light and systematically manipulating water velocity (10, 60, 100 cm/s). Additionally, we conducted an in situ experiment to study how shrimps respond to tourists’ lights under three intensities (50, 400, 9000 lux) and four colors (white, blue, green, orange, and red). We found most shrimps prefer to leave the river when it is dark and there is low water flow. Shrimps responded the least to red (λmax = 630 nm) and orange (λmax = 625 nm) light at 50 lux. These findings were used to develop a management plan by creating three different tourist zones, which maximize tourist needs and minimize the anthropogenic impacts on the shrimps. This work could be used as an example of the application of conservation behavior framework in developing management plan for sustainable ecotourism for other invertebrate taxa.


2020 ◽  
Vol 202 ◽  
pp. 110938
Author(s):  
Rakeshkumar Yadav ◽  
Vinay Rajput ◽  
Kushal Gohil ◽  
Krishna Khairnar ◽  
Mahesh Dharne

2020 ◽  
Vol 492 (2) ◽  
pp. 2709-2721
Author(s):  
Luca Piccotti ◽  
José Ángel Docobo ◽  
Roberta Carini ◽  
Vakhtang S Tamazian ◽  
Enzo Brocato ◽  
...  

ABSTRACT The study of a selected set of 69 double-lined spectroscopic binaries (SB2) with well-defined visual and spectroscopic orbits was carried out. The orbital parallax, the mass, the colour, and the luminosity of each component were derived from observational data for almost all of these systems. We have also obtained an independent estimation of the component masses by comparing the colour–magnitude diagram (CMD) to the stellar evolution tracks reported by Pietrinferni. Nearly all of the observational points on the CMD are located between two tracks of slightly different mass or which fall very close to the one corresponding to a unique mass value. The masses obtained from the stellar model are in good agreement with their empirical values determined by parallax techniques (orbital, Gaia, and dynamical). This means that our adopted model is rather reliable and can therefore be used to infer further information, such as the age of each component in the studied systems. Our results indicate a fair correspondence between the age of primaries and secondary stars within 3σ. Nevertheless, we caution that these age indications suffer of uncertainties due to both inhomogeneities/low precision of the adopted photometric data and possible systematics. Finally, it is statistically shown that along with the orbital and trigonometric parallaxes, the dynamical parallax can serve as a reliable tool for distance estimates.


2019 ◽  
Author(s):  
Weiming Yang ◽  
Minghui Ao ◽  
Angellina Song ◽  
Yuanwei Xu ◽  
Hui Zhang

AbstractTn antigen (Tn), a single N-acetylgalactosamine (GalNAc) monosaccharide attached to protein Ser/Thr residues, is found on most solid tumors yet rarely detected in adult tissues, featuring it one of the most distinctive signatures of cancers. Although it is prevalent in cancers, Tn-glycosylation sites are not entirely clear owing to the lack of suitable technology. Knowing the Tn-glycosylation sites will spur the development of new vaccines, diagnostics, and therapeutics of cancers. Here, we report a novel technology named EXoO-Tn for large-scale mapping of Tn-glycosylation sites. EXoO-Tn utilizes glycosyltransferase C1GalT1 and isotopically-labeled UDP-Gal(13C6) to tag and convert Tn to Gal(13C6)-Tn, which has a unique mass being distinguishable to other glycans. This exquisite Gal(13C6)-Tn structure is recognized by OpeRATOR that specifically cleaves N-termini of the Gal(13C6)-Tn-occupied Ser/Thr residues to yield site-containing glycopeptides. The use of EXoO-Tn mapped 947 Tn-glycosylation sites from 480 glycoproteins in Jurkat cells. Given the importance of Tn in diseases, EXoO-Tn is anticipated to have broad utility in clinical studies.


2019 ◽  
Vol 36 (1) ◽  
pp. 209-219
Author(s):  
Bill Hickman

Abstract The Eşrefoğlu Mosque in Iznik was destroyed during the Turkish War of Independence, not long after Cornelius Gurlitt published a black and white photograph of its facade taken by G. Berggren. The photograph constitutes the only remaining visual evidence of a building whose initial construction likely dates to the lifetime of the shaykh whose memory it preserved. The flamboyant facade shown in the photograph reveals a unique mass of calligraphy, including inscriptions, published many years ago but revisited here. These inscriptions add to our understanding of the mosque’s history. My own telling of the phases of the building’s construction involves a reexamination of the identity of the mosque’s Ottoman dynastic patrons, principally Gülbahar Hatun, mother of Sultan Bayezid II. The inscriptions also raise questions about the shaykh’s spiritual legacy. Finally, the mosque’s spatial relationship to a nearby dervish lodge and to türbes associated with the shaykh and his family, buildings that also no longer survive, can be newly addressed.


2019 ◽  
Vol 7 ◽  
pp. 783-789
Author(s):  
Martin Novak ◽  
Tatiana Kochlanova ◽  
Anna Tvrda ◽  
Nina Kotlebova

Introduction: Infections caused by Salmonella are an ongoing worldwide public health problem, often found as a source of nosocomial infections, which cause significant socio-economic burdens. Salmonella is a major food-borne pathogen causing primarily gastrointestinal diseases as well as other localized and systemic infections and extraintestinal complications. MALDI-TOF MS is a new method used by clinical laboratories for rapid, reliable, cost-effective and user-friendly diagnosis of many medical important bacteria of public health interest. The use of this technique improves early identification of genus Salmonella on the species, subspecies and even serovar level, which has a positive impact on public health. Objectives: The aim of the study was to evaluate the importance of MALDI-TOF mass spectrometry for rapid identification of epidemiologically important Salmonella serovars. Based on the latest knowledge about specific biomarker molecules the possibility to identify Salmonella enterica subsp. enterica serovar Enteritidis was verified, which is one of the most common serovars present in Europe associated with gastrointestinal diseases. For serovar Enteritidis a unique mass peak at m/z 6,036 was used. Methods: 140 clinical Salmonella isolates were collected from January to October 2017. Serotyping of Salmonella species, subspecies and serovars was performed by slide agglutination technique: 139 isolates were identified as Salmonella enterica subsp. enterica and one isolate as Salmonella enterica subsp. diarizonae (IIIb). From 139 isolates of Salmonella enterica subsp. enterica the following serovars were detected: 108 Enteritidis, 12 Typhimurium, 6 Infantis, 3 Agona, 3 Derby, 7 others. All isolates were identified also by MALDI-TOF MS as Salmonella spp. For all isolates a unique mass peak at m/z 6.036 was used, which is considered to be relevant for serovar Enteritidis according to the most recent known data. Results: 103 isolates from a total of 108 slide agglutination positive isolates for serovar Enteritidis showed a specific mass signal at  m/z 6,036 (+/-). 5 isolates did not contain this specific protein. After repeated analysis from re-culture, the specific protein was found also in the remaining 5 isolates. 32 serovars other than Enteritidis did not contain this specific biomarker molecule. Conclusion: We can confirm that MALDI-TOF MS is a rapid and reliable method to identify of the most common serovar Salmonella Enteritidis based on the diagnostic marker peak at m/z 6,036 identified by recent studies.  This unique mass signal showed 100% specificity and 95% sensitivity for Enteritidis serovar in our study. We can conclude that the determination of this frequently present serovar is significantly accelerated by MALDI-TOF MS. The rapid and reliable diagnosis is important for the early treatment and prevention of the spread of salmonellosis with a positive impact on public health.


2019 ◽  
Vol 164 ◽  
pp. 202-210 ◽  
Author(s):  
Qiang Zhao ◽  
Nan Zhao ◽  
Xueting Ye ◽  
Meixi He ◽  
Yiren Yang ◽  
...  

2018 ◽  
Author(s):  
Wenfa Ng

Ribosomes are the protein synthesis factories of a cell and thus are evolutionary conserved in structure and function. Comprising a large and small subunit, the ribosome is further made up of ribosomal proteins that give structure and function to different parts of the macromolecular complex. Current methods for isolating the ribosome include density gradient ultracentrifugation that separates the ribosome into the large and small subunit. Separation of the various ribosomal proteins that comprise each of the subunit would require a solubilization step followed by the use of sodium dodecyl sulphate and polyacrylamide gel electrophoresis (SDS-PAGE). However, possibility exists for the use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) to profile the set of ribosomal proteins that could be solubilized from each ribosome subunit. Using ribosomal protein amino acid sequence information from Kyoto Encyclopaedia of Genes and Genomes (KEGG), the molecular weight of each ribosomal protein from Pseudomonas aeruginosa PAO1 was calculated in this report. Obtained results revealed that each ribosomal protein had a unique mass that could be detected by mid-range MALDI-TOF MS instruments. More importantly, the mass of ribosomal proteins constitutes a unique mass fingerprint of each ribosome subunit, which accounts for the different structure and functions of the large and small ribosome subunit. Overall, current mass resolution of MALDI-TOF MS instruments could resolve ribosomal proteins and thus provides a tool for profiling the set of ribosomal proteins that constitute the large and small subunit of the ribosome.


2018 ◽  
Author(s):  
Wenfa Ng

Ribosomes are the protein synthesis factories of a cell and thus are evolutionary conserved in structure and function. Comprising a large and small subunit, the ribosome is further made up of ribosomal proteins that give structure and function to different parts of the macromolecular complex. Current methods for isolating the ribosome include density gradient ultracentrifugation that separates the ribosome into the large and small subunit. Separation of the various ribosomal proteins that comprise each of the subunit would require a solubilization step followed by the use of sodium dodecyl sulphate and polyacrylamide gel electrophoresis (SDS-PAGE). However, possibility exists for the use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) to profile the set of ribosomal proteins that could be solubilized from each ribosome subunit. Using ribosomal protein amino acid sequence information from Kyoto Encyclopaedia of Genes and Genomes (KEGG), the molecular weight of each ribosomal protein from Pseudomonas aeruginosa PAO1 was calculated in this report. Obtained results revealed that each ribosomal protein had a unique mass that could be detected by mid-range MALDI-TOF MS instruments. More importantly, the mass of ribosomal proteins constitutes a unique mass fingerprint of each ribosome subunit, which accounts for the different structure and functions of the large and small ribosome subunit. Overall, current mass resolution of MALDI-TOF MS instruments could resolve ribosomal proteins and thus provides a tool for profiling the set of ribosomal proteins that constitute the large and small subunit of the ribosome.


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