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Article ; Online: Role of Telemedicine in Diabetes Management.

Dhediya, Rajnish / Chadha, Manoj / Bhattacharya, Arpan D / Godbole, Shreerang / Godbole, Shreeharsh

Journal of diabetes science and technology

2022 Volume 17, Issue 3, Page(s) 775–781

Abstract: Introduction: Telemedicine is a growing arena that may increase access to care for patients with diabetes. It has more relevance for rural populations or those with limited physical access to health care, for improving diabetes care. Telemedicine can ... ...

Abstract	Introduction: Telemedicine is a growing arena that may increase access to care for patients with diabetes. It has more relevance for rural populations or those with limited physical access to health care, for improving diabetes care. Telemedicine can also be used to offer diabetes self-education and transportation barriers for patients living in under-resourced areas or with disabilities. Method: "This review explores the landscape of telemedicine approaches and evidence for incorporation into general practice. Results & discussion: Telehealth platforms have been shown to be both feasible and effective for health care delivery in diabetes, although there are many caveats that require tailoring to the institution, clinician, and patient population. Research in diabetes telehealth should focus next on how to increase access to patients who are known to be marginalized from traditional models of health care.
MeSH term(s)	Humans ; Telemedicine ; Diabetes Mellitus/therapy ; Delivery of Health Care ; Rural Population ; Health Services Accessibility
Language	English
Publishing date	2022-02-28
Publishing country	United States
Document type	Journal Article ; Review
ISSN	1932-2968
ISSN (online)	1932-2968
DOI	10.1177/19322968221081133
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Article: Severe Diabetic Ketoacidosis with Malignant Hyperthermia Like Syndrome and Rhabdomyolysis Treated with ECMO: Unusual Severity and a Rare Occurrence.

Accamma, Krithi / Shamarao, Shivakumar / Ram, Ashwath / Devananda, N S / Krishna, Murali / Bandagi, Lalchand S / Bhattacharya, Arpan Dev / Kinimi, Ilin

Indian journal of critical care medicine : peer-reviewed, official publication of Indian Society of Critical Care Medicine

2023 Volume 27, Issue 11, Page(s) 859–860

Abstract: How to cite this ... ...

Abstract	How to cite this article
Language	English
Publishing date	2023-10-23
Publishing country	India
Document type	Journal Article
ZDB-ID	2121263-6
ISSN	1998-359X ; 0972-5229
ISSN (online)	1998-359X
ISSN	0972-5229
DOI	10.5005/jp-journals-10071-24569
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Article ; Online: Synergistic Enhancement of Electron-Accepting and -Donating Ability of Nonconjugated Polymer Nanodot in Micellar Environment.

Bhattacharya, Arpan / Mukherjee, Tushar Kanti

Langmuir : the ACS journal of surfaces and colloids

2017 Volume 33, Issue 51, Page(s) 14718–14727

Abstract: Understanding the fundamental electron-transfer dynamics in photoactive carbon nanoparticles (CNPs) is vitally important for their fruitful application in photovoltaics and photocatalysis. Herein, photoinduced electron transfer (PET) to and from the ... ...

Abstract	Understanding the fundamental electron-transfer dynamics in photoactive carbon nanoparticles (CNPs) is vitally important for their fruitful application in photovoltaics and photocatalysis. Herein, photoinduced electron transfer (PET) to and from the nonconjugated polymer nanodot (PND), a new class of luminescent CNP, has been investigated in the presence of N,N-dimethylaniline (DMA) and methyl viologen (MV
Language	English
Publishing date	2017--26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2005937-1
ISSN	1520-5827 ; 0743-7463
ISSN (online)	1520-5827
ISSN	0743-7463
DOI	10.1021/acs.langmuir.7b04030
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Article ; Online: Assembly of the Mitochondrial Translation Initiation Complex.

Remes, Cristina / Nguyen, Minh Duc / Spahr, Henrik / Ng, Martin / Fritsch, Clark / Bhattacharya, Arpan / Li, Hong / Cooperman, Barry / Rorbach, Joanna

Methods in molecular biology (Clifton, N.J.)

2023 Volume 2661, Page(s) 217–232

Abstract: Mitochondria maintain their own translational machinery that is responsible for the synthesis of essential components of the oxidative phosphorylation system. The mammalian mitochondrial translation system differs significantly from its cytosolic and ... ...

Abstract	Mitochondria maintain their own translational machinery that is responsible for the synthesis of essential components of the oxidative phosphorylation system. The mammalian mitochondrial translation system differs significantly from its cytosolic and bacterial counterparts. Here, we describe detailed protocols for efficient in vitro reconstitution of the mammalian mitochondrial translation initiation complex, which can be further used for mechanistic analyses of different aspects of mitochondrial translation.
MeSH term(s)	Animals ; Mitochondria/genetics ; Mitochondria/metabolism ; Protein Biosynthesis ; Oxidative Phosphorylation ; Protein Processing, Post-Translational ; Cytosol/metabolism ; Mitochondrial Proteins/metabolism ; Mitochondrial Ribosomes/metabolism ; Mammals/metabolism
Chemical Substances	Mitochondrial Proteins
Language	English
Publishing date	2023-05-10
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-3171-3_13
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Article: Synergistic Enhancement of Electron-Accepting and -Donating Ability of Nonconjugated Polymer Nanodot in Micellar Environment

Bhattacharya, Arpan / Tushar Kanti Mukherjee

Langmuir. 2017 Dec. 26, v. 33, no. 51

2017

Abstract	Understanding the fundamental electron-transfer dynamics in photoactive carbon nanoparticles (CNPs) is vitally important for their fruitful application in photovoltaics and photocatalysis. Herein, photoinduced electron transfer (PET) to and from the nonconjugated polymer nanodot (PND), a new class of luminescent CNP, has been investigated in the presence of N,N-dimethylaniline (DMA) and methyl viologen (MV2+) in homogeneous methanol and sodium dodecyl sulfate (SDS) micelles. It has been observed that both DMA and MV2+ interact with the photoexcited PND and quench the PL intensity as well as excited-state lifetime in bulk methanol. While in bulk methanol, purely diffusion-controlled PET from DMA to MV2+ via PND has been observed, the mechanism and dynamics differ significantly in SDS micelles. In contrast to homogeneous methanol medium, a distinct synergic effect has been observed in SDS micelles. The presence of both DMA and MV2+ enhances the electron-accepting and -donating abilities of PND in SDS micelles. Time-resolved photoluminescence (PL) measurements reveal that the PET process in SDS micelles is nondiffusive in nature mainly due to instantaneous electron transfer at the confined micellar surface. These results have been explained on the basis of heterogeneous microenvironments of SDS micelles which compartmentalize the donor and acceptor inside its micellar pseudo phase. The present findings provide valuable insights into the intrinsic relation between redox and PL properties of nonconjugated PND.
Keywords	carbon nanoparticles ; electron transfer ; methanol ; micelles ; paraquat ; photocatalysis ; photoluminescence ; polymers ; sodium dodecyl sulfate ; solar energy ; synergism
Language	English
Dates of publication	2017-1226
Size	p. 14718-14727.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	2005937-1
ISSN	1520-5827 ; 0743-7463
ISSN (online)	1520-5827
ISSN	0743-7463
DOI	10.1021/acs.langmuir.7b04030
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Article ; Online: Femtosecond laser-induced spin dynamics in single-layer graphene/CoFeB thin films.

Panda, Surya Narayan / Majumder, Sudip / Choudhury, Samiran / Bhattacharya, Arpan / Sinha, Sumona / Barman, Anjan

Nanoscale

2021 Volume 13, Issue 32, Page(s) 13709–13718

Abstract: Graphene/ferromagnet hybrid heterostructures are important building blocks of spintronics due to the unique ability of graphene to transport spin current over unprecedented distances and possible increase in its spin-orbit coupling due to proximity and ... ...

Abstract	Graphene/ferromagnet hybrid heterostructures are important building blocks of spintronics due to the unique ability of graphene to transport spin current over unprecedented distances and possible increase in its spin-orbit coupling due to proximity and hybridization. Here, we present magnetization dynamics over a femtosecond to nanosecond timescale by employing an all-optical time-resolved magneto-optical Kerr effect technique in single-layer graphene (SLG)/CoFeB thin films with varying CoFeB thickness and compared them with reference CoFeB thin films without an SLG underlayer. Gilbert damping variation with CoFeB thickness is modelled to extract spin-mixing conductance for the SLG/CoFeB interface and isolate the two-magnon scattering contribution from spin pumping. In SLG/CoFeB, we have established an inverse relationship between ultrafast demagnetization time (τ
Language	English
Publishing date	2021-07-28
Publishing country	England
Document type	Journal Article
ZDB-ID	2515664-0
ISSN	2040-3372 ; 2040-3364
ISSN (online)	2040-3372
ISSN	2040-3364
DOI	10.1039/d1nr03397b
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Article ; Online: Ataluren binds to multiple protein synthesis apparatus sites and competitively inhibits release factor-dependent termination.

Huang, Shijie / Bhattacharya, Arpan / Ghelfi, Mikel D / Li, Hong / Fritsch, Clark / Chenoweth, David M / Goldman, Yale E / Cooperman, Barry S

Nature communications

2022 Volume 13, Issue 1, Page(s) 2413

Abstract: Genetic diseases are often caused by nonsense mutations, but only one TRID (translation readthrough inducing drug), ataluren, has been approved for clinical use. Ataluren inhibits release factor complex (RFC) termination activity, while not affecting ... ...

Abstract	Genetic diseases are often caused by nonsense mutations, but only one TRID (translation readthrough inducing drug), ataluren, has been approved for clinical use. Ataluren inhibits release factor complex (RFC) termination activity, while not affecting productive binding of near-cognate ternary complex (TC, aa-tRNA.eEF1A.GTP). Here we use photoaffinity labeling to identify two sites of ataluren binding within rRNA, proximal to the decoding center (DC) and the peptidyl transfer center (PTC) of the ribosome, which are directly responsible for ataluren inhibition of termination activity. A third site, within the RFC, has as yet unclear functional consequences. Using single molecule and ensemble fluorescence assays we also demonstrate that termination proceeds via rapid RFC-dependent hydrolysis of peptidyl-tRNA followed by slow release of peptide and tRNA from the ribosome. Ataluren is an apparent competitive inhibitor of productive RFC binding, acting at or before the hydrolysis step. We propose that designing more potent TRIDs which retain ataluren's low toxicity should target areas of the RFC binding site proximal to the DC and PTC which do not overlap the TC binding site.
MeSH term(s)	Oxadiazoles/pharmacology ; Peptide Termination Factors/metabolism ; Protein Biosynthesis ; RNA, Transfer/metabolism ; Ribosomes/metabolism
Chemical Substances	Oxadiazoles ; Peptide Termination Factors ; RNA, Transfer (9014-25-9) ; ataluren (K16AME9I3V)
Language	English
Publishing date	2022-05-06
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-022-30080-6
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Article ; Online: Unraveling the physical properties and superparamagnetism in anti-site disorder controlled Fe

Chaudhuri, S / Bhobe, P A / Bhattacharya, Arpan / Nigam, A K

Journal of physics. Condensed matter : an Institute of Physics journal

2019 Volume 31, Issue 4, Page(s) 45801

Abstract: With an aim to control the anti-site disorder between Fe and Ti atoms in the full Heusler alloy, Fe[Formula: see text]TiSn, we substitute a small percentage of Ti at Fe site to form the Fe[Formula: see text]Ti[Formula: see text]Sn ([Formula: see text]) ... ...

Abstract	With an aim to control the anti-site disorder between Fe and Ti atoms in the full Heusler alloy, Fe[Formula: see text]TiSn, we substitute a small percentage of Ti at Fe site to form the Fe[Formula: see text]Ti[Formula: see text]Sn ([Formula: see text]) series. Using the incident x-rays tuned to the Fe K-edge absorption energy, we record the high resolution synchrotron x-ray diffraction profiles and unambiguously show the reduction in anti-site disorder. In particular, the Fe-Ti anti-site disorder decreases up to an excess Ti content of 0.07; further increase of Ti content leads to disorder between Ti-Sn sites. Detailed characterization vis-á-vis the excess Ti content has been carried out in terms of its thermal and electrical transport, and magnetic properties. Signatures of strong spin fluctuation are seen in all the physical properties reported here. The much disputed high value of the Sommerfeld constant has been shown to be a resultant of such strong spin fluctuations, thus ruling out the long standing controversy of heavy fermionic nature of Fe[Formula: see text]TiSn. Magnetization and the Seebeck coefficient show clear dependence on the disorder. Both dc and ac magnetic measurements reveal the low temperature superparamagnetic nature of this system, comprising of large magnetic clusters [Formula: see text]3 nm in size.
Language	English
Publishing date	2019-01-30
Publishing country	England
Document type	Journal Article
ZDB-ID	1472968-4
ISSN	1361-648X ; 0953-8984
ISSN (online)	1361-648X
ISSN	0953-8984
DOI	10.1088/1361-648X/aaf0c7
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Article: Insights into the Thermodynamics of Polymer NanodotâHuman Serum Albumin Association: A Spectroscopic and Calorimetric Approach

Bhattacharya, Arpan / Das Somnath / Mukherjee Tushar Kanti

Langmuir. 2016 Nov. 22, v. 32, no. 46

2016

Abstract: With the advent of newer luminescent nanoparticles for bioimaging applications, their complex interactions with individual biomolecules need to be understood in great detail, before their direct application into cellular environments. Here, we have ... ...

Abstract	With the advent of newer luminescent nanoparticles for bioimaging applications, their complex interactions with individual biomolecules need to be understood in great detail, before their direct application into cellular environments. Here, we have presented a systematic and detailed study on the interaction between luminescent polymer nanodots (PNDs) and human serum albumin (HSA) in its free and ligand-bound state with the help of spectrophotometric and calorimetric techniques. At physiological pH (pH = 7.4), PNDs quench the intrinsic fluorescence of HSA as a consequence of ground-state complex formation. The binding stoichiometry and various thermodynamic parameters have been evaluated by using isothermal titration calorimetry and the vanât Hoff equation. It has been found that the association of PNDs with HSA is spontaneous (ÎGâ° = â32.48 Â± 1.24 kJ molâÂ¹) and is driven by a favorable negative standard enthalpy change (ÎHâ° = â52.86 Â± 2.12 kJ molâÂ¹) and an unfavorable negative standard entropy change (ÎSâ° = â68.38 Â± 2.96 J molâÂ¹ KâÂ¹). These results have been explained by considering hydrogen bonding interactions between amino and hydroxyl groups (âNHâ and âOH) of PNDs and carboxylate groups (âCOOâ) of glutamate (Glu) and aspartate (Asp) residues of HSA. The binding constant of PNDs with HSA is estimated to be 4.90 Â± 0.19 Ã 10âµ MâÂ¹. Moreover, it has been observed that warfarin-bound HSA (warâHSA) shows a significantly lower binding affinity (Kb = 1.15 Â± 0.19 Ã 10âµ MâÂ¹) toward PNDs, whereas ibuprofen-bound HSA (ibuâHSA) shows a slightly lower affinity (Kb = 3.47 Â± 0.13 Ã 10âµ MâÂ¹) compared with the free HSA. In addition, our results revealed that PNDs displace warfarin from site I (subdomain IIA) of HSA because of the partial unfolding of warâHSA. We hope that the present study will be helpful to understand the fundamental interactions of these biocompatible PNDs with various biological macromolecules.
Keywords	aspartic acid ; binding capacity ; calorimetry ; cellular microenvironment ; enthalpy ; entropy ; equations ; fluorescence ; glutamic acid ; human serum albumin ; hydrogen bonding ; nanoparticles ; pH ; polymers ; spectroscopy ; stoichiometry ; titration ; warfarin
Language	English
Dates of publication	2016-1122
Size	p. 12067-12077.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	2005937-1
ISSN	1520-5827 ; 0743-7463
ISSN (online)	1520-5827
ISSN	0743-7463
DOI	10.1021%2Facs.langmuir.6b02658
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Article ; Online: Insights into the Thermodynamics of Polymer Nanodot-Human Serum Albumin Association: A Spectroscopic and Calorimetric Approach.

Bhattacharya, Arpan / Das, Somnath / Mukherjee, Tushar Kanti

Langmuir : the ACS journal of surfaces and colloids

2016 Volume 32, Issue 46, Page(s) 12067–12077

Abstract	With the advent of newer luminescent nanoparticles for bioimaging applications, their complex interactions with individual biomolecules need to be understood in great detail, before their direct application into cellular environments. Here, we have presented a systematic and detailed study on the interaction between luminescent polymer nanodots (PNDs) and human serum albumin (HSA) in its free and ligand-bound state with the help of spectrophotometric and calorimetric techniques. At physiological pH (pH = 7.4), PNDs quench the intrinsic fluorescence of HSA as a consequence of ground-state complex formation. The binding stoichiometry and various thermodynamic parameters have been evaluated by using isothermal titration calorimetry and the van't Hoff equation. It has been found that the association of PNDs with HSA is spontaneous (ΔG
MeSH term(s)	Binding Sites ; Circular Dichroism ; Humans ; Polymers ; Protein Binding ; Serum Albumin ; Serum Albumin, Human ; Spectrometry, Fluorescence ; Thermodynamics
Chemical Substances	Polymers ; Serum Albumin ; Serum Albumin, Human (ZIF514RVZR)
Language	English
Publishing date	2016--22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2005937-1
ISSN	1520-5827 ; 0743-7463
ISSN (online)	1520-5827
ISSN	0743-7463
DOI	10.1021/acs.langmuir.6b02658
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