Institution
Aligarh Muslim University
Education•Aligarh, Uttar Pradesh, India•
About: Aligarh Muslim University is a education organization based out in Aligarh, Uttar Pradesh, India. It is known for research contribution in the topics: Population & Adsorption. The organization has 8218 authors who have published 16416 publications receiving 289068 citations. The organization is also known as: AMU.
Topics: Population, Adsorption, Metal ions in aqueous solution, Aqueous solution, Circular dichroism
Papers published on a yearly basis
Papers
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TL;DR: A molecular frame work through H-bonding interactions via n→π(*) transitions between neighboring moieties is found which is responsible for high melting point of resulting CT complex and has been attributed to the formation of 1:1 CT complex.
75 citations
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TL;DR: The practical applicability of the cation-exchanger was demonstrated in the separation of Cu(II)-Zn(II) from a synthetic mixture as well as from real samples of pharmaceutical formulation and brass alloy.
75 citations
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TL;DR: In this article, a two-dimensional metal organic framework was designed under solvothermal condition and characterized thoroughly by FTIR, PXRD, TGA and single crystal X-ray studies.
75 citations
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TL;DR: Conformational alterations of bovine hemoglobin upon sequential addition of glyoxal over a range of 0–90% v/v were investigated and revealed aggregates and AGEs to be genotoxic in nature.
Abstract: Conformational alterations of bovine hemoglobin (Hb) upon sequential addition of glyoxal over a range of 0–90% v/v were investigated. At 20% v/v glyoxal, molten globule (MG) state of Hb was observed by altered tryptophan fluorescence, high ANS binding, existence of intact heme, native-like secondary structure as depicted by far-UV circular dichroism (CD) and ATR-FTIR spectra as well as loss in tertiary structure as confirmed by near-UV CD spectra. In addition, size exclusion chromatography analysis depicted that MG state at 20% v/v glyoxal corresponded to expanded pre-dissociated dimers. Aggregates of Hb were detected at 70% v/v glyoxal. These aggregates of Hb had altered tryptophan environment, low ANS binding, exposed heme, increased β-sheet secondary structure, loss in tertiary structure, enhanced thioflavin T (ThT) fluorescence and red shifted Congo Red (CR) absorbance. On incubating Hb with 30% v/v glyoxal for 0–20 days, advanced glycation end products (AGEs) were detected on day 20. These AGEs were characterised by enhanced tryptophan fluorescence at 450 nm, exposure of heme, increase in intermolecular β-sheets, enhanced ThT fluorescence and red shift in CR absorbance. Comet assay revealed aggregates and AGEs to be genotoxic in nature. Scanning electron microscopy confirmed the amorphous structure of aggregates and branched fibrils of AGEs. The transformation of α-helix to β-sheet usually alters the normal protein to amyloidogenic resulting in a variety of protein conformational disorders such as diabetes, prion and Huntington's.
75 citations
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TL;DR: In this paper, a copper-based metal organic framework (MOF), [Cu2(Hbtc) 2(H2O)2(µ2-H 2O] (Cu-btc-1), where H3btc=benzene-1,2,4-tricarboxylic acid is synthesized employing one pot solvothermal method, is shown to be water stable and recyclable and therefore has been employed in adsorption and separation of methylene blue with excellent efficiency from the mixture of three organic
75 citations
Authors
Showing all 8370 results
Name | H-index | Papers | Citations |
---|---|---|---|
Sandeep Kumar | 94 | 1563 | 38652 |
Detlef W. Bahnemann | 88 | 517 | 48826 |
Gaurav Sharma | 82 | 1244 | 31482 |
Sang Un Ahn | 82 | 391 | 22067 |
M. Irfan | 80 | 241 | 20154 |
M. Mohisin Khan | 77 | 266 | 17940 |
Nazeer Ahmad | 74 | 143 | 18305 |
Rajeev Kumar | 72 | 296 | 20848 |
Syed F. Ali | 71 | 446 | 18669 |
Ahmad Umar | 71 | 740 | 21014 |
Aamir Ahmad | 63 | 251 | 13404 |
Mohammad Athar | 63 | 329 | 14384 |
A. Ahmad Masoodi | 62 | 80 | 12771 |
Shahid Husain | 62 | 437 | 14444 |
Mohd Danish Azmi | 61 | 186 | 13130 |