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21
Bovine serum albumin catalyzed one-pot, three-component synthesis of dihydropyrano[2,3-c]pyrazole derivatives in aqueous ethanol
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Bovine serum albumin catalyzed one-pot, three-component synthesis of dihydropyrano[2,3-c]pyrazole derivatives in aqueous ethanol

Dalal, Kiran S. ; Tayade, Yogesh A. ; Wagh, Yogesh B. ; Trivedi, Darshak R. ; Dalal, Dipak S. ; Chaudhari, Bhushan L.

RSC advances, 2016-01, Vol.6 (18), p.14868-14879 [Periódico revisado por pares]

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22
Binding studies of aristololactam-β- d -glucoside and daunomycin to human serum albumin
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Binding studies of aristololactam-β- d -glucoside and daunomycin to human serum albumin

Das, Abhi ; Kumar, Gopinatha Suresh

RSC advances, 2014-01, Vol.4 (62), p.33082-33090 [Periódico revisado por pares]

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23
Biophysical investigation of thymoquinone binding to ‘N’ and ‘B’ isoforms of human serum albumin: exploring the interaction mechanism and radical scavenging activity
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Biophysical investigation of thymoquinone binding to ‘N’ and ‘B’ isoforms of human serum albumin: exploring the interaction mechanism and radical scavenging activity

Ishtikhar, Mohd ; Rabbani, Gulam ; Khan, Shawez ; Khan, Rizwan Hasan

RSC advances, 2015-01, Vol.5 (24), p.18218-18232 [Periódico revisado por pares]

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24
A comparative binding mechanism between human serum albumin and α-1-acid glycoprotein with corilagin: biophysical and computational approach
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A comparative binding mechanism between human serum albumin and α-1-acid glycoprotein with corilagin: biophysical and computational approach

Yeggoni, Daniel Pushparaju ; Rachamallu, Aparna ; Subramanyam, Rajagopal

RSC advances, 2016-01, Vol.6 (46), p.40225-40237 [Periódico revisado por pares]

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25
pH-Dependent Adsorption of Human Serum Albumin Protein on a Polystyrene-Block-Poly(acrylic acid)-Coated PVDF Membrane
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pH-Dependent Adsorption of Human Serum Albumin Protein on a Polystyrene-Block-Poly(acrylic acid)-Coated PVDF Membrane

Merzougui, Charaf-Eddine ; Aimar, Pierre ; Bacchin, Patrice ; Causserand, Christel

Membranes (Basel), 2023-11, Vol.13 (12), p.886 [Periódico revisado por pares]

Switzerland: MDPI AG

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26
Binding interactions and FRET between bovine serum albumin and various phenothiazine-/anthracene-based dyes: a structure-property relationship
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Binding interactions and FRET between bovine serum albumin and various phenothiazine-/anthracene-based dyes: a structure-property relationship

Bhuin, Shouvik ; Halder, Sayantan ; Saha, Subit Kumar ; Chakravarty, Manab

RSC advances, 2021-01, Vol.11 (3), p.1679-1693 [Periódico revisado por pares]

England: Royal Society of Chemistry

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27
Characterizing the binding interaction of astilbin with bovine serum albumin: a spectroscopic study in combination with molecular docking technology
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Characterizing the binding interaction of astilbin with bovine serum albumin: a spectroscopic study in combination with molecular docking technology

Liu, Jianli ; He, Yonglin ; Liu, Dan ; He, Yin ; Tang, Zhipeng ; Lou, Hong ; Huo, Yapeng ; Cao, Xiangyu

RSC advances, 2018-01, Vol.8 (13), p.728-7286 [Periódico revisado por pares]

England: Royal Society of Chemistry

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28
Inhibition of toxic metal-alpha synuclein interactions by human serum albumin
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Inhibition of toxic metal-alpha synuclein interactions by human serum albumin

Martinez Pomier, Karla ; Ahmed, Rashik ; Huang, Jinfeng ; Melacini, Giuseppe

Chemical science (Cambridge), 2024-03, Vol.15 (1), p.352-3515 [Periódico revisado por pares]

England: Royal Society of Chemistry

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29
An Overview of Serum Albumin Interactions with Biomedical Alloys
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An Overview of Serum Albumin Interactions with Biomedical Alloys

Klok, Oksana ; Igual Munoz, Anna ; Mischler, Stefano

Materials, 2020-10, Vol.13 (21), p.4858 [Periódico revisado por pares]

Switzerland: MDPI AG

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30
Surface Characterisation of Human Serum Albumin Layers on Activated Ti6Al4V
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Surface Characterisation of Human Serum Albumin Layers on Activated Ti6Al4V

Hierro-Oliva, Margarita ; Gallardo-Moreno, Amparo M ; González-Martín, María Luisa

Materials, 2021-12, Vol.14 (23), p.7416 [Periódico revisado por pares]

Switzerland: MDPI AG

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