On the public citation graph

Amyloid Fibrils for Β- Carotene Delivery – Influence of Self-Assembled Structures on Binding and in Vitro Bioaccessibility

https://doi.org/10.2139/ssrn.4874530
0 signed · 36 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1007/s00109-003-0464-5openalex-snapshot
Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
inferredcites →https://doi.org/10.1007/s00217-014-2294-9openalex-snapshot
Effects of additional fibrils on structural and rheological properties of rice bran albumin solution and gel
inferredcites →https://doi.org/10.1016/j.cis.2019.05.002openalex-snapshot
Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications
inferredcites →https://doi.org/10.1016/j.cis.2022.102750openalex-snapshot
Recent progresses in the delivery of β-carotene: From nano/microencapsulation to bioaccessibility
inferredcites →https://doi.org/10.1016/j.foodchem.2015.03.128openalex-snapshot
Fluorescence quenching study of resveratrol binding to zein and gliadin: Towards a more rational approach to resveratrol encapsulation using water-insoluble proteins
inferredcites →https://doi.org/10.1016/j.foodchem.2018.01.143openalex-snapshot
Spectroscopic and docking studies on the interaction between caseins and β-carotene
inferredcites →https://doi.org/10.1016/j.foodchem.2020.128963openalex-snapshot
Application of whey protein isolate fibrils in encapsulation and protection of β-carotene
inferredcites →https://doi.org/10.1016/j.foodchem.2022.132884openalex-snapshot
Structural and chemical changes induced by temperature and pH hinder the digestibility of whey proteins
inferredcites →https://doi.org/10.1016/j.foodhyd.2014.04.028openalex-snapshot
Beta-carotene encapsulated in food protein nanoparticles reduces peroxyl radical oxidation in Caco-2 cells
inferredcites →https://doi.org/10.1016/j.foodhyd.2016.03.039openalex-snapshot
Formation and pH-stability of whey protein fibrils in the presence of lecithin
inferredcites →https://doi.org/10.1016/j.foodhyd.2018.09.001openalex-snapshot
Enhancing the aqueous solubility of curcumin at acidic condition through the complexation with whey protein nanofibrils
inferredcites →https://doi.org/10.1016/j.foodhyd.2020.106396openalex-snapshot
Assembly behavior, structural characterization and rheological properties of legume proteins based amyloid fibrils
inferredcites →https://doi.org/10.1016/j.foodhyd.2022.107756openalex-snapshot
Changes of in vitro digestion rate and antioxidant activity of digestion products of ethanol-modified whey protein isolates
inferredcites →https://doi.org/10.1016/j.foodhyd.2022.108248openalex-snapshot
Alpha-lactalbumin amyloid-like fibrils for intestinal delivery: Formation, physiochemical characterization, and digestive fate of capsaicin-loaded fibrils
inferredcites →https://doi.org/10.1016/j.foodres.2018.01.040openalex-snapshot
Complexation of thermally-denatured soybean protein isolate with anthocyanins and its effect on the protein structure and in vitro digestibility
inferredcites →https://doi.org/10.1016/j.ijbiomac.2014.02.051openalex-snapshot
Investigation on the binding interaction between silybin and pepsin by spectral and molecular docking
inferredcites →https://doi.org/10.1016/j.ijbiomac.2022.06.062openalex-snapshot
Structural and physicochemical properties of composites between starch nanoparticles and β-carotene prepared via nanoprecipitation
inferredcites →https://doi.org/10.1016/j.jcis.2007.07.015openalex-snapshot
Simultaneous nanoparticle formation and encapsulation driven by hydrophobic interaction of casein-graft-dextran and β-carotene
inferredcites →https://doi.org/10.1016/j.jmb.2006.08.030openalex-snapshot
Mechanism by Which the Amyloid-like Fibrils of a β2-Microglobulin Fragment Are Induced by Fluorine-substituted Alcohols
inferredcites →https://doi.org/10.1016/j.jsb.2004.08.002openalex-snapshot
The binding of thioflavin-T to amyloid fibrils: localisation and implications
inferredcites →https://doi.org/10.1016/j.lwt.2021.111904openalex-snapshot
Physicochemical, emulsifying, and interfacial properties of different whey protein aggregates obtained by thermal treatment
inferredcites →https://doi.org/10.1016/j.saa.2019.118023openalex-snapshot
Analysis of inhibitory interaction between epigallocatechin gallate and alpha-glucosidase: A spectroscopy and molecular simulation study
inferredcites →https://doi.org/10.1021/acs.jafc.9b02423openalex-snapshot
Protein Oxidation and In Vitro Gastric Digestion of Processed Soy-Based Matrices
inferredcites →https://doi.org/10.1021/bm101119topenalex-snapshot
Disassembly and Reassembly of Amyloid Fibrils in Water−Ethanol Mixtures
inferredcites →https://doi.org/10.1021/bm7014224openalex-snapshot
Peptides are Building Blocks of Heat-Induced Fibrillar Protein Aggregates of β-Lactoglobulin Formed at pH 2
inferredcites →https://doi.org/10.1021/jf9042908openalex-snapshot
Characterization of β-Lactoglobulin Fibrillar Assembly Using Atomic Force Microscopy, Polyacrylamide Gel Electrophoresis, and in Situ Fourier Transform Infrared Spectroscopy
inferredcites →https://doi.org/10.1021/ma202157hopenalex-snapshot
Proteins Fibrils from a Polymer Physics Perspective
inferredcites →https://doi.org/10.1038/nrm3810openalex-snapshot
The amyloid state and its association with protein misfolding diseases
inferredcites →https://doi.org/10.1038/s41596-018-0119-1openalex-snapshot
INFOGEST static in vitro simulation of gastrointestinal food digestion
inferredcites →https://doi.org/10.1039/c7ra10981dopenalex-snapshot
On the role of peptide hydrolysis for fibrillation kinetics and amyloid fibril morphology
inferredcites →https://doi.org/10.1039/d2fo03204jopenalex-snapshot
In vitro oxidation and digestibility profiles of iron-loaded whey protein isolate/gum Arabic complexes with different morphologies
inferredcites →https://doi.org/10.1098/rsos.160696openalex-snapshot
Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation
inferredcites →https://doi.org/10.1111/1541-4337.12404openalex-snapshot
Rational Design of Amyloid‐Like Fibrillary Structures for Tailoring Food Protein Techno‐Functionality and Their Potential Health Implications
inferredcites →https://doi.org/10.1126/science.1150057openalex-snapshot
Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils
inferredcites →https://doi.org/10.1515/arh-2006-0018openalex-snapshot
Ca2+-Induced Cold-Set Gelation of Whey Protein Isolate Fibrils
inferredcites →https://doi.org/10.3390/ani13111745openalex-snapshot
Serum Protein Concentration and Serum Protein Fractions in Bottlenose Dolphins (Tursiops truncatus) under Human Care Using Agarose Gel Electrophoresis
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.