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Analysis of the Thermal Aggregation Behavior and Mechanism of Black Bean Protein

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

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Effects of succinylation on thermal induced amyloid formation in Concanavalin A

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Thermal Denaturation and Aggregation of Whey Proteins

inferredcites →https://doi.org/10.1016/j.foodchem.2016.09.064openalex-extracted

Alkali solution extraction of rice residue protein isolates: Influence of alkali concentration on protein functional, structural properties and lysinoalanine formation

inferredcites →https://doi.org/10.1016/j.foodhyd.2016.10.003openalex-extracted

Effects of ultrasound treatment on physicochemical and emulsifying properties of whey proteins pre- and post-thermal aggregation

inferredcites →https://doi.org/10.1016/j.foodhyd.2018.03.016openalex-extracted

Radical cross-linked whey protein aggregates as building blocks of non-heated cold-set gels

inferredcites →https://doi.org/10.1016/j.lwt.2020.110786openalex-extracted

Robustness of protein: Using pH shifting and low speed shearing to partially recover conformation and dispersibility of myosin from pale, soft, exudative (PSE)-like chicken breast

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Effects of flexibility and surface hydrophobicity on emulsifying properties: Ultrasound-treated soybean protein isolate

inferredcites →https://doi.org/10.1016/s0167-4838(96)00190-2openalex-extracted

The application of circular dichroism to studies of protein folding and unfolding

inferredcites →https://doi.org/10.1021/jf0718897openalex-extracted

Micrometer-Sized Fibrillar Protein Aggregates from Soy Glycinin and Soy Protein Isolate

inferredcites →https://doi.org/10.1021/jf072400copenalex-extracted

Surface Hydrophobicity of Physicochemically and Enzymatically Treated Milk Proteins in Relation to Techno-functional Properties

inferredcites →https://doi.org/10.1021/jp070212jopenalex-extracted

A Lumry−Eyring Nucleated Polymerization Model of Protein Aggregation Kinetics: 1. Aggregation with Pre-Equilibrated Unfolding

inferredcites →https://doi.org/10.3168/jds.s0022-0302(05)72836-8openalex-extracted

The Kinetics of Heat-Induced Structural Changes of β-Lactoglobulin

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.