On the public citation graph
A Lumry−Eyring Nucleated Polymerization Model of Protein Aggregation Kinetics: 1. Aggregation with Pre-Equilibrated Unfolding
0 signed · 310 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.
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known work and none has been retracted — and get a dated CiteStamped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.
What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/(sici)1097-0290(19970520)54:4<333::aid-bit6>3.0.co;2-lopenalex-snapshot
Polymerization mechanism of polypeptide chain aggregation
inferredcites →https://doi.org/10.1002/(sici)1097-0290(19990605)63:5<552::aid-bit5>3.0.co;2-8openalex-snapshot
Hydrostatic pressure rescues native protein from aggregates
inferredcites →https://doi.org/10.1002/bit.10705openalex-snapshot
A new kinetic scheme for lysozyme refolding and aggregation
inferredcites →https://doi.org/10.1002/bit.260250908openalex-snapshot
On the role of reversible denaturation (unfolding) in the irreversible thermal inactivation of enzymes
inferredcites →https://doi.org/10.1002/jps.10377openalex-snapshot
Irreversible aggregation of recombinant bovine granulocyte-colony stimulating factor (bG-CSF) and implications for predicting protein shelf life
inferredcites →https://doi.org/10.1002/jps.20079openalex-snapshot
Challenges in the development of high protein concentration formulations
inferredcites →https://doi.org/10.1002/jps.20488openalex-snapshot
Population balance modeling of aggregation kinetics of recombinant human interleukin-1 receptor antagonist
inferredcites →https://doi.org/10.1002/jps.20529openalex-snapshot
Influence of aggregation on immunogenicity of recombinant human Factor VIII in hemophilia A mice
inferredcites →https://doi.org/10.1006/jmbi.1996.0280openalex-snapshot
Intermediate States in Protein Folding
inferredcites →https://doi.org/10.1006/jsbi.2000.4273openalex-snapshot
Review: TTR Amyloidosis—Structural Features Leading to Protein Aggregation and Their Implications on Therapeutic Strategies
inferredcites →https://doi.org/10.1007/978-0-387-36063-8_2openalex-snapshot
Nonnative Protein Aggregation
inferredcites →https://doi.org/10.1007/978-0-387-76643-0_9openalex-snapshot
Challenges in the Development of High Protein Concentration Formulations
inferredcites →https://doi.org/10.1007/s00249-003-0336-5openalex-snapshot
Effect of environmental conditions on aggregation and fibril formation of barstar
inferredcites →https://doi.org/10.1016/0022-2836(85)90174-3openalex-snapshot
Kinetics of sickle hemoglobin polymerization
inferredcites →https://doi.org/10.1016/j.bbadis.2004.09.010openalex-snapshot
Tau aggregation is driven by a transition from random coil to beta sheet structure
inferredcites →https://doi.org/10.1016/j.bbapap.2003.12.008openalex-snapshot
Conformational constraints for amyloid fibrillation: the importance of being unfolded
inferredcites →https://doi.org/10.1016/j.ijpharm.2004.11.014openalex-snapshot
Protein aggregation and its inhibition in biopharmaceutics
inferredcites →https://doi.org/10.1016/j.jmb.2004.06.043openalex-snapshot
Prediction of the Absolute Aggregation Rates of Amyloidogenic Polypeptide Chains
inferredcites →https://doi.org/10.1016/j.sbi.2006.01.011openalex-snapshot
Protein aggregation and amyloidosis: confusion of the kinds?
inferredcites →https://doi.org/10.1016/j.semcdb.2003.12.008openalex-snapshot
Principles of protein folding, misfolding and aggregation
inferredcites →https://doi.org/10.1016/s0006-3495(01)75831-6openalex-snapshot
A Mathematical Model of the Kinetics of β-Amyloid Fibril Growth from the Denatured State
inferredcites →https://doi.org/10.1016/s0006-3495(86)83498-1openalex-snapshot
Cooperative polymerization reactions. Analytical approximations, numerical examples, and experimental strategy
inferredcites →https://doi.org/10.1016/s0006-3495(92)81899-4openalex-snapshot
Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry
inferredcites →https://doi.org/10.1016/s0076-6879(99)09019-9openalex-snapshot
[17] Analysis of protein aggregation kinetics
inferredcites →https://doi.org/10.1016/s0301-4622(03)00134-0openalex-snapshot
Kinetics of heat- and acidification-induced aggregation of firefly luciferase
inferredcites →https://doi.org/10.1016/s1359-0278(98)00002-9openalex-snapshot
Protein aggregation: folding aggregates, inclusion bodies and amyloid
inferredcites →https://doi.org/10.1021/ar0500618openalex-snapshot
The Structural Biology of Protein Aggregation Diseases: Fundamental Questions and Some Answers
inferredcites →https://doi.org/10.1021/bi001547topenalex-snapshot
Conformational Origin of the Aggregation of Recombinant Human Factor VIII
inferredcites →https://doi.org/10.1021/bi001782bopenalex-snapshot
Partially Folded Intermediates as Critical Precursors of Light Chain Amyloid Fibrils and Amorphous Aggregates
inferredcites →https://doi.org/10.1021/bi002555copenalex-snapshot
Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation: Elucidation of the Molecular Mechanism
inferredcites →https://doi.org/10.1021/bi0262698openalex-snapshot
Conformational Prerequisites for α-Lactalbumin Fibrillation
inferredcites →https://doi.org/10.1021/bi047404eopenalex-snapshot
Aggregation of a Slow-Folding Mutant of a β-Clam Protein Proceeds through a Monomeric Nucleus
inferredcites →https://doi.org/10.1021/bi049621lopenalex-snapshot
Transthyretin Aggregation under Partially Denaturing Conditions Is a Downhill Polymerization
inferredcites →https://doi.org/10.1021/bi050225sopenalex-snapshot
Design of Peptidyl Compounds That Affect β-Amyloid Aggregation: Importance of Surface Tension and Context
inferredcites →https://doi.org/10.1021/bi0511484openalex-snapshot
Partitioning Conformational Intermediates between Competing Refolding and Aggregation Pathways: Insights into Transthyretin Amyloid Disease
inferredcites →https://doi.org/10.1021/bi0604936openalex-snapshot
Fibrillation of Human Insulin A and B Chains
inferredcites →https://doi.org/10.1021/bi0606748openalex-snapshot
Exothermic Effects Observed upon Heating of β2-Microglobulin Monomers in the Presence of Amyloid Seeds
inferredcites →https://doi.org/10.1021/bi0618520openalex-snapshot
Kinetics of Inhibition of β-Amyloid Aggregation by Transthyretin
inferredcites →https://doi.org/10.1021/bi982881gopenalex-snapshot
Minimization of Recombinant Human Flt3 Ligand Aggregation at the Tm Plateau: A Matter of Thermal Reversibility
inferredcites →https://doi.org/10.1021/bi991518mopenalex-snapshot
Aggregation Events Occur Prior to Stable Intermediate Formation during Refolding of Interleukin 1β
inferredcites →https://doi.org/10.1021/ja054719oopenalex-snapshot
Light-Activated Hydrogel Formation via the Triggered Folding and Self-Assembly of a Designed Peptide
inferredcites →https://doi.org/10.1021/jp026827sopenalex-snapshot
Kinetics of Irreversible Protein Aggregation: Analysis of Extended Lumry−Eyring Models and Implications for Predicting Protein Shelf Life
inferredcites →https://doi.org/10.1021/js9801384openalex-snapshot
Aggregation of Recombinant Human Interferon Gamma: Kinetics and Structural Transitions
inferredcites →https://doi.org/10.1023/a:1015589926728openalex-snapshot
Kinetics of Thermal Aggregation of Tobacco Mosaic Virus Coat Protein
inferredcites →https://doi.org/10.1023/a:1015899011324openalex-snapshot
Inactivation kinetics of enzyme pharmaceuticals in aqueous solution.
inferredcites →https://doi.org/10.1023/a:1018955031042openalex-snapshot
Is Stability Prediction Possible for Protein Drugs? Denaturation Kinetics of β- Galactosidase in Solution
inferredcites →https://doi.org/10.1023/a:1025771421906openalex-snapshot
Physical Stability of Proteins in Aqueous Solution: Mechanism and Driving Forces in Nonnative Protein Aggregation
inferredcites →https://doi.org/10.1038/nature05290openalex-snapshot
A century-old debate on protein aggregation and neurodegeneration enters the clinic
inferredcites →https://doi.org/10.1038/nbt1012openalex-snapshot
Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
inferredcites →https://doi.org/10.1038/nrm1742openalex-snapshot
What is the role of protein aggregation in neurodegeneration?
inferredcites →https://doi.org/10.1042/bst0041168openalex-snapshot
Thermodynamics of the Polymerization of Protein
inferredcites →https://doi.org/10.1073/pnas.182276099openalex-snapshot
Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
inferredcites →https://doi.org/10.1073/pnas.93.12.5975openalex-snapshot
Kinetics of self-assembling microtubules: an "inverse problem" in biochemistry.
inferredcites →https://doi.org/10.1073/pnas.94.15.7942openalex-snapshot
Kinetic theory of fibrillogenesis of amyloid β-protein
inferredcites →https://doi.org/10.1073/pnas.96.23.13029openalex-snapshot
High pressure fosters protein refolding from aggregates at high concentrations
inferredcites →https://doi.org/10.1074/jbc.274.28.19509openalex-snapshot
α-Synuclein Fibrillogenesis Is Nucleation-dependent
inferredcites →https://doi.org/10.1074/jbc.m005374200openalex-snapshot
Entrapping Intermediates of Thermal Aggregation in α-Helical Proteins with Low Concentration of Guanidine Hydrochloride
inferredcites →https://doi.org/10.1074/jbc.m103629200openalex-snapshot
Reversibility of Scrapie-associated Prion Protein Aggregation
inferredcites →https://doi.org/10.1074/jbc.m311300200openalex-snapshot
Seeding Specificity in Amyloid Growth Induced by Heterologous Fibrils
inferredcites →https://doi.org/10.1110/ps.051471205openalex-snapshot
Prediction of aggregation rate and aggregation‐prone segments in polypeptide sequences
inferredcites →https://doi.org/10.1146/annurev.biochem.66.1.385openalex-snapshot
MODELS OF AMYLOID SEEDING IN ALZHEIMER'S DISEASE AND SCRAPIE: Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid Proteins
inferredcites →https://doi.org/10.1146/annurev.bioeng.4.092801.094202openalex-snapshot
Peptide Aggregation in Neurodegenerative Disease
inferredcites →https://doi.org/10.1208/aapsj080359openalex-snapshot
Effects of protein aggregates: An immunologic perspective
inferredcites →https://doi.org/10.1208/aapsj080366openalex-snapshot
Protein aggregation and bioprocessing
inferredcites →https://doi.org/10.1529/biophysj.104.052415openalex-snapshot
Molecular Dynamics Simulations Indicate a Possible Role of Parallel β-Helices in Seeded Aggregation of Poly-Gln
inferredcites →https://doi.org/10.1529/biophysj.105.073767openalex-snapshot
The Kinetics of Nucleated Polymerizations at High Concentrations: Amyloid Fibril Formation Near and Above the “Supercritical Concentration”
inferredcites →https://doi.org/10.1557/mrs2005.123openalex-snapshot
The Materials Science of Protein Aggregation
inferredcites →https://doi.org/10.2174/092986606775338362openalex-snapshot
Protein Aggregation and Its Consequences for Human Disease
inferredcites →https://doi.org/10.2174/1568013033483230openalex-snapshot
Amyloid Formation by Transthyretin: From Protein Stability to Protein Aggregation
inferredcites →https://doi.org/10.2307/2981344openalex-snapshot
A First Course in Mathematical Statistics.
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4647969openalex-extracted
Analysis of the Thermal Aggregation Behavior and Mechanism of Black Bean Protein
inferred← citeshttps://doi.org/10.1002/9780470572702.ch4openalex-snapshot
Kinetic Models for Protein Misfolding and Association
inferred← citeshttps://doi.org/10.1002/9780470769829.ch2openalex-snapshot
Protein Aggregation Pathways, Kinetics, and Thermodynamics
inferred← citeshttps://doi.org/10.1002/9781118183373.ch14openalex-snapshot
Thermodynamic and Kinetic Models for Aggregation of Intrinsically Disordered Proteins
inferred← citeshttps://doi.org/10.1002/9781118523063.ch12openalex-snapshot
Amyloid‐Like Fibrils: Origin, Structure, Properties, and Potential Technological Applications
inferred← citeshttps://doi.org/10.1002/aic.14349openalex-snapshot
Evaluation of nanoparticle tracking for characterization of fibrillar protein aggregates
inferred← citeshttps://doi.org/10.1002/ange.201305184openalex-snapshot
Molecular Mechanism of Prion Protein Oligomerization at Atomic Resolution
inferred← citeshttps://doi.org/10.1002/anie.201305184openalex-snapshot
Molecular Mechanism of Prion Protein Oligomerization at Atomic Resolution
inferred← citeshttps://doi.org/10.1002/biot.201400018openalex-snapshot
Prediction of IgG1 aggregation in solution
inferred← citeshttps://doi.org/10.1002/biot.201400858openalex-snapshot
A multiscale view of therapeutic protein aggregation: A colloid science perspective
inferred← citeshttps://doi.org/10.1002/bit.21627openalex-snapshot
Non‐native protein aggregation kinetics
inferred← citeshttps://doi.org/10.1002/bit.22957openalex-snapshot
Thermodynamic parameters for salt‐induced reversible protein precipitation from automated microscale experiments
inferred← citeshttps://doi.org/10.1002/bit.23155openalex-snapshot
Aggregates in monoclonal antibody manufacturing processes
inferred← citeshttps://doi.org/10.1002/bit.23188openalex-snapshot
Quaternary conformational stability: The effect of reversible self‐association on the fibrillation of two insulin analogs
inferred← citeshttps://doi.org/10.1002/bit.25129openalex-snapshot
Aggregates of α‐chymotrypsinogen anneal to access more stable states
inferred← citeshttps://doi.org/10.1002/bit.27237openalex-snapshot
Understanding mAb aggregation during low pH viral inactivation and subsequent neutralization
inferred← citeshttps://doi.org/10.1002/btpr.1812openalex-snapshot
Protein misfolding and aggregation research: Some thoughts on improving quality and utility
inferred← citeshttps://doi.org/10.1002/cphc.201402400openalex-snapshot
Concluding the Amyloid Formation Pathway of a Coiled‐Coil‐Based Peptide from the Size of the Critical Nucleus
inferred← citeshttps://doi.org/10.1002/elsc.201600033openalex-snapshot
Downstream process development strategies for effective bioprocesses: Trends, progress, and combinatorial approaches
inferred← citeshttps://doi.org/10.1002/jps.21521openalex-snapshot
Principles, approaches, and challenges for predicting protein aggregation rates and shelf life
inferred← citeshttps://doi.org/10.1002/jps.21566openalex-snapshot
Protein aggregation: Pathways, induction factors and analysis
inferred← citeshttps://doi.org/10.1002/jps.21726openalex-snapshot
Characterization of High-Molecular-Weight Nonnative Aggregates and Aggregation Kinetics by Size Exclusion Chromatography With Inline Multi-Angle Laser Light Scattering
inferred← citeshttps://doi.org/10.1002/jps.21869openalex-snapshot
Multi-variate approach to global protein aggregation behavior and kinetics: Effects of pH, NaCl, and temperature for α-chymotrypsinogen A
inferred← citeshttps://doi.org/10.1002/jps.21938openalex-snapshot
Use of a folding model and in situ spectroscopic techniques for rational formulation development and stability testing of monoclonal antibody therapeutics**Gauri Rao and Vandana Iyer contributed equally to this work.
inferred← citeshttps://doi.org/10.1002/jps.22198openalex-snapshot
Comparative Effects of pH and Ionic Strength on Protein–Protein Interactions, Unfolding, and Aggregation for IgG1 Antibodies
inferred← citeshttps://doi.org/10.1002/jps.22447openalex-snapshot
Nonnative Aggregation of an IgG1 Antibody in Acidic Conditions, Part 2: Nucleation and Growth Kinetics with Competing Growth Mechanisms
inferred← citeshttps://doi.org/10.1002/jps.22448openalex-snapshot
Nonnative Aggregation of an IgG1 Antibody in Acidic Conditions: Part 1. Unfolding, Colloidal Interactions, and Formation of High-Molecular-Weight Aggregates
inferred← citeshttps://doi.org/10.1002/jps.22450openalex-snapshot
High Throughput Formulation Screening for Global Aggregation Behaviors of Three Monoclonal Antibodies
inferred← citeshttps://doi.org/10.1002/jps.22633openalex-snapshot
Predicting accelerated aggregation rates for monoclonal antibody formulations, and challenges for low-temperature predictions
inferred← citeshttps://doi.org/10.1002/jps.23056openalex-snapshot
Aggregation and pH–Temperature Phase Behavior for Aggregates of an IgG2 Antibody
inferred← citeshttps://doi.org/10.1002/jps.23076openalex-snapshot
Comparison of High-Throughput Biophysical Methods to Identify Stabilizing Excipients for a Model IgG2 Monoclonal Antibody: Conformational Stability and Kinetic Aggregation Measurements
inferred← citeshttps://doi.org/10.1002/jps.23264openalex-snapshot
Relating particle formation to salt‐ and pH‐dependent phase separation of non‐native aggregates of alpha‐chymotrypsinogen a
inferred← citeshttps://doi.org/10.1002/jps.24703openalex-snapshot
Probing Submicron Aggregation Kinetics of an IgG Protein by Asymmetrical Flow Field-Flow Fractionation
inferred← citeshttps://doi.org/10.1002/jrs.3013openalex-snapshot
Reversible and irreversible denaturation processes in globular proteins: from collective to molecular spectroscopic analysis
inferred← citeshttps://doi.org/10.1002/jsfa.7184openalex-snapshot
Thermal aggregation behaviour of soy protein: characteristics of different polypeptides and sub‐units
inferred← citeshttps://doi.org/10.1002/pro.281openalex-snapshot
The Hofmeister effect on amyloid formation using yeast prion protein
inferred← citeshttps://doi.org/10.1002/pro.3382openalex-snapshot
Protein–protein interactions controlling interfacial aggregation of rhIL‐1ra are not described by simple colloid models
inferred← citeshttps://doi.org/10.1002/pro.3435openalex-snapshot
Parallel chromatography and in situ scattering to interrogate competing protein aggregation pathways
inferred← citeshttps://doi.org/10.1002/prot.24586openalex-snapshot
Kinetics of protein fibrillation controlled by fibril elongation
inferred← citeshttps://doi.org/10.1002/sfp2.70037openalex-snapshot
A Review of Gelation of Plant Proteins and Their Influencing Factors
inferred← citeshttps://doi.org/10.1002/wnan.102openalex-snapshot
Nanoimaging for protein misfolding diseases
inferred← citeshttps://doi.org/10.1007/10_2019_119openalex-snapshot
Insights on the Formulation of Recombinant Proteins
inferred← citeshttps://doi.org/10.1007/978-1-4939-9678-0_11openalex-snapshot
Evaluation of Temporal Aggregation Processes Using Spatial Intensity Distribution Analysis
inferred← citeshttps://doi.org/10.1007/978-1-61779-921-1_25openalex-snapshot
Size-Exclusion Chromatography with Multi-angle Light Scattering for Elucidating Protein Aggregation Mechanisms
inferred← citeshttps://doi.org/10.1007/978-1-61779-921-1_26openalex-snapshot
Computational Methods to Predict Therapeutic Protein Aggregation
inferred← citeshttps://doi.org/10.1007/978-1-62703-438-8_15openalex-snapshot
Kinetic Analysis of Aggregation Data
inferred← citeshttps://doi.org/10.1007/978-3-031-47567-2_1openalex-snapshot
Design Strategies of Dry Powders for Pulmonary Delivery of Pharmaceutical Peptides
inferred← citeshttps://doi.org/10.1007/s10973-008-9307-5openalex-snapshot
Effect of sucrose on BSA denatured aggregation at high concentration studied by the iso-conversional method and the master plots method
inferred← citeshttps://doi.org/10.1007/s11095-013-1263-5openalex-snapshot
Significance of Unfolding Thermodynamics for Predicting Aggregation Kinetics: A Case Study on High Concentration Solutions of a Multi-Domain Protein
inferred← citeshttps://doi.org/10.1007/s11095-020-02792-1openalex-snapshot
Thermodynamic Unfolding and Aggregation Fingerprints of Monoclonal Antibodies Using Thermal Profiling
inferred← citeshttps://doi.org/10.1007/s11095-021-03120-xopenalex-snapshot
Expanding the toolbox for predictive parameters describing antibody stability considering thermodynamic and kinetic determinants
inferred← citeshttps://doi.org/10.1007/s11095-024-03726-xopenalex-snapshot
Stability of Protein Pharmaceuticals: Recent Advances
inferred← citeshttps://doi.org/10.1007/s11095-025-03874-8openalex-snapshot
Impact of Initial Aggregate Level on Aggregation Potential of Monoclonal Antibodies in Different Buffer Systems
inferred← citeshttps://doi.org/10.1007/s11095-025-03980-7openalex-snapshot
Emerging Technologies and Integrated Interdisciplinary Strategies for Mitigating Protein Aggregation in Therapeutic Formulations
inferred← citeshttps://doi.org/10.1007/s11746-015-2684-6openalex-snapshot
Examination of the Causes of Instability of Soy Protein Isolate During Storage Through Probing of the Heat‐Induced Aggregation
inferred← citeshttps://doi.org/10.1007/s11947-020-02417-wopenalex-snapshot
Incorporation of High-Speed Shearing in the Fabrication of Whole Soybean Curd: Effects on Aggregation Behaviors and Microstructures
inferred← citeshttps://doi.org/10.1007/s11947-026-04332-yopenalex-snapshot
Transglutaminase-Catalyzed Composite Gel of Sonicated Amyloid Fibrils-Whey Protein Isolate: The Role of Amyloid Fibrils and Sonication on Rheological and Intermolecular Perspectives
inferred← citeshttps://doi.org/10.1007/s12013-013-9700-yopenalex-snapshot
A Modified Lumry–Eyring Analysis for the Determination of the Predominant Mechanism Underlying the Diminution of Protein Aggregation by Glycerol
inferred← citeshttps://doi.org/10.1007/s13197-019-04119-4openalex-snapshot
Gel properties of salty liquid whole egg as affected by preheat treatment
inferred← citeshttps://doi.org/10.1016/b978-0-12-819132-3.00008-7openalex-snapshot
Molecular mechanisms of amyloid aggregation in human proteinopathies
inferred← citeshttps://doi.org/10.1016/b978-0-444-64046-8.00465-1openalex-snapshot
Protein Refolding/Renaturation
inferred← citeshttps://doi.org/10.1016/j.ab.2016.08.002openalex-snapshot
Identifying protein aggregation mechanisms and quantifying aggregation rates from combined monomer depletion and continuous scattering
inferred← citeshttps://doi.org/10.1016/j.bbapap.2008.10.016openalex-snapshot
Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature
inferred← citeshttps://doi.org/10.1016/j.bbapap.2012.05.001openalex-snapshot
Inter-domain interactions influence the stability and catalytic activity of the bi-domain protein tyrosine phosphatase PTP99A
inferred← citeshttps://doi.org/10.1016/j.bbapap.2019.140264openalex-snapshot
Early mechanisms of amyloid fibril nucleation in model and disease-related proteins
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2019.04.008openalex-snapshot
Engineering enzyme access tunnels
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2023.108192openalex-snapshot
Understanding and controlling the molecular mechanisms of protein aggregation in mAb therapeutics
inferred← citeshttps://doi.org/10.1016/j.bpc.2009.02.001openalex-snapshot
Kinetic folding studies of the P22 tailspike beta-helix domain reveal multiple unfolded states
inferred← citeshttps://doi.org/10.1016/j.bpc.2011.04.006openalex-snapshot
Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptides
inferred← citeshttps://doi.org/10.1016/j.bpc.2012.06.001openalex-snapshot
Thermodynamics of amyloid dissociation provide insights into aggregate stability regimes
inferred← citeshttps://doi.org/10.1016/j.bpc.2013.11.005openalex-snapshot
Reduction of the C191-C220 disulfide of α-chymotrypsinogen A reduces nucleation barriers for aggregation
inferred← citeshttps://doi.org/10.1016/j.bpc.2015.07.002openalex-snapshot
Aggregate structure, morphology and the effect of aggregation mechanisms on viscosity at elevated protein concentrations
inferred← citeshttps://doi.org/10.1016/j.bpj.2008.12.3903openalex-snapshot
Model Discrimination and Mechanistic Interpretation of Kinetic Data in Protein Aggregation Studies
inferred← citeshttps://doi.org/10.1016/j.ces.2012.04.031openalex-snapshot
Time evolution of amyloid fibril length distribution described by a population balance model
inferred← citeshttps://doi.org/10.1016/j.ces.2020.115479openalex-snapshot
Population balance modelling of aggregation of monoclonal antibody based therapeutic proteins
inferred← citeshttps://doi.org/10.1016/j.cocis.2014.10.002openalex-snapshot
Protein aggregation, particle formation, characterization & rheology
inferred← citeshttps://doi.org/10.1016/j.compositesb.2021.108920openalex-snapshot
Economical improvement on the performances of a soybean flour-based adhesive for wood composites via montmorillonite hybridization
inferred← citeshttps://doi.org/10.1016/j.ejpb.2017.01.019openalex-snapshot
The effect of charge mutations on the stability and aggregation of a human single chain Fv fragment
inferred← citeshttps://doi.org/10.1016/j.ejpb.2019.02.018openalex-snapshot
The ReFOLD assay for protein formulation studies and prediction of protein aggregation during long-term storage
inferred← citeshttps://doi.org/10.1016/j.ejps.2015.06.011openalex-snapshot
Fitting bevacizumab aggregation kinetic data with the Finke–Watzky two-step model: Effect of thermal and mechanical stress
inferred← citeshttps://doi.org/10.1016/j.ejps.2016.03.007openalex-snapshot
Global kinetic analysis of seeded BSA aggregation
inferred← citeshttps://doi.org/10.1016/j.ejps.2024.106924openalex-snapshot
Evaluating the influence of the initial high molecular weight level on monoclonal antibody particle formation kinetics using a short-term chemical stress study
inferred← citeshttps://doi.org/10.1016/j.febslet.2014.01.051openalex-snapshot
Competing aggregation pathways for monoclonal antibodies
inferred← citeshttps://doi.org/10.1016/j.foodchem.2021.130900openalex-snapshot
Heat-induced conversion of multiscale molecular structure of natural food nutrients: A review
inferred← citeshttps://doi.org/10.1016/j.foodchem.2024.141931openalex-snapshot
Controlling the co-aggregation and gelation of cod-soy binary proteins based on partially/fully denatured soy proteins
inferred← citeshttps://doi.org/10.1016/j.foodchem.2025.143232openalex-snapshot
Characterization of the effects of insoluble soybean polysaccharides on the formation and physicochemical properties of soybean isolate protein gel
inferred← citeshttps://doi.org/10.1016/j.foodchem.2025.147442openalex-snapshot
Aggregation behavior and structure analysis of rice bran protein aggregates regulated by ferulic acid
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2017.08.030openalex-snapshot
Effects of selected phosphate salts on gelling properties and water state of whole egg gel
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2019.105379openalex-snapshot
Exploring the mechanism of hollow microcapsule formation by self-assembly of soy 11s protein upon heating
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2025.112049openalex-snapshot
Sustainable protein stabilization: Soy β-conglycinin suppresses the heat-induced aggregation of cod protein by blocking active sites
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2026.112808openalex-snapshot
Crowding-confined thermal unfolding drives hydrophobic compaction to inhibit gelation of soy proteins at high concentrations
inferred← citeshttps://doi.org/10.1016/j.foodres.2025.118199openalex-snapshot
Gel properties of whole soybean curd reinforced by soybean protein isolate amyloid fibrils: Formation mechanism and texture enhancement
inferred← citeshttps://doi.org/10.1016/j.foodres.2026.118683openalex-snapshot
Structural design and cutting-edge applications in food industry of food gels: A comprehensive review
inferred← citeshttps://doi.org/10.1016/j.ifset.2021.102873openalex-snapshot
To improve the gel properties of liquid whole egg by short-term lactic acid bacteria fermentation
inferred← citeshttps://doi.org/10.1016/j.ifset.2025.104075openalex-snapshot
Controlled thermal unfolding of pea protein for additive-free cod-pea binary gel enhancement: A sustainable hybrid protein strategy
inferred← citeshttps://doi.org/10.1016/j.ijadhadh.2023.103389openalex-snapshot
Effects of wood dyestuff on the bonding properties of soybean-based adhesive for commercial plywood production
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2016.08.077openalex-snapshot
Transient structures of keratins from hoof and horn influence their self association and supramolecular assemblies
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2019.06.050openalex-snapshot
Human islet amyloid polypeptide (hIAPP) aggregation in type 2 diabetes: Correlation between intrinsic physicochemical properties of hIAPP aggregates and their cytotoxicity
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2024.129418openalex-snapshot
Heat-induced agglomeration of water-soluble cod proteins toward gelled structures
inferred← citeshttps://doi.org/10.1016/j.ijpharm.2011.03.064openalex-snapshot
Predicting solution aggregation rates for therapeutic proteins: Approaches and challenges
inferred← citeshttps://doi.org/10.1016/j.ijpharm.2018.08.043openalex-snapshot
Protein aggregation – Mechanisms, detection, and control
inferred← citeshttps://doi.org/10.1016/j.ijpharm.2023.123545openalex-snapshot
A comprehensive evaluation of arginine and its derivatives as protein formulation stabilizers
inferred← citeshttps://doi.org/10.1016/j.jmb.2008.06.043openalex-snapshot
β-Lactoglobulin Assembles into Amyloid through Sequential Aggregated Intermediates
inferred← citeshttps://doi.org/10.1016/j.jmb.2008.09.026openalex-snapshot
Atomistic Simulations of the Effects of Polyglutamine Chain Length and Solvent Quality on Conformational Equilibria and Spontaneous Homodimerization
inferred← citeshttps://doi.org/10.1016/j.jmb.2008.12.069openalex-snapshot
Thermodynamic and Kinetic Characterization of a Germ Line Human λ6 Light-Chain Protein: The Relation between Unfolding and Fibrillogenesis
inferred← citeshttps://doi.org/10.1016/j.jmb.2009.10.019openalex-snapshot
Role of Small Oligomers on the Amyloidogenic Aggregation Free-Energy Landscape
inferred← citeshttps://doi.org/10.1016/j.jmb.2012.02.031openalex-snapshot
From Macroscopic Measurements to Microscopic Mechanisms of Protein Aggregation
inferred← citeshttps://doi.org/10.1016/j.jmb.2017.05.006openalex-snapshot
Salt-Mediated Oligomerization of the Mouse Prion Protein Monitored by Real-Time NMR
inferred← citeshttps://doi.org/10.1016/j.tifs.2016.06.005openalex-snapshot
Particle formation and gelation of soymilk: Effect of heat
inferred← citeshttps://doi.org/10.1016/j.xphs.2015.12.017openalex-snapshot
Acetate- and Citrate-Specific Ion Effects on Unfolding and Temperature-Dependent Aggregation Rates of Anti-Streptavidin IgG1
inferred← citeshttps://doi.org/10.1016/j.xphs.2016.02.027openalex-snapshot
Evaluating the Role of the Air-Solution Interface on the Mechanism of Subvisible Particle Formation Caused by Mechanical Agitation for an IgG1 mAb
inferred← citeshttps://doi.org/10.1016/j.xphs.2016.08.009openalex-snapshot
A Comprehensive Evaluation of Nanoparticle Tracking Analysis (NanoSight) for Characterization of Proteinaceous Submicron Particles
inferred← citeshttps://doi.org/10.1016/j.xphs.2016.08.020openalex-snapshot
Both Reversible Self-Association and Structural Changes Underpin Molecular Viscoelasticity of mAb Solutions
inferred← citeshttps://doi.org/10.1016/j.xphs.2019.10.038openalex-snapshot
Relation of Colloidal and Conformational Stabilities to Aggregate Formation in a Monoclonal Antibody
inferred← citeshttps://doi.org/10.1016/j.xphs.2019.10.048openalex-snapshot
Accelerated Aggregation Studies of Monoclonal Antibodies: Considerations for Storage Stability
inferred← citeshttps://doi.org/10.1016/j.xphs.2021.10.039openalex-snapshot
Stress-dependent Flexibility of a Full-length Human Monoclonal Antibody: Insights from Molecular Dynamics to Support Biopharmaceutical Development
inferred← citeshttps://doi.org/10.1016/j.xphs.2022.01.016openalex-snapshot
Effects of Transportation of IV Bags Containing Protein Formulations Via Hospital Pneumatic Tube System: Particle Characterization by Multiple Methods
inferred← citeshttps://doi.org/10.1016/j.xphs.2022.01.017openalex-snapshot
Nucleation in Protein Aggregation in Biotherapeutic Development: A look into the Heart of the Event
inferred← citeshttps://doi.org/10.1016/j.xphs.2022.08.036openalex-snapshot
Advanced Formulations/Drug Delivery Systems for Subcutaneous Delivery of Protein-Based Biotherapeutics
inferred← citeshttps://doi.org/10.1016/j.xphs.2022.11.020openalex-snapshot
An Intercompany Perspective on Practical Experiences of Predicting, Optimizing and Analyzing High Concentration Biologic Therapeutic Formulations
inferred← citeshttps://doi.org/10.1016/j.xphs.2025.103826openalex-snapshot
Analytical control strategy for biologics. Part I: Foundations
inferred← citeshttps://doi.org/10.1016/s0079-6603(08)00606-5openalex-snapshot
Folding Considerations for Therapeutic Protein Formulations
inferred← citeshttps://doi.org/10.1017/9781108332897openalex-snapshot
Continuous Biopharmaceutical Processes
inferred← citeshttps://doi.org/10.1017/9781108332897.002openalex-snapshot
Introduction to Biopharmaceutical Processes
inferred← citeshttps://doi.org/10.1017/9781108332897.003openalex-snapshot
Fundamentals of Protein Chromatography
inferred← citeshttps://doi.org/10.1017/9781108332897.004openalex-snapshot
Countercurrrent Separation Processes
inferred← citeshttps://doi.org/10.1017/9781108332897.005openalex-snapshot
Countercurrent Chromatography for the Capture Step
inferred← citeshttps://doi.org/10.1017/9781108332897.006openalex-snapshot
Countercurrent Chromatography for the Polishing Steps
inferred← citeshttps://doi.org/10.1017/9781108332897.008openalex-snapshot
Protein Aggregation in Biopharmaceutical Processes
inferred← citeshttps://doi.org/10.1021/acs.analchem.5c03781openalex-snapshot
Optimized Tangential Flow Filtration for Efficient Isolation of Highly Pure and Bioactive sEVs
inferred← citeshttps://doi.org/10.1021/acs.biochem.9b00367openalex-snapshot
Arginine to Lysine Mutations Increase the Aggregation Stability of a Single-Chain Variable Fragment through Unfolded-State Interactions
inferred← citeshttps://doi.org/10.1021/acs.bioconjchem.8b00360openalex-snapshot
Suppression of Aggregation of Therapeutic Monoclonal Antibodies during Storage by Removal of Aggregation Precursors Using a Specific Adsorbent of Non-Native IgG Conformers
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5b01160openalex-snapshot
Fragmentation of Amyloid Fibrils Occurs in Preferential Positions Depending on the Environmental Conditions
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5b08748openalex-snapshot
Structural Changes and Aggregation Mechanisms for Anti-Streptavidin IgG1 at Elevated Concentration
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5b11791openalex-snapshot
Kinetics of Monoclonal Antibody Aggregation from Dilute toward Concentrated Conditions
inferred← citeshttps://doi.org/10.1021/acs.jpcb.6b03878openalex-snapshot
Effects of Protein Conformation, Apparent Solubility, and Protein–Protein Interactions on the Rates and Mechanisms of Aggregation for an IgG1Monoclonal Antibody
inferred← citeshttps://doi.org/10.1021/acs.jpcb.6b05473openalex-snapshot
Kinetics of Antibody Aggregation at Neutral pH and Ambient Temperatures Triggered by Temporal Exposure to Acid
inferred← citeshttps://doi.org/10.1021/acs.jpcb.6b09302openalex-snapshot
Modeling the Effect of Monomer Conformational Change on the Early Stage of Protein Self-Assembly into Fibrils
inferred← citeshttps://doi.org/10.1021/acs.jpcb.7b05603openalex-snapshot
Fate of a Stressed Therapeutic Antibody Tracked by Fluorescence Correlation Spectroscopy: Folded Monomers Survive Aggregation
inferred← citeshttps://doi.org/10.1021/acs.langmuir.2c02399openalex-snapshot
Evolution of π-Peptide Self-Assembly: From Understanding to Prediction and Control
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.3c00013openalex-snapshot
Chemometrics in Protein Formulation: Stability Governed by Repulsion and Protein Unfolding
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.3c00081openalex-snapshot
Enhanced Thermal Stability and Reduced Aggregation in an Antibody Fab Fragment at Elevated Concentrations
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.4c00332openalex-snapshot
Molecular Dynamics Simulations Reveal How Competing Protein–Surface Interactions for Glycine, Citrate, and Water Modulate Stability in Antibody Fragment Formulations
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.4c00609openalex-snapshot
Predicting the Long-Term Stability of Biologics with Short-Term Data
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.4c00859openalex-snapshot
Predictive Model Building for Aggregation Kinetics Based on Molecular Dynamics Simulations of an Antibody Fragment
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.5c00993openalex-snapshot
Aggregate Suppression of Recombinant Human Serum Albumin (HSA) by Adenosine Triphosphate (ATP)
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.5c01398openalex-snapshot
Deconvoluting Biophysical Factors that Influence Long-Term Aggregation Rates of High-Concentration Monoclonal Antibody Formulations
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.7b01127openalex-snapshot
Protein Adsorption and Layer Formation at the Stainless Steel–Solution Interface Mediates Shear-Induced Particle Formation for an IgG1 Monoclonal Antibody
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.9b01000openalex-snapshot
The Impact of the Metal Interface on the Stability and Quality of a Therapeutic Fusion Protein
inferred← citeshttps://doi.org/10.1021/bi100978ropenalex-snapshot
Computational Design and Biophysical Characterization of Aggregation-Resistant Point Mutations for γD Crystallin Illustrate a Balance of Conformational Stability and Intrinsic Aggregation Propensity
inferred← citeshttps://doi.org/10.1021/bi7019244openalex-snapshot
Nucleation, Growth, and Activation Energies for Seeded and Unseeded Aggregation of α-Chymotrypsinogen A
inferred← citeshttps://doi.org/10.1021/bi900853vopenalex-snapshot
Physical Instability of a Therapeutic Fc Fusion Protein: Domain Contributions to Conformational and Colloidal Stability
inferred← citeshttps://doi.org/10.1021/bm800056ropenalex-snapshot
Modulation of Self-Association and Subsequent Fibril Formation in an Alanine-Rich Helical Polypeptide
inferred← citeshttps://doi.org/10.1021/ja308852bopenalex-snapshot
A Mechanistic Model for Amorphous Protein Aggregation of Immunoglobulin-like Domains
inferred← citeshttps://doi.org/10.1021/ja311228dopenalex-snapshot
Confounding the Paradigm: Peculiarities of Amyloid Fibril Nucleation
inferred← citeshttps://doi.org/10.1021/ja403147mopenalex-snapshot
Dynamics of an Intrinsically Disordered Protein Reveal Metastable Conformations That Potentially Seed Aggregation
inferred← citeshttps://doi.org/10.1021/jacs.7b08830openalex-snapshot
A Free Energy Barrier Caused by the Refolding of an Oligomeric Intermediate Controls the Lag Time of Amyloid Formation by hIAPP
inferred← citeshttps://doi.org/10.1021/jf300409yopenalex-snapshot
Limited Aggregation Behavior of β-Conglycinin and Its Terminating Effect on Glycinin Aggregation during Heating at pH 7.0
inferred← citeshttps://doi.org/10.1021/jp301091nopenalex-snapshot
Population Balance Modeling of Antibodies Aggregation Kinetics
inferred← citeshttps://doi.org/10.1021/jp4035369openalex-snapshot
Measuring and Modeling Hemoglobin Aggregation below the Freezing Temperature
inferred← citeshttps://doi.org/10.1021/jp505295jopenalex-snapshot
Kinetic Analysis of the Multistep Aggregation Mechanism of Monoclonal Antibodies
inferred← citeshttps://doi.org/10.1021/jp508000wopenalex-snapshot
Role of Cosolutes in the Aggregation Kinetics of Monoclonal Antibodies
inferred← citeshttps://doi.org/10.1021/jp8083088openalex-snapshot
Lumry−Eyring Nucleated-Polymerization Model of Protein Aggregation Kinetics. 2. Competing Growth via Condensation and Chain Polymerization
inferred← citeshttps://doi.org/10.1021/ma901423nopenalex-snapshot
Sequence-Dependent Gelation Kinetics of β-Hairpin Peptide Hydrogels
inferred← citeshttps://doi.org/10.1038/s41598-017-16360-yopenalex-snapshot
Exploration of Protein Unfolding by Modelling Calorimetry Data from Reheating
inferred← citeshttps://doi.org/10.1039/c3an01693eopenalex-snapshot
Real-time evaluation of aggregation using confocal imaging and image analysis tools
inferred← citeshttps://doi.org/10.1039/c3cp54383hopenalex-snapshot
Mapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis
inferred← citeshttps://doi.org/10.1039/c5cp07845hopenalex-snapshot
Estimation of the lag time in a subsequent monomer addition model for fibril elongation
inferred← citeshttps://doi.org/10.1039/c6cs00542jopenalex-snapshot
Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology
inferred← citeshttps://doi.org/10.1039/d0ma00760aopenalex-snapshot
Review of the current state of protein aggregation inhibition from a materials chemistry perspective: special focus on polymeric materials
inferred← citeshttps://doi.org/10.1039/d3cp03103aopenalex-snapshot
Structural, kinetic, and thermodynamic aspects of insulin aggregation
inferred← citeshttps://doi.org/10.1063/1.2779323openalex-snapshot
A quasichemical approach for protein-cluster free energies in dilute solution
inferred← citeshttps://doi.org/10.1063/1.3238569openalex-snapshot
Structure and thermodynamics of colloidal protein cluster formation: Comparison of square-well and simple dipolar models
inferred← citeshttps://doi.org/10.1063/1.3608916openalex-snapshot
Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments
inferred← citeshttps://doi.org/10.1063/1.4819496openalex-snapshot
Protein fibrillation due to elongation and fragmentation of initially appeared fibrils: A simple kinetic model
inferred← citeshttps://doi.org/10.1063/1.4940149openalex-snapshot
Modeling generic aspects of ideal fibril formation
inferred← citeshttps://doi.org/10.1063/1.4965040openalex-snapshot
Kinetics of spontaneous filament nucleation via oligomers: Insights from theory and simulation
inferred← citeshttps://doi.org/10.1063/5.0180691openalex-snapshot
Advanced computational approaches to understand protein aggregation
inferred← citeshttps://doi.org/10.1073/pnas.1211557109openalex-snapshot
First-order rate-determining aggregation mechanism of p53 and its implications
inferred← citeshttps://doi.org/10.1073/pnas.2006684117openalex-snapshot
Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors
inferred← citeshttps://doi.org/10.1073/pnas.2309884120openalex-snapshot
MEnTaT: A machine-learning approach for the identification of mutations to increase protein stability
inferred← citeshttps://doi.org/10.1074/jbc.m116.744573openalex-snapshot
N-terminal Prion Protein Peptides (PrP(120–144)) Form Parallel In-register β-Sheets via Multiple Nucleation-dependent Pathways
inferred← citeshttps://doi.org/10.1080/00218464.2021.1942854openalex-snapshot
Effects of working time on properties of a soybean meal-based adhesive for engineered wood flooring
inferred← citeshttps://doi.org/10.1080/08927022.2015.1125997openalex-snapshot
Thermodynamics, morphology, and kinetics of early-stage self-assembly of π-conjugated oligopeptides
inferred← citeshttps://doi.org/10.1080/19420862.2015.1079678openalex-snapshot
Weak protein interactions and pH- and temperature-dependent aggregation of human Fc1
inferred← citeshttps://doi.org/10.1080/19420862.2017.1358328openalex-snapshot
Preferential interactions of trehalose, L-arginine.HCl and sodium chloride with therapeutically relevant IgG1 monoclonal antibodies
inferred← citeshttps://doi.org/10.1080/19420862.2023.2285277openalex-snapshot
Monoclonal antibody and protein therapeutic formulations for subcutaneous delivery: high-concentration, low-volume vs. low-concentration, high-volume
inferred← citeshttps://doi.org/10.1088/0953-8984/25/37/373101openalex-snapshot
Modelling amyloid fibril formation kinetics: mechanisms of nucleation and growth
inferred← citeshttps://doi.org/10.1088/1361-648x/aa5f10openalex-snapshot
Physical principles of filamentous protein self-assembly kinetics
inferred← citeshttps://doi.org/10.1093/protein/gzu008openalex-snapshot
Conformational stability as a design target to control protein aggregation
inferred← citeshttps://doi.org/10.1093/protein/gzz017openalex-snapshot
Nanobody stability engineering by employing the ΔTm shift; a comparison with apparent rate constants of heat-induced aggregation
inferred← citeshttps://doi.org/10.1101/2020.01.06.895649openalex-snapshot
Unraveling the aggregation dynamics of amyloidogenesis: A data-driven mathematical modeling approach
inferred← citeshttps://doi.org/10.1101/2024.03.06.583680openalex-snapshot
Deep Learning-Based Prediction and Suppression of Protein Aggregation- Prone Regions
inferred← citeshttps://doi.org/10.1103/prxlife.2.043002openalex-snapshot
Spatiotemporal Modeling of Mitochondrial Network Architecture
showing the first 200 of 239 · page through all 239
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.