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Ice-binding structure and mechanism of an antifreeze protein from winter flounder
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/bip.360260805openalex-snapshot
Conformational constraints of amino acid side chains in α‐helices
inferredcites →https://doi.org/10.1016/0006-291x(77)90357-6openalex-snapshot
Structural studies on the freezing-point-depressing protein of the winter flounder Pseudopleuronectes americanus
inferredcites →https://doi.org/10.1016/0020-711x(88)90194-2openalex-snapshot
Integration and control of metabolic processes: pure and applied aspects
inferredcites →https://doi.org/10.1016/0022-2836(86)90504-8openalex-snapshot
Single crystals of a winter flounder antifreeze polypeptide
inferredcites →https://doi.org/10.1016/0022-2836(87)90314-7openalex-snapshot
Analysis of the relationship between side-chain conformation and secondary structure in globular proteins
inferredcites →https://doi.org/10.1016/0022-2836(88)90292-6openalex-snapshot
Distributions of water around amino acid residues in proteins
inferredcites →https://doi.org/10.1016/0079-6107(84)90007-5openalex-snapshot
Hydrogen bonding in globular proteins
inferredcites →https://doi.org/10.1016/0307-4412(88)90032-5openalex-snapshot
Integration and control of metabolic processes: pure and applied aspects
inferredcites →https://doi.org/10.1016/s0006-3495(91)82234-2openalex-snapshot
Adsorption of alpha-helical antifreeze peptides on specific ice crystal surface planes
inferredcites →https://doi.org/10.1016/s0006-3495(92)81750-2openalex-snapshot
A model for binding of an antifreeze polypeptide to ice
inferredcites →https://doi.org/10.1016/s0006-3495(93)81361-4openalex-snapshot
Adsorption to ice of fish antifreeze glycopeptides 7 and 8
inferredcites →https://doi.org/10.1016/s0021-9258(18)60465-xopenalex-snapshot
Structure-Function Relationships in a Winter Flounder Antifreeze Polypeptide
inferredcites →https://doi.org/10.1016/s0021-9258(19)49684-1openalex-snapshot
Structure-function relationships in an antifreeze polypeptide. The role of neutral, polar amino acids.
inferredcites →https://doi.org/10.1021/ja00080a066openalex-snapshot
Interactions of the D- and L-Forms of Winter Flounder Antifreeze Peptide with the {201} Planes of Ice
inferredcites →https://doi.org/10.1038/333232a0openalex-snapshot
Crystal structure of an antifreeze polypeptide and its mechanistic implications
inferredcites →https://doi.org/10.1039/fd9939500299openalex-snapshot
Inhibition of ice crystal growth by preferential peptide adsorption: a molecular modelling study
inferredcites →https://doi.org/10.1093/protein/6.1.19openalex-snapshot
Molecular dynamics simulation of winter flounder antifreeze protein variants in solution: correlation between side chain spacing and ice lattice
inferredcites →https://doi.org/10.1107/s0021889887012299openalex-snapshot
MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement
inferredcites →https://doi.org/10.1107/s0108767390010224openalex-snapshot
Improved methods for building protein models in electron density maps and the location of errors in these models
inferredcites →https://doi.org/10.1111/j.1432-1033.1986.tb09966.xopenalex-snapshot
Biosynthesis of antifreeze polypeptides in the winter flounder
inferredcites →https://doi.org/10.1111/j.1432-1033.1991.tb16470.xopenalex-snapshot
The effect of enhanced α‐helicity on the activity of a winter flounder antifreeze polypeptide
inferredcites →https://doi.org/10.1126/science.235.4787.458openalex-snapshot
Crystallographic R Factor Refinement by Molecular Dynamics
inferredcites →https://doi.org/10.1126/science.3381086openalex-snapshot
Amino Acid Preferences for Specific Locations at the Ends of α Helices
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Effect of Larval Rearing Temperature on Steroidogenesis Pathway Development in Early Life History in Winter Flounder (Pseudopleuronectes Americanus)
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Structural and chemical complementarity between antibodies and the crystal surfaces they recognize
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Rapid amyloid fibril formation by a winter flounder antifreeze protein requires specific interaction with ice
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Marine Antifreeze Proteins: Types, Functions and Applications
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Metagenomic Analysis of Microbial Cold Stress Proteins in Polar Lacustrine Ecosystems
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The Impact of Climate Change on Marine and Inland Fisheries and Aquaculture in India
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Vertebrates: Fish, Reptiles, and Mammals
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An Ultrapotent, Ultraeconomical, Antifreeze Polypeptide
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Development and Applications of Antifreeze Materials: From Nature to Design
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Bioinspired (Glyco)Polypeptides for Ice‐Control and Cell Cryopreservation
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Antifreeze Protein Activity: From Ice Binding to Ice Growth Inhibition
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Effect of antifreeze protein on nucleation, growth and memory of gas hydrates
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Antifreeze Glycoproteins: Elucidation of the Structural Motifs That Are Essential for Antifreeze Activity
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Mode of Action and Design Rules for Additives That Modulate Crystal Nucleation
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Antifreeze Glycoproteins: Elucidation of the Structural Motifs That Are Essential for Antifreeze Activity
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Mode of Action and Design Rules for Additives That Modulate Crystal Nucleation
inferred← citeshttps://doi.org/10.1002/bip.20104openalex-snapshot
Intermolecular interaction studies of winter flounder antifreeze protein reveal the existence of thermally accessible binding state
inferred← citeshttps://doi.org/10.1002/bip.20844openalex-snapshot
Activity of short segments of Type I antifreeze protein
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Directed self‐immobilization of alkaline phosphatase on micro‐patterned substrates via genetically fused metal‐binding peptide
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Biomass‐assisted Zeolite Syntheses as a Tool for Designing New Acid Catalysts
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Crystal structure of human lithostathine, the pancreatic inhibitor of stone formation.
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An adenosine kinase in apoplastic location is involved in Magnaporthe oryzae cold acclimation
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The structure, dynamics, and energetics of protein adsorption—lessons learned from adsorption of statherin to hydroxyapatite
inferred← citeshttps://doi.org/10.1002/pro.516openalex-snapshot
Increased flexibility decreases antifreeze protein activity
inferred← citeshttps://doi.org/10.1002/pro.5560050617openalex-snapshot
A natural variant of type I antifreeze protein with four ice‐binding repeats is a particularly potent antifreeze
inferred← citeshttps://doi.org/10.1002/prot.20397openalex-snapshot
A multibody, whole‐residue potential for protein structures, with testing by Monte Carlo simulated annealing
inferred← citeshttps://doi.org/10.1002/prot.20429openalex-snapshot
Hydrophobic tendency of polar group hydration as a major force in type I antifreeze protein recognition
inferred← citeshttps://doi.org/10.1002/prot.20889openalex-snapshot
Effect of a mutation on the structure and dynamics of an α‐helical antifreeze protein in water and ice
inferred← citeshttps://doi.org/10.1002/qua.21857openalex-snapshot
Investigations of structure and dynamics of water solvation of the type I antifreeze protein
inferred← citeshttps://doi.org/10.1006/abbi.1998.0930openalex-snapshot
Secondary Structure of Antifreeze Proteins from Overwintering Larvae of the BeetleDendroides canadensis
inferred← citeshttps://doi.org/10.1006/cryo.1999.2158openalex-snapshot
Anin VivoStudy of Antifreeze Protein Adjuvant Cryosurgery
inferred← citeshttps://doi.org/10.1006/cryo.2000.2265openalex-snapshot
A Comprehensive Evaluation of the Effects and Mechanisms of Antifreeze Proteins during Low-Temperature Preservation
inferred← citeshttps://doi.org/10.1006/cryo.2001.2321openalex-snapshot
Flounder Antifreeze Peptides Increase the Efficacy of Cryosurgery
inferred← citeshttps://doi.org/10.1006/jmbi.2000.4336openalex-snapshot
Understanding the mechanism of ice binding by type III antifreeze proteins
inferred← citeshttps://doi.org/10.1006/prep.1999.1176openalex-snapshot
Extracellular Expression, Purification, and Characterization of a Winter Flounder Antifreeze Polypeptide from Escherichia coli
inferred← citeshttps://doi.org/10.1006/prep.2000.1219openalex-snapshot
Folding and Structural Characterization of Highly Disulfide-Bonded Beetle Antifreeze Protein Produced in Bacteria
inferred← citeshttps://doi.org/10.1007/0-306-46862-x_326openalex-snapshot
A new paradigm for fish antifreeze protein binding to ice
inferred← citeshttps://doi.org/10.1007/128_2006_078openalex-snapshot
Conformation of Glycopeptides and Glycoproteins
inferred← citeshttps://doi.org/10.1007/978-1-0716-3503-2_3openalex-snapshot
Ice Isn’t the Only Crystal in Town: Structure Determination of Ice-Binding Proteins via X-Ray Crystallography
inferred← citeshttps://doi.org/10.1007/978-1-4899-0277-1_12openalex-snapshot
Characterization of Antifreeze Proteins from Winter Rye
inferred← citeshttps://doi.org/10.1007/978-3-030-41929-5_6openalex-snapshot
Insect Antifreeze Proteins
inferred← citeshttps://doi.org/10.1007/978-3-030-41948-6_14openalex-snapshot
Mutational Studies on Antifreeze Proteins
inferred← citeshttps://doi.org/10.1007/978-3-030-41948-6_4openalex-snapshot
Structure–Function of IBPs and Their Interactions with Ice
inferred← citeshttps://doi.org/10.1007/978-3-030-41948-6_5openalex-snapshot
Interaction of Antifreeze Proteins with Water
inferred← citeshttps://doi.org/10.1007/978-3-642-18950-0_3openalex-snapshot
Temperaturwirkungen und Thermoregulation
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Das biologische Abschlusskapitel
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Molecular responses in cold-adapted plants
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Das biologische Abschlusskapitel
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Snow Algae: Adaptation Strategies to Survive on Snow and Ice
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Applications of Antifreeze Proteins: Practical Use of the Quality Products from Japanese Fishes
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Physiological and Biochemical Significance of Antifreeze Substances in Plants
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Catalysis in abiotic structured media: an approach to selective synthesis of biopolymers
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Structure, function and evolution of antifreeze proteins
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Cryo-bioorganic chemistry: molecular interactions at low temperature
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Mechanisms of antifreeze proteins investigated via the site-directed spin labeling technique
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Molecular cloning, expression and characterisation of Afp4, an antifreeze protein from Glaciozyma antarctica
inferred← citeshttps://doi.org/10.1007/s003600050140openalex-snapshot
Molecular characterization and sequencing of antifreeze proteins from larvae of the beetle Dendroides canadensis
inferred← citeshttps://doi.org/10.1007/s10867-012-9291-7openalex-snapshot
Effects of a type I antifreeze protein (AFP) on the melting of frozen AFP and AFP+solute aqueous solutions studied by NMR microimaging experiment
inferred← citeshttps://doi.org/10.1007/s10973-014-4171-yopenalex-snapshot
Enhancement effect of solutes of low molecular mass on the insect antifreeze protein ApAFP752 from Anatolica polita
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Crystallization of Organic Glasses: Effects of Polymer Additives on Bulk and Surface Crystal Growth in Amorphous Nifedipine
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Psychrophilic and psychrotrophic fungi: a comprehensive review
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Ultra-strong anti-freezing hydrogel-based smart window with wide geographical adaptability
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Plant antifreeze proteins and their expression regulatory mechanism
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How to measure the activity of antifreeze proteins?
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A brief review of applications of antifreeze proteins in cryopreservation and metabolic genetic engineering
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Antifreeze Proteins
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Controlling the Freezing Process with Antifreeze Proteins
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Pharmacological Interventions in Vitro
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Light in evaluation of molecular diffusion in tissues: Discrimination of pathologies
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Structure and potential energy surface studies on 310 helices of hen egg white lysozyme and Phaseolus vulgaris arcelin-1 proteins
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Polycarboxylates enhance beetle antifreeze protein activity
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Effects of polyhydroxy compounds on beetle antifreeze protein activity
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Paradoxical effects on ice nucleation are intrinsic to a small winter flounder antifreeze protein
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Rational design of short antifreeze peptides derived from Rhagium inquisitor antifreeze protein
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Influence of surface groups of proteins on water studied by freezing/thawing hysteresis and infrared spectroscopy
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Solution- and Adsorbed-State Structural Ensembles Predicted for the Statherin-Hydroxyapatite System
inferred← citeshttps://doi.org/10.1016/j.cbpa.2012.10.017openalex-snapshot
Epithelial dominant expression of antifreeze proteins in cunner suggests recent entry into a high freeze-risk ecozone
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Effect of larval rearing temperature on steroidogenesis pathway development in winter flounder (Pseudopleuronectes americanus) early life history
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Hydrogen bonds and hydrate interaction between RiAFP and water revealed by molecular dynamics simulations
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Recent advances of bio-inspired anti-icing surfaces
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The adsorption of antifreeze glycoprotein fraction 8 on dry and wet mica
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Molecular dynamics studies show solvation structure of type III antifreeze protein is disrupted at low pH
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Thermal hysteresis caused by non-equilibrium antifreeze activity of poly(vinyl alcohol)
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Significant alterations in anisotropic ice growth rate induced by the ice nucleation-active bacteria Xanthomonas campestris
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Characterization of a family of ice-active proteins from the Ryegrass, Lolium perenne
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inferred← citeshttps://doi.org/10.1016/j.foodchem.2022.134480openalex-snapshot
Screening and characterization of a novel antifreeze peptide from silver carp muscle hydrolysate
inferred← citeshttps://doi.org/10.1016/j.heliyon.2021.e07953openalex-snapshot
Prediction and analysis of antifreeze proteins
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inferred← citeshttps://doi.org/10.1016/j.jcrysgro.2009.12.038openalex-snapshot
Potential of mean force calculation of the free energy of adsorption of Type I winter flounder antifreeze protein on ice
inferred← citeshttps://doi.org/10.1016/j.jct.2020.106267openalex-snapshot
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The response of watercress (Nasturtium officinale) to vacuum impregnation: Effect of an antifreeze protein type I
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Antifreeze Protein from Freeze-Tolerant Grass Has a Beta-Roll Fold with an Irregularly Structured Ice-Binding Site
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Tracing the Origin of the Genetic Code and Thermostability to Dipeptide Sequences in Proteomes
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Identification and isolation of a novel antifreeze peptide from crayfish shells
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Crystallization and self-assembly of calcium carbonate under albumin Langmuir monolayers
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Surface design strategies for mitigating ice and snow accretion
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Cold denaturation induced helix-to-helix transition and its implication to activity of helical antifreeze protein
inferred← citeshttps://doi.org/10.1016/j.molliq.2025.128870openalex-snapshot
Modulation of growth process by hyperactive antifreeze proteins ensue in synergistic way
inferred← citeshttps://doi.org/10.1016/j.pep.2011.11.013openalex-snapshot
Thermolabile antifreeze protein produced in Escherichia coli for structural analysis
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inferred← citeshttps://doi.org/10.1016/j.sbi.2011.01.007openalex-snapshot
The ribosomal tunnel as a functional environment for nascent polypeptide folding and translational stalling
inferred← citeshttps://doi.org/10.1016/j.ssnmr.2011.03.002openalex-snapshot
Threonine side chain conformational population distribution of a type I antifreeze protein on interacting with ice surface studied via 13C–15N dynamic REDOR NMR
inferred← citeshttps://doi.org/10.1016/j.surfin.2026.110973openalex-snapshot
Comparative Evaluation of Antifreeze Proteins for Anti-Icing Coatings and Cryopreservation Applications
inferred← citeshttps://doi.org/10.1016/j.tifs.2025.105252openalex-snapshot
The expanding horizons of antifreeze proteins from food science to multidisciplinary technological innovations
inferred← citeshttps://doi.org/10.1016/s0006-3495(01)75821-3openalex-snapshot
Structure of Type I Antifreeze Protein and Mutants in Supercooled Water
inferred← citeshttps://doi.org/10.1016/s0006-3495(01)75986-3openalex-snapshot
A Theoretical Model of a Plant Antifreeze Protein from Lolium perenne
inferred← citeshttps://doi.org/10.1016/s0006-3495(02)73980-5openalex-snapshot
Analysis of Ice-Binding Sites in Fish Type II Antifreeze Protein by Quantum Mechanics
inferred← citeshttps://doi.org/10.1016/s0006-3495(03)74874-7openalex-snapshot
Freezing of a Fish Antifreeze Protein Results in Amyloid Fibril Formation
inferred← citeshttps://doi.org/10.1016/s0006-3495(96)79204-4openalex-snapshot
Analysis of shorthorn sculpin antifreeze protein stereospecific binding to (2–1 0) faces of ice
inferred← citeshttps://doi.org/10.1016/s0006-3495(96)79476-6openalex-snapshot
Effect of type III antifreeze protein dilution and mutation on the growth inhibition of ice
inferred← citeshttps://doi.org/10.1016/s0006-3495(97)78315-2openalex-snapshot
Ice-binding mechanism of winter flounder antifreeze proteins
inferred← citeshttps://doi.org/10.1016/s0006-3495(98)77862-2openalex-snapshot
Antifreeze Proteins Bind Independently to Ice
inferred← citeshttps://doi.org/10.1016/s0006-3495(98)77923-8openalex-snapshot
Identification of the Ice-Binding Surface on a Type III Antifreeze Protein with a “Flatness Function” Algorithm
inferred← citeshttps://doi.org/10.1016/s0009-2614(03)01257-0openalex-snapshot
A theoretical model on thermal hysteresis activity of the winter flounder protein ‘HPLC-6’
inferred← citeshttps://doi.org/10.1016/s0011-2240(02)00105-0openalex-snapshot
Effects of warming rate, temperature, and antifreeze proteins on the survival of mouse spermatozoa frozen at an optimal rate
inferred← citeshttps://doi.org/10.1016/s0014-5793(01)02213-xopenalex-snapshot
Hydrophobic analogues of the winter flounder ‘antifreeze’ protein
inferred← citeshttps://doi.org/10.1016/s0014-5793(02)03355-0openalex-snapshot
Identification of the ice‐binding face of antifreeze protein from Tenebrio molitor
inferred← citeshttps://doi.org/10.1016/s0014-5793(03)00843-3openalex-snapshot
The effect of hydrophobic analogues of the type I winter flounder antifreeze protein on lipid bilayers
inferred← citeshttps://doi.org/10.1016/s0014-5793(97)00787-4openalex-snapshot
Kinetics of antifreeze protein‐induced ice growth inhibition
inferred← citeshttps://doi.org/10.1016/s0014-5793(98)00327-5openalex-snapshot
The skin‐type antifreeze protein gene intron of the winter flounder is a ubiquitous enhancer lacking a functional C/EBPα binding motif
inferred← citeshttps://doi.org/10.1016/s0014-5793(98)00652-8openalex-snapshot
Valine substituted winter flounder `antifreeze': preservation of ice growth hysteresis
inferred← citeshttps://doi.org/10.1016/s0014-5793(99)00752-8openalex-snapshot
Studies of a putative ice‐binding motif in winter flounder skin‐type anti‐freeze polypeptide
inferred← citeshttps://doi.org/10.1016/s0014-5793(99)00906-0openalex-snapshot
Artificial antifreeze polypeptides: α‐helical peptides with KAAK motifs have antifreeze and ice crystal morphology modifying properties
inferred← citeshttps://doi.org/10.1016/s0014-5793(99)01588-4openalex-snapshot
New ice‐binding face for type I antifreeze protein
inferred← citeshttps://doi.org/10.1016/s0022-0248(99)00267-5openalex-snapshot
Analysis of ice crystal growth for a crystal surface containing adsorbed antifreeze proteins
inferred← citeshttps://doi.org/10.1016/s0022-1910(01)00150-0openalex-snapshot
The role of endogenous antifreeze protein enhancers in the hemolymph thermal hysteresis activity of the beetle Dendroides canadensis
inferred← citeshttps://doi.org/10.1016/s0022-2836(03)00235-3openalex-snapshot
Spruce Budworm Antifreeze Protein: Changes in Structure and Dynamics at Low Temperature
inferred← citeshttps://doi.org/10.1016/s0031-9422(03)00420-5openalex-snapshot
Antifreeze proteins in higher plants
inferred← citeshttps://doi.org/10.1016/s0040-4039(00)01750-0openalex-snapshot
An amino acid that controls polypeptide helicity: β-amino alanine, the first strongly stabilizing C-terminal helix stop signal
inferred← citeshttps://doi.org/10.1016/s0074-7696(01)06019-3openalex-snapshot
Freeze-substitution: Origins and applications
inferred← citeshttps://doi.org/10.1016/s0076-6879(98)95032-7openalex-snapshot
[1] Deciphering rules of helix stability in peptides
inferred← citeshttps://doi.org/10.1016/s0079-6352(99)80101-5openalex-snapshot
Biotechnological potential of North Sea salt marsh plants—a review of traditional knowledge
inferred← citeshttps://doi.org/10.1016/s0168-1656(99)00061-9openalex-snapshot
Biotechnological potential of North Sea salt marsh plants—a review of traditional knowledge
inferred← citeshttps://doi.org/10.1016/s0887-7963(97)80094-6openalex-snapshot
Liquid cold storage of platelets: A revitalized possible alternative for limiting bacterial contamination of platelet products
inferred← citeshttps://doi.org/10.1016/s0959-440x(98)80013-4openalex-snapshot
Simplified proteins: minimalist solutions to the ‘protein folding problem’
inferred← citeshttps://doi.org/10.1016/s0969-2126(02)00745-1openalex-snapshot
Crystal Structure of β-Helical Antifreeze Protein Points to a General Ice Binding Model
inferred← citeshttps://doi.org/10.1016/s0969-2126(96)00140-2openalex-snapshot
Refined solution structure of type III antifreeze protein: hydrophobic groups may be involved in the energetics of the protein–ice interaction
inferred← citeshttps://doi.org/10.1016/s1357-2725(00)00083-2openalex-snapshot
Thermal hysteresis proteins
inferred← citeshttps://doi.org/10.1016/s1359-0294(03)00009-8openalex-snapshot
‘Apples’ and ‘oranges’: comparing the structural aspects of biomineral- and ice-interaction proteins
inferred← citeshttps://doi.org/10.1016/s1380-7323(99)80089-2openalex-snapshot
Modeling of Antifreeze Proteins
inferred← citeshttps://doi.org/10.1016/s2095-3119(20)63463-3openalex-snapshot
Molecular characteristics and structure–activity relationships of food-derived bioactive peptides
inferred← citeshttps://doi.org/10.1017/cbo9780511675997.004openalex-snapshot
Antifreeze and ice-nucleator proteins
inferred← citeshttps://doi.org/10.1021/acs.cgd.8b00172openalex-snapshot
Growth of Ice Crystals in the Presence of Type III Antifreeze Protein
inferred← citeshttps://doi.org/10.1021/acs.chemmater.8b03650openalex-snapshot
Antifreeze Hydrogels from Amphiphilic Statistical Copolymers
inferred← citeshttps://doi.org/10.1021/acs.chemrev.7b00285openalex-snapshot
Crystal Growth with Macromolecular Additives
inferred← citeshttps://doi.org/10.1021/acs.energyfuels.5c00558openalex-snapshot
Recent Development in Molecular Dynamics Simulations of Gas Hydrates in Flow Assurance
inferred← citeshttps://doi.org/10.1021/acs.jafc.6b01911openalex-snapshot
Identification and Evaluation of Cryoprotective Peptides from Chicken Collagen: Ice-Growth Inhibition Activity Compared to That of Type I Antifreeze Proteins in Sucrose Model Systems
inferred← citeshttps://doi.org/10.1021/acs.jcim.1c00915openalex-snapshot
Hyperactive Antifreeze Proteins Promote Ice Growth before Binding to It
inferred← citeshttps://doi.org/10.1021/acs.jctc.0c00773openalex-snapshot
Genetic Algorithm Approach for the Optimization of Protein Antifreeze Activity Using Molecular Simulations
inferred← citeshttps://doi.org/10.1021/acs.jpca.8b00379openalex-snapshot
Excited-State Proton Transfer in 3-Cyano-7-azaindole: From Aqueous Solution to Ice
inferred← citeshttps://doi.org/10.1021/acs.jpcb.2c06478openalex-snapshot
Elucidating the Sluggish Water Dynamics at the Ice-Binding Surface of the Hyperactive Tenebrio molitor Antifreeze Protein
inferred← citeshttps://doi.org/10.1021/acs.jpcb.3c01089openalex-snapshot
Engulfment Avalanches and Thermal Hysteresis for Antifreeze Proteins on Supercooled Ice
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5b04919openalex-snapshot
Will It Be Beneficial To Simulate the Antifreeze Proteins at Ice Freezing Condition or at Lower Temperature?
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5b06474openalex-snapshot
Revealing Surface Waters on an Antifreeze Protein by Fusion Protein Crystallography Combined with Molecular Dynamic Simulations
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5b11164openalex-snapshot
Structure and Dynamics of Antifreeze Protein–Model Membrane Interactions: A Combined Spectroscopic and Molecular Dynamics Study
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5c05027openalex-snapshot
Computational Analysis of Threonine Ladders on Distinct β-Solenoid Scaffolds, with Implications for the Design of Novel Antifreeze Proteins
inferred← citeshttps://doi.org/10.1021/acs.jpcb.6c03191openalex-snapshot
Identifying Ice-Philic Protein Patches to Inform the Ice-Binding Sites of Antifreeze Proteins
inferred← citeshttps://doi.org/10.1021/acs.jpcb.8b00846openalex-snapshot
Operation of Kelvin Effect in the Activities of an Antifreeze Protein: A Molecular Dynamics Simulation Study
inferred← citeshttps://doi.org/10.1021/acs.jpcb.8b04491openalex-snapshot
Solvation Layer of Antifreeze Proteins Analyzed with a Markov State Model
inferred← citeshttps://doi.org/10.1021/acs.jpclett.1c01855openalex-snapshot
High Water Density at Non-Ice-Binding Surfaces Contributes to the Hyperactivity of Antifreeze Proteins
inferred← citeshttps://doi.org/10.1021/acs.jpclett.8b03468openalex-snapshot
Determination of the Solution Structure of Antifreeze Glycoproteins Using Two-Dimensional Infrared Spectroscopy
inferred← citeshttps://doi.org/10.1021/acs.langmuir.5c01771openalex-snapshot
Optimization of the Gold Nanoparticle Colorimetric Assay for Screening and Quantifying Ice Recrystallization Inhibition Activity of Antifreeze Proteins
inferred← citeshttps://doi.org/10.1021/acs.langmuir.7b01733openalex-snapshot
Molecular Insight into the Adsorption of Spruce Budworm Antifreeze Protein to an Ice Surface: A Clathrate-Mediated Recognition Mechanism
inferred← citeshttps://doi.org/10.1021/acs.nanolett.3c03059openalex-snapshot
Self-Assembled Nanostructures of Homo-Oligopeptide as a Potent Ice Growth Inhibitor
inferred← citeshttps://doi.org/10.1021/acsaelm.4c01717openalex-snapshot
Electrically Conductive Zwitterionic Hydrogel with Extraordinary Antifreezing Performance
inferred← citeshttps://doi.org/10.1021/acsnano.4c06610openalex-snapshot
Globular Antifreeze Protein-Inspired Nanoparticle-Based Large-Scale T-Cell Cryoprotection System for Lymphoma Immunotherapy
inferred← citeshttps://doi.org/10.1021/acssuschemeng.9b07701openalex-snapshot
Design of Alanine-Rich Short Peptides as a Green Alternative of Gas Hydrate Inhibitors: Dual Methyl Group Docking for Efficient Adsorption on the Surface of Gas Hydrates
inferred← citeshttps://doi.org/10.1021/bc2004318openalex-snapshot
Conjugation of Type I Antifreeze Protein to Polyallylamine Increases Thermal Hysteresis Activity
inferred← citeshttps://doi.org/10.1021/bi100516eopenalex-snapshot
Compound Ice-Binding Site of an Antifreeze Protein Revealed by Mutagenesis and Fluorescent Tagging
inferred← citeshttps://doi.org/10.1021/bi2003108openalex-snapshot
The Thr- and Ala-Rich Hyperactive Antifreeze Protein from Inchworm Folds as a Flat Silk-like β-Helix
inferred← citeshttps://doi.org/10.1021/bi7020316openalex-snapshot
Hyperactive Antifreeze Protein from Fish Contains Multiple Ice-Binding Sites
inferred← citeshttps://doi.org/10.1021/bi901283popenalex-snapshot
Arginine, a Key Residue for the Enhancing Ability of an Antifreeze Protein of the Beetle Dendroides canadensis
inferred← citeshttps://doi.org/10.1021/bm000004wopenalex-snapshot
Structure−Function Relationship in the Antifreeze Activity of Synthetic Alanine−Lysine Antifreeze Polypeptides
inferred← citeshttps://doi.org/10.1021/bm300366fopenalex-snapshot
Local Ice Melting by an Antifreeze Protein
inferred← citeshttps://doi.org/10.1021/bm4019006openalex-snapshot
Thermodynamics of Engineered Gold Binding Peptides: Establishing the Structure–Activity Relationships
inferred← citeshttps://doi.org/10.1021/cg100336gopenalex-snapshot
Guest Organization by an Amino Acid-Derived Amide Linkage in a Cluster-Based Open Framework
inferred← citeshttps://doi.org/10.1021/cg800269wopenalex-snapshot
In Situ Observation of Antifreeze Glycoprotein Kinetics at the Ice Interface Reveals a Two-Step Reversible Adsorption Mechanism
inferred← citeshttps://doi.org/10.1021/ci000449bopenalex-snapshot
Source of the Ice-Binding Specificity of Antifreeze Protein Type I
inferred← citeshttps://doi.org/10.1021/ci9702353openalex-snapshot
Modeling Studies of Binding of Sea Raven Type II Antifreeze Protein to Ice
inferred← citeshttps://doi.org/10.1021/cr950260copenalex-snapshot
Antifreeze Proteins: Structures and Mechanisms of Function
inferred← citeshttps://doi.org/10.1021/ja003680eopenalex-snapshot
Structure and Conformational Behavior of Biopolymers by Density Functional Calculations Employing Periodic Boundary Conditions. I. The Case of Polyglycine, Polyalanine, and Poly-α-aminoisobutyric Acid in Vacuo
inferred← citeshttps://doi.org/10.1021/ja027557uopenalex-snapshot
Reversible Binding of the HPLC6 Isoform of Type I Antifreeze Proteins to Ice Surfaces and the Antifreeze Mechanism Studied by Multiple Quantum Filtering−Spin Exchange NMR Experiment
inferred← citeshttps://doi.org/10.1021/ja963218nopenalex-snapshot
The Role of Alanine Sequences in Forming β-Sheets of Spider Dragline Silk
inferred← citeshttps://doi.org/10.1021/ja9633777openalex-snapshot
A Novel Approach to the Study of Solution Structures and Dynamic Behavior of Paclitaxel and Docetaxel Using Fluorine-Containing Analogs as Probes
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