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References from Casting Environment and Water Retention Modulate β-Sheet Crystallization and Shelf Stability of Native Bombyx mori Silk Fibroin Films. Local targets link to admitted publications; unresolved targets remain external evidence.
Phylogeny and Evolutionary History of the Silkworm
10.1007/s11427-012-4334-7 · 2012 · External reference
Comparative Mitochondrial Genomes Provide New Insights into the True Wild Progenitor and Origin of Domestic Silkworm Bombyx mori
10.1016/j.ijbiomac.2019.03.002 · 2019 · External reference
Materials Fabrication from Bombyx mori Silk Fibroin
10.1038/nprot.2011.379 · 2011 · External reference
Silk-Based Biomaterials
10.1016/s0142-9612(02)00353-8 · 2003 · External reference
Silk as a Biomaterial
10.1016/j.progpolymsci.2007.05.013 · 2007 · External reference
Functional Modification of Silk Fibroin from Silkworms and Its Application to Medical Biomaterials: A Review
10.1016/j.ijbiomac.2023.129099 · 2024 · External reference
Mechanism of Enzymatic Degradation of Beta-Sheet Crystals
10.1016/j.biomaterials.2009.12.026 · 2010 · External reference
Silk Film Biomaterials for Cornea Tissue Engineering
10.1016/j.biomaterials.2008.11.018 · 2009 · External reference
Micro and Nano-Scale Compartments Guide the Structural Transition of Silk Protein Monomers into Silk Fibers
10.1038/s41467-022-35505-w · 2022 · External reference
Fabrication and Characterization of Biomaterial Film from Gland Silk of Muga and Eri Silkworms
10.1002/bip.22168 · 2013 · External reference
Silk Fibroin of Bombyx mori Is Secreted, Assembling a High Molecular Mass Elementary Unit Consisting of H-Chain, L-Chain, and P25, with a 6:6:1 Molar Ratio
10.1074/jbc.m006897200 · 2000 · External reference
Hydrophobic Interaction of P25, Containing Asn-Linked Oligosaccharide Chains, with the H-L Complex of Silk Fibroin Produced by Bombyx mori
10.1016/s0965-1748(98)00135-0 · 1999 · External reference
Determination of the Site of Disulfide Linkage between Heavy and Light Chains of Silk Fibroin Produced by Bombyx mori
10.1016/s0167-4838(99)00088-6 · 1999 · External reference
Immunological Identification of the Major Disulfide-Linked Light Component of Silk Fibroin
10.1093/oxfordjournals.jbchem.a124122 · 1993 · External reference
New Insight into the Mechanism Underlying Fibroin Secretion in Silkworm Bombyx mori
10.1111/febs.13105 · 2015 · External reference
Functional Material Features of Bombyx mori Silk Light vs Heavy Chain Proteins
10.1021/bm501667j · 2015 · External reference
Structural Study of Irregular Amino Acid Sequences in the Heavy Chain of Bombyx mori Silk Fibroin
10.1021/bm050294m · 2005 · External reference
Silk Fibroin: Structural Implications of a Remarkable Amino Acid Sequence
10.1002/prot.1078 · 2001 · External reference
Conformational Characterization of Bombyx mori Silk Fibroin in the Solid State by High-Frequency Carbon-13 Cross Polarization–Magic Angle Spinning NMR, X-Ray Diffraction, and Infrared Spectroscopy
10.1021/ma00152a009 · 1985 · External reference
Structure of Silk I (Bombyx mori Silk Fibroin before Spinning) –Type II β-Turn, Not α-Helix-
10.3390/molecules26123706 · 2021 · External reference
Chain-Folded Lamellar Stacking Structure of the Crystalline Fraction of Bombyx mori Silk Fibroin with Silk II Form Studied by 2D 13C–13C Homonuclear Correlation NMR Spectroscopy
10.1021/acs.jpcb.4c03716 · 2024 · External reference
Chemical, Thermal, Time, and Enzymatic Stability of Silk Materials with Silk I Structure
10.3390/ijms22084136 · 2021 · External reference
Real-Time Monitoring of the Structural Transition of Bombyx mori Liquid Silk under Pressure by Solid-State NMR
10.1021/jacs.3c04361 · 2023 · External reference
Mechanism of Silk Processing in Insects and Spiders
10.1038/nature01809 · 2003 · External reference
Solid State NMR Spectroscopy
10.1021/ac100761m · 2010 · External reference
Solid-State NMR Spectroscopy
10.1038/s43586-020-00002-1 · 2021 · External reference
Advances in Solid-State NMR for the Studies of Mesoporous Solids: Fast Magic Angle Spinning and Dynamic Nuclear Polarization
10.1016/j.pnmrs.2025.101573 · 2025 · External reference
Proton-Enhanced NMR of Dilute Spins in Solids
10.1063/1.1680061 · 1973 · External reference
13C–1H Dipolar-Assisted Rotational Resonance in Magic-Angle Spinning NMR
10.1016/s0009-2614(01)00791-6 · 2001 · External reference
Determining Secondary Structure in Spider Dragline Silk by Carbon–Carbon Correlation Solid-State NMR Spectroscopy
10.1021/ja8021208 · 2008 · External reference
13C CP/MAS NMR Study on Structural Heterogeneity in Bombyx mori Silk Fiber and Their Generation by Stretching
10.1110/ps.0221702 · 2002 · External reference
Analysis of the Structure of Bombyx mori Silk Fibroin by NMR
10.1021/acs.macromol.5b00160 · 2015 · External reference
Structural Analysis of Silk Using Solid-State NMR
10.1016/j.mrl.2024.200111 · 2024 · External reference
Comparative Structure Analysis of Tyrosine and Valine Residues in Unprocessed Silk Fibroin (Silk I) and in the Processed Silk Fiber (Silk II) from Bombyx mori Using Solid-State 13C, 15N, and 2H NMR
10.1021/bi0119013 · 2002 · External reference
Differential Scanning Calorimetry Techniques: Applications in Biology and Nanoscience
2010 · External reference
Advancing Analysis of Differential Scanning Calorimetry Data – Converging DSC and AI
10.1016/j.mattod.2025.12.036 · 2026 · External reference
Application of Differential Scanning Calorimetry (DSC) and Modulated Differential Scanning Calorimetry (MDSC) in Food and Drug Industries
10.3390/polym12010005 · 2019 · External reference
Water-Insoluble Silk Films with Silk I Structure
10.1016/j.actbio.2009.10.041 · 2010 · External reference
Silk I and Silk II Studied by Fast Scanning Calorimetry
10.1016/j.actbio.2017.04.001 · 2017 · External reference
Determining Beta-Sheet Crystallinity in Fibrous Proteins by Thermal Analysis and Infrared Spectroscopy
10.1021/ma0610109 · 2006 · External reference
Influence of Water Content on the β-Sheet Formation, Thermal Stability, Water Removal, and Mechanical Properties of Silk Materials
10.1021/acs.biomac.5b01685 · 2016 · External reference
Dynamic Protein–Water Relationships during β-Sheet Formation
10.1021/ma071551d · 2008 · External reference
Heat Capacity of Silk Fibroin Based on the Vibrational Motion of Poly(amino acid)s in the Presence and Absence of Water
10.1021/ma8003357 · 2008 · External reference
Characterization of Water in Hydrated Bombyx mori Silk Fibroin Fiber and Films by 2H NMR Relaxation and 13C Solid State NMR
10.1016/j.actbio.2016.12.052 · 2017 · External reference
Thermo-Rheological Behaviour of Native Silk Feedstocks
10.1016/j.eurpolymj.2016.10.054 · 2017 · External reference
Rheological Behaviour of Native Silk Feedstocks
10.1016/j.polymer.2015.04.049 · 2015 · External reference
Chemical Shift Referencing in MAS Solid State NMR
10.1016/s1090-7807(03)00082-x · 2003 · External reference
Physical Properties and Structure of Silk. V. Thermal Behavior of Silk Fibroin in the Random-Coil Conformation
10.1002/pol.1977.180150915 · 1977 · External reference
DSC Studies on Bound Water in Silk Fibroin/S-Carboxymethyl Kerateine Blend Films
10.1016/s0032-3861(98)00611-9 · 1999 · External reference
Structure of Silk Studied with NMR
10.1016/s0079-6565(01)00039-5 · 2001 · External reference
Beating the Heat – Fast Scanning Melts Silk Beta Sheet Crystals
10.1038/srep01130 · 2013 · External reference
Regulation of Silk Material Structure by Temperature-Controlled Water Vapor Annealing
10.1021/bm200062a · 2011 · External reference
Structure–Dynamics–Property Relationships in Silk Fibroin Films Probed via Solid-State NMR
10.1021/acsomega.6c01268 · 2026 · External reference
Understanding Solid-State Structural Transitions and Stability of Silk Fibroin from a Bound Water Perspective
10.1021/acs.biomac.6c00256 · 2026 · External reference
