about
Silk from crickets: a new twist on spinning.Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteinsTunable silk: using microfluidics to fabricate silk fibers with controllable propertiesAssembly mechanism of recombinant spider silk proteins.Harnessing Nature's wisdom. Turning to Nature for inspiration and avoiding her folliesSilk Spinning in Silkworms and SpidersSensing surface morphology of biofibers by decorating spider silk and cellulosic filaments with nematic microdroplets.Solution structure of eggcase silk protein and its implications for silk fiber formationA conserved spider silk domain acts as a molecular switch that controls fibre assemblyProcessing Techniques and Applications of Silk Hydrogels in BioengineeringBiomolecular Evidence of Silk from 8,500 Years AgoConductive polymer combined silk fiber bundle for bioelectrical signal recordingCharacterization of the Fishing Lines in Titiwai (=Arachnocampa luminosa Skuse, 1890) from New Zealand and AustraliaComprehensive Proteomic Analysis of Spider Dragline Silk from Black Widows: A Recipe to Build Synthetic Silk FibersVortex-induced injectable silk fibroin hydrogels.The well-designed hierarchical structure of Musa basjoo for supercapacitors.Non-invasive characterization of structure and morphology of silk fibroin biomaterials using non-linear microscopy.Doxorubicin-loaded silk films: drug-silk interactions and in vivo performance in human orthotopic breast cancer.Microstructure elucidation of historic silk (Bombyx mori) by nuclear magnetic resonance.Mechanical and physical properties of recombinant spider silk films using organic and aqueous solventsEfficient protein production inspired by how spiders make silkRegenerated silk materials for functionalized silk orthopedic devices by mimicking natural processing.Egg case protein-1. A new class of silk proteins with fibroin-like properties from the spider Latrodectus hesperus.Biopolymers: shape memory in spider draglines.High-resolution NMR characterization of a spider-silk mimetic composed of 15 tandem repeats and a CRGD motif.Biomimetics: lessons from nature--an overview.Bioengineered silk protein-based gene delivery systemsMolecular evolution of lepidopteran silk proteins: insights from the ghost moth, Hepialus californicusSoft tissue augmentation using silk gels: an in vitro and in vivo study.On the strength of β-sheet crystallites of Bombyx mori silk fibroin.Water-insoluble silk films with silk I structure.Increased stem cells delivered using a silk gel/scaffold complex for enhanced bone regenerationSequence Identification, Recombinant Production, and Analysis of the Self-Assembly of Egg Stalk Silk Proteins from Lacewing Chrysoperla carnea.Mandibular repair in rats with premineralized silk scaffolds and BMP-2-modified bMSCs.Ultra strong pyroprotein fibres with long-range orderingQuantifying cellular alignment on anisotropic biomaterial platforms.Charge-Tunable Silk-Tropoelastin Protein Alloys That Control Neuron Cell Responses.Reversible hydrogel-solution system of silk with high beta-sheet content.Native-sized recombinant spider silk protein produced in metabolically engineered Escherichia coli results in a strong fiber.Biomaterials derived from silk-tropoelastin protein systems
P2860
Q21134806-A90D5A22-3B7E-4F03-9165-5860D1310192Q24559049-88221221-F060-423B-BCCC-9E22F4FFA199Q24616052-A6B94559-6A7B-4860-AEBE-A9A66B869809Q24645472-E8DB666B-241B-4827-A00C-EECECB0F646EQ24654279-59A0ACD8-20C8-4226-9B64-CD73E86142DDQ26741619-79EA082B-A229-4C42-9228-6BE7BAA48D8EQ27318043-C631C1CD-DFEC-4151-A5C2-11E9C0113F3EQ27655552-6E572E22-EB5E-4FA6-8EA4-1869B7346DE0Q27661584-1B24D317-8688-45EF-A165-1400E6EE5AC7Q28070885-099D02F7-1D5D-4D98-AD1C-97E79BA19009Q28554993-83930535-F977-4161-8C4B-05222C4C7138Q28730719-CCDDBFB4-6092-4C27-9683-506738AA8788Q28817443-88B1F231-E89A-43D6-9FCE-2E40D9433241Q28828898-7BD0FE04-565A-4340-A281-B69C638BC198Q30381342-641608C2-D96B-4238-839F-533717B97788Q30391462-66033C8A-066E-4BCD-ADBA-3A8508DF45EFQ30489968-982FB575-E9C5-40B8-96E3-60E2FCD2A841Q30525060-5D27D03F-7120-4D70-A324-BDC4E48DE221Q30758519-AD1676BA-5365-4BA8-B4FD-BE38F83967ACQ30836825-B35CBEA7-1825-4655-BBBE-DEA880A15362Q30854561-F1D50939-5D34-45B4-BD53-70E1DA1846ABQ31134496-9605C726-5D47-471F-A214-C8469B26F14BQ31157260-B7D944D5-F00F-4BC4-BCD9-7E70D6FF2100Q33237978-0DDAA268-4A86-4F15-AD3B-A11BE960FBD0Q33403773-C9F2DF13-A355-4B36-81AB-C1B24373B928Q33422756-D67A87B1-37A5-491B-98DD-D5E45E96A417Q33478275-BA60858D-A5B8-42BD-B354-D6709DF588B6Q33574536-98AF4CB9-F654-4D8A-A909-D60C131230C5Q33606732-D7D3B847-9144-4C5B-991E-26DE149094ECQ33656070-17D21C99-B165-4A93-9FB3-A2C83BFBF56AQ33695565-4D4303F0-CA8F-4B49-BF54-C91AE96B8AB6Q33708592-B8C89900-4605-42DA-9F70-3AB516CDEAD0Q33837710-A561E15C-7BA2-4285-B9F7-3D52DA76D1D2Q33856099-9BDB4698-75DF-449E-B900-9E09AF765B5CQ33903217-9FDE00AF-24C3-4338-8B66-12A09F13A121Q33944567-BE22BBCC-CFFB-48BF-93DB-04CF19D2D5CFQ33988574-4EB4529B-DFFD-4426-8A23-C5BE53AE8DD0Q34033759-36C8D542-E3C1-4E14-ACE0-897094AFEFF7Q34069650-2664663C-1EB7-4BC6-BAC8-4A80114A940FQ34106425-01632E61-247F-4100-922D-8D6290BA15D3
P2860
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
Mechanism of silk processing in insects and spiders.
@en
Mechanism of silk processing in insects and spiders.
@nl
type
label
Mechanism of silk processing in insects and spiders.
@en
Mechanism of silk processing in insects and spiders.
@nl
prefLabel
Mechanism of silk processing in insects and spiders.
@en
Mechanism of silk processing in insects and spiders.
@nl
P2860
P356
P1433
P1476
Mechanism of silk processing in insects and spiders.
@en
P2093
David L Kaplan
Hyoung-Joon Jin
P2860
P2888
P304
P356
10.1038/NATURE01809
P407
P577
2003-08-01T00:00:00Z
P5875
P6179
1023466213