about
The synaptic acetylcholinesterase tetramer assembles around a polyproline II helixComplex networks govern coiled-coil oligomerization--predicting and profiling by means of a machine learning approachInteraction cloning of Rabin3, a novel protein that associates with the Ras-like GTPase Rab3AIntroducing intermediate filaments: from discovery to diseaseThe discovery of the alpha-helix and beta-sheet, the principal structural features of proteinsStructure of myosin filaments from relaxed Lethocerus flight muscle by cryo-EM at 6 Å resolution.An α/β-Peptide Helix Bundle with a Pure β 3 -Amino Acid Core and a Distinctive Quaternary StructureStructure of a designed, right-handed coiled-coil tetramer containing all biological amino acidsA coiled-coil motif that sequesters ions to the hydrophobic coreMolecular basis for amyloid- polymorphismStructural basis for heteromeric assembly and perinuclear organization of keratin filamentsRibonuclease inhibitor: structure and functionA novel murine gene, Sickle tail, linked to the Danforth's short tail locus, is required for normal development of the intervertebral discEvolutionary patterns in coiled-coils.Coiled coils as possible models of protein structure evolution.Fibrous Protein Structures: Hierarchy, History and Heroes.An amino acid packing code for α-helical structure and protein designDesign of a single-chain polypeptide tetrahedron assembled from coiled-coil segments.Intermediate filaments: a historical perspectiveThe X-Ray Crystal Structure of the Keratin 1-Keratin 10 Helix 2B Heterodimer Reveals Molecular Surface Properties and Biochemical Insights into Human Skin Disease.Structure-functional intimacies of transient receptor potential channels.Elastic Moduli of Helical Polypeptide Chain StructuresThe structure of people's hair.Mechanical response and conformational amplification in α-helical coiled coils.The importance of hydration and DNA conformation in interpreting infrared spectra of cells and tissues.Antimicrobial and antibiofilm activity of designed and synthesized antimicrobial peptide, KABT-AMP.The human keratins: biology and pathology.A helical-dipole model describes the single-channel current rectification of an uncharged peptide ion channelStructural Abnormalities in the Hair of a Patient with a Novel Ribosomopathy.Different polypeptides form the intermediate filaments in bovine hoof and esophageal epithelium and in aortic endothelium.Isolation and characterization of two polypeptides that form intermediate filaments in bovine esophageal epithelium.Sec2 protein contains a coiled-coil domain essential for vesicular transport and a dispensable carboxy terminal domain.Effect of shampoo, conditioner and permanent waving on the molecular structure of human hairConformational intermediates in the folding of a coiled-coil model peptide of the N-terminus of tropomyosin and alpha alpha-tropomyosinA small surface hydrophobic stripe in the coiled-coil domain of type I keratins mediates tetramer stability.X-ray scattering indicates that the leucine zipper is a coiled coilRibonuclease A variants with potent cytotoxic activity.The Molecular Structure of Human Red Blood Cell Membranes from Highly Oriented, Solid Supported Multi-Lamellar Membranes.Modular design in natural and biomimetic soft materials.Phase transition-induced elasticity of α-helical bioelastomeric fibres and networks.
P2860
Q24311587-6B3E95B4-5C25-49D1-8230-CD47ED4D37F0Q24632790-52D28B17-9836-4CB9-91EF-768EA9CAB9EBQ24652911-949D78A7-20AB-4E3D-B5B2-8E04E4D7B3CCQ24657631-F3C1CE3C-79E9-4E33-A23D-6CCA24F546DEQ24673268-459BF8D2-FEBB-4DA1-B121-59D7D86F333BQ27334005-4F499330-278F-474D-9226-CCA22FF22BCCQ27646473-C48E8E9A-5439-4CC7-89BE-732D91252034Q27647767-BF423DF7-4BD8-40E6-A482-F1FEE35759D9Q27657676-DC601092-383D-46DC-8B7F-6EDA850E65B6Q27674499-9EB0EF64-A5E3-4580-9A40-4A34969C3BFCQ27681198-A0ADB002-5BFA-4BB5-B6F7-E0B6AABBBF60Q28272410-822BF3B7-842C-40CC-8C06-EBEEB1A06149Q28589639-CAED01AE-5F4B-4979-8EC9-975A888E615FQ30370663-6FD68C9F-EB65-4341-8108-11499C19F23BQ30374588-9FC6DDF2-5978-4E9E-BDB6-F40B939B923AQ30397687-10840B40-644F-4FC6-9528-6BFF811795F6Q30414380-94A90BBA-6DFB-41D6-9BD8-54940A4A685BQ30446671-C632A107-700C-493E-8CA8-3F7A557C0DB2Q33284286-DF9F0EF4-FEA8-4658-80D7-F5E7E09AC869Q33912727-412D02E0-3676-4266-8352-AFCF8FF687FEQ34089246-F7118B60-8F6E-4FDD-85A4-6D230B60E8DFQ34349934-F952A818-0370-43F9-B123-E4718C632321Q34360736-9D4A0613-2DDE-41A4-9136-AF9945494975Q34398441-C9C3BE6C-FED9-4ED5-AC1C-124FA66340A7Q34495586-F664B50D-3B45-4C0A-8763-096ED232C8B6Q34708068-7707714B-CC33-4333-BF8B-B785B2B3FD73Q34776574-73AC8CFF-1010-4B4D-9932-D6C8B770FCE0Q35305953-90348E51-7EE9-4E66-A35E-451F39388EA6Q35959632-B87D0BD8-AD57-4020-AF13-CF07AD72DC61Q36204639-D92276E6-92C8-44FC-91A1-79B1659BBEC9Q36204691-19496C0B-6F8E-4245-9770-7DA9E16284CDQ36223046-103AF8CB-CF64-4A44-84A6-64B04E2256B8Q36257931-F9454570-FC5A-4431-A46F-E37979A9B845Q36278160-4CCEC57F-B250-4C64-A641-A435104F3790Q36321471-EC384583-58D6-4A06-849C-CC6495F12927Q37376089-A9156B5A-6CE3-4EE1-9ED1-5B05050CBD13Q37466565-31D78E54-EB94-47BB-9889-E5813125B890Q37550456-FBE21EE6-A70C-4AAB-922B-5F3C11FC694FQ37928600-FE39DA3B-2C3D-4413-851B-369220135DCDQ38066383-318BF6BF-5556-4D6F-BDD1-DD950AC92809
P2860
description
1952 nî lūn-bûn
@nan
1952 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1952 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1952年の論文
@ja
1952年論文
@yue
1952年論文
@zh-hant
1952年論文
@zh-hk
1952年論文
@zh-mo
1952年論文
@zh-tw
1952年论文
@wuu
name
Is alpha-keratin a coiled coil?
@ast
Is alpha-keratin a coiled coil?
@en
type
label
Is alpha-keratin a coiled coil?
@ast
Is alpha-keratin a coiled coil?
@en
prefLabel
Is alpha-keratin a coiled coil?
@ast
Is alpha-keratin a coiled coil?
@en
P356
P1433
P1476
Is alpha-keratin a coiled coil?
@en
P2093
P2888
P304
P356
10.1038/170882B0
P407
P577
1952-11-01T00:00:00Z
P6179
1030114758