Sequential interactions of structural proteins in phage phi 29 procapsid assembly.
about
Involvement of the portal at an early step in herpes simplex virus capsid assembly.The proteome and interactome of Streptococcus pneumoniae phage Cp-1Assembly of the herpes simplex virus capsid: identification of soluble scaffold-portal complexes and their role in formation of portal-containing capsids.Bacteriophage protein-protein interactionsThe bacteriophage lambda gpNu3 scaffolding protein is an intrinsically disordered and biologically functional procapsid assembly catalyst.Construction of bacteriophage phi29 DNA packaging motor and its applications in nanotechnology and therapySequence requirement for hand-in-hand interaction in formation of RNA dimers and hexamers to gear phi29 DNA translocation motor.Fabrication of stable and RNase-resistant RNA nanoparticles active in gearing the nanomotors for viral DNA packaging.Role of channel lysines and the "push through a one-way valve" mechanism of the viral DNA packaging motor.Molecular dissection of ø29 scaffolding protein function in an in vitro assembly systemCrystallization and initial X-ray diffraction studies of scaffolding protein (gp7) of bacteriophage phi29.Dynamic motions of free and bound O29 scaffolding protein identified by hydrogen deuterium exchange mass spectrometryNew approach to develop ultra-high inhibitory drug using the power function of the stoichiometry of the targeted nanomachine or biocomplex.Solid-State and Biological Nanopore for Real-Time Sensing of Single Chemical and Sequencing of DNA.Development of Potent Antiviral Drugs Inspired by Viral Hexameric DNA-Packaging Motors with Revolving Mechanism.In vitro incorporation of the phage Phi29 connector complex.Discovery of a new method for potent drug development using power function of stoichiometry of homomeric biocomplexes or biological nanomotorsBiomedical and Catalytic Opportunities of Virus-Like Particles in Nanotechnology.A P22 scaffold protein mutation increases the robustness of head assembly in the presence of excess portal protein.In vitro assembly of infectious virions of double-stranded DNA phage phi 29 from cloned gene products and synthetic nucleic acids.Complete inhibition of virion assembly in vivo with mutant procapsid RNA essential for phage phi 29 DNA packaging.Approaches to determine stoichiometry of viral assembly components.Magnesium-induced conformational change of packaging RNA for procapsid recognition and binding during phage phi29 DNA encapsidation.Sequential action of six virus-encoded DNA-packaging RNAs during phage phi29 genomic DNA translocation.Channel size conversion of Phi29 DNA-packaging nanomotor for discrimination of single- and double-stranded nucleic acidsOne-way traffic of a viral motor channel for double-stranded DNA translocationIncorporation of a viral DNA-packaging motor channel in lipid bilayers for real-time, single-molecule sensing of chemicals and double-stranded DNA.
P2860
Q24534403-F57FB085-19AB-4E1D-9838-1FB6A879E4AEQ24634323-480C2012-53E8-4164-8EE1-C458E953CBF4Q24646283-5C6E6E83-C2DB-4D7E-8322-9BF25DC5151AQ28269950-42BA2F34-EADC-4F6E-A4CC-DE5154BAED3DQ30405723-3C403ADC-36F2-41D1-B425-6495A9FEB2FBQ30494134-FD828B46-7349-4880-ABC8-EE90EDDF7785Q34361921-C0398F3F-CC00-4552-BFC5-94331DAB7FB2Q34520490-27F66D3A-BBCD-45F1-A8AE-8542F432E31DQ35649535-E8D4DD22-79F4-4522-8436-E065AEAFB5B4Q35750313-C4154D4E-2A65-464D-B483-73AC64E64FD4Q35951013-F2CBF422-3B17-49B7-91AD-2E4FCC285BDAQ36458301-F6B3E921-A3F5-4D3E-A991-080EAA42A4BFQ36522581-BEEDE783-4164-40B7-97A6-249D241B9127Q36680392-3BCFDE74-3967-4D84-BBFB-7237D9051359Q37224816-F74802EA-3A64-4AD1-9F9B-3242252EFEFAQ37399759-95A89E5C-57A3-4263-BB43-41F548E6FE95Q38573837-D1EDF627-4DE6-433C-9834-3D4D4390A6D0Q39068831-9D92B4D6-B0F5-458F-B568-811638329B81Q39685066-3078AB85-394F-432E-90AB-BFF0696F0CDAQ39871258-26E8601A-7AA3-4D61-991B-A2DE957226CCQ39872937-0085C29D-D906-4085-9814-63A206340484Q39877750-77AA0DA9-C6AE-4DF0-8AF7-40F01BE70133Q39877755-3B59CA93-B85D-4094-9A99-E9DD00FC6041Q39879435-D199E8D0-745E-4141-B471-DACBBF013C5EQ41002380-614D8E0A-90C4-4E9C-8153-EE42BF7854BAQ42142685-3BDC69C1-8894-4443-8373-627837263C17Q42787771-A79EEF16-B94F-40E9-BEDF-999DA396B0C4
P2860
Sequential interactions of structural proteins in phage phi 29 procapsid assembly.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Sequential interactions of structural proteins in phage phi 29 procapsid assembly.
@en
Sequential interactions of structural proteins in phage phi 29 procapsid assembly.
@nl
type
label
Sequential interactions of structural proteins in phage phi 29 procapsid assembly.
@en
Sequential interactions of structural proteins in phage phi 29 procapsid assembly.
@nl
prefLabel
Sequential interactions of structural proteins in phage phi 29 procapsid assembly.
@en
Sequential interactions of structural proteins in phage phi 29 procapsid assembly.
@nl
P2860
P1433
P1476
Sequential interactions of structural proteins in phage phi 29 procapsid assembly
@en
P2860
P304
P407
P577
1995-08-01T00:00:00Z