Cleavage of head and tail proteins during bacteriophage T5 assembly: selective host involvement in the cleavage of a tail protein.
about
Assembly of both the head and tail of bacteriophage Mu is blocked in Escherichia coli groEL and groES mutants.Bacteriophage-encoded cochaperonins can substitute for Escherichia coli's essential GroES proteinControl of src kinase activity by activators, inhibitors, and substrate chaperones.Identification of a groES-like chaperonin in mitochondria that facilitates protein folding.Identification of a host protein necessary for bacteriophage morphogenesis (the groE gene product)A single-ring mitochondrial chaperonin (Hsp60-Hsp10) can substitute for GroEL-GroES in vivo.Head length control in T4 bacteriophage morphogenesis: effect of canavanine on assembly.The T-odd bacteriophages.In vitro assembly of the T=13 procapsid of bacteriophage T5 with its scaffolding domain.Genomic, proteomic and physiological characterization of a T5-like bacteriophage for control of Shiga toxin-producing Escherichia coli O157:H7.Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis.Characterization of the Heat Shock Response in Lactococcus lactis subsp. lactis.Sequence analysis and phenotypic characterization of groEL mutations that block lambda and T4 bacteriophage growth.The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures.Effect of bacteriophage lambda infection on synthesis of groE protein and other Escherichia coli proteins.Evidence that the two Escherichia coli groE morphogenetic gene products interact in vivo.Identity of the B56.5 protein, the A-protein, and the groE gene product of Escherichia coli.Identification of the heat-inducible protein C15.4 as the groES gene product in Escherichia coli.Correct Assembly of the Bacteriophage T5 Procapsid Requires Both the Maturation Protease and the Portal ComplexStructural aberrations in T-even bacteriophage. V. Effects of canavanine on the maturation and utilization of specific gene products.Morphogenesis of bacteriophage phi29 of Bacillus subtilis: cleavage and assembly of the neck appendage protein.Bacteriophage SPO1 structure and morphogenesis. III. SPO1 proteins and synthesis.Identification of a mammalian 10-kDa heat shock protein, a mitochondrial chaperonin 10 homologue essential for assisted folding of trimeric ornithine transcarbamoylase in vitroMechanisms of genome propagation and helper exploitation by satellite phage P4.Interactions of bacteriophage and host macromolecules in the growth of bacteriophage lambda.Protein fusion: a novel reaction in bacteriophage lambda head assembly.Phage T5 straight tail fiber is a multifunctional protein acting as a tape measure and carrying fusogenic and muralytic activities.Spinach chloroplast cpn21 co-chaperonin possesses two functional domains fused together in a toroidal structure and exhibits nucleotide-dependent binding to plastid chaperonin 60.In vivo and in vitro function of GroEL mutants with impaired allosteric properties.Novel chaperonins are prevalent in the virioplankton and demonstrate links to viral biology and ecologyStructural aberrations in group A Staphylococcus bacteriophagesHead morphogenesis of complex double-stranded deoxyribonucleic acid bacteriophages.A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12.Molecular cloning, sequencing, and transcriptional analysis of the groESL operon from Bacillus stearothermophilusA survey of the heat shock response in four Streptomyces species reveals two groEL-like genes and three groEL-like proteins in Streptomyces albus.Characterization of the groEL-like genes in Streptomyces albus.Genetic suppression of a temperature-sensitive groES mutation by an altered subunit of RNA polymerase of Escherichia coli K-12Participation of Escherichia coli K-12 groE gene products in the synthesis of cellular DNA and RNA.Cloning and expression of the ltf gene of bacteriophage T5.Irreversible binding to the receptor of bacteriophages T5 and BF23 does not occur with the tip of the tail.
P2860
Q33725398-3C59D171-9783-4FBB-B8D4-857851E000CFQ33758153-411E428D-B373-46F5-A72C-30B3B0CA76E4Q33789721-B710FE4E-4BEB-45E9-8DE1-C9E0891DCE6FQ33825821-A7A77D49-C77D-4782-BEC1-39C0AEBF0E93Q33954194-6BE854A7-3327-43A6-A108-61C0FEC52EC0Q33993039-8486967D-7BCF-4E40-96DC-14B925335C30Q34071656-BB2E904F-F3EE-4A9F-A0EF-D85932C4BA55Q34078616-AD4A60D1-D01D-40B5-AD63-9118494F02DAQ34120093-D6A54AED-2265-40BB-80B9-FC62D9DC343FQ34238595-71ACE882-92C3-49D7-8E31-659B496EDE7EQ35326913-66578D41-AADB-47F5-8047-4FB675448DB8Q35691975-20961DFA-C0D8-48D1-9F8C-182204BEC012Q35908833-4BA5AEAE-C35F-4738-BB5C-D2F7A54218A2Q36174913-2C8AF9DE-21C8-4D3A-9A9F-C26D1128FC95Q36310650-7D81DFFC-837A-4C7A-A1BB-EC15B15CF7F1Q36310729-FC08C73D-34DE-4B87-A3ED-571366B39304Q36323625-2E4DF267-AF56-4A68-B244-3E84344A6D2CQ36331021-86525CF2-12AB-40B9-A5B8-F6E4BECAF74CQ36535193-FC5B4527-EBDB-4B7A-A47F-0144D45BB06DQ36561238-7D9B8D91-514A-4086-A52D-B1CCCFFF7F21Q36568446-B243C688-9BF3-4EE6-AE50-EC58644E4833Q36905451-08AD452D-E7AE-48A4-BCBA-27D24DED4A9BQ36952262-6AE4DF6D-8792-4E55-89F8-00E32C81D548Q37059637-7E202046-6359-424D-93E4-9C752F121F66Q37066576-30A2F79C-D5BD-4B1B-87AE-BA4B95606344Q37440265-9BC91CCA-3D69-4A58-92FA-6B82F81E12A3Q38292602-FE857A7D-03BB-4E81-BE9E-20491460527CQ38295580-2596A3F8-CE3C-48F0-8D7A-6C7AF39D7625Q38308570-9D92A4A3-0338-46E2-9255-69DB4DD5CF44Q38668214-77F2657B-B643-4F8A-BF4F-A2F545767A7CQ39769619-4EC544BD-0496-4D89-8DD9-0CDAE489F48FQ39778286-EF225CE8-6F52-4A0C-B06B-9D459C9A7502Q39899055-46FC1BE6-9AB9-43F6-B7EF-7E6F88E18612Q39928096-C2E7A31A-F8BB-4CCC-B821-DA4AEF01F52BQ39946461-9F3DB8D7-D95F-45ED-A89F-B9EF81E2F296Q39946467-AF052527-A39F-4BB4-9B62-C857862308EDQ39956040-51883504-DE44-4EB5-87BC-B34F248EC42EQ39967869-CB9A4199-E832-43E4-B887-C562282FE29AQ39970325-570760AB-4E0A-4ADF-BF2E-1267B258B778Q39980052-A1B5ADC6-5E88-4137-984F-7E8893B53D1B
P2860
Cleavage of head and tail proteins during bacteriophage T5 assembly: selective host involvement in the cleavage of a tail protein.
description
1973 nî lūn-bûn
@nan
1973 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1973 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1973年の論文
@ja
1973年論文
@yue
1973年論文
@zh-hant
1973年論文
@zh-hk
1973年論文
@zh-mo
1973年論文
@zh-tw
1973年论文
@wuu
name
Cleavage of head and tail prot ...... he cleavage of a tail protein.
@ast
Cleavage of head and tail prot ...... he cleavage of a tail protein.
@en
Cleavage of head and tail prot ...... he cleavage of a tail protein.
@nl
type
label
Cleavage of head and tail prot ...... he cleavage of a tail protein.
@ast
Cleavage of head and tail prot ...... he cleavage of a tail protein.
@en
Cleavage of head and tail prot ...... he cleavage of a tail protein.
@nl
prefLabel
Cleavage of head and tail prot ...... he cleavage of a tail protein.
@ast
Cleavage of head and tail prot ...... he cleavage of a tail protein.
@en
Cleavage of head and tail prot ...... he cleavage of a tail protein.
@nl
P1476
Cleavage of head and tail prot ...... he cleavage of a tail protein.
@en
P2093
P304
P356
10.1016/0022-2836(73)90418-X
P407
P577
1973-11-01T00:00:00Z