Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations.
about
Condensation of FtsZ filaments can drive bacterial cell division.In the beginning, Escherichia coli assembled the proto-ring: an initial phase of divisionSlow polymerization of Mycobacterium tuberculosis FtsZIdentification of the SlmA active site responsible for blocking bacterial cytokinetic ring assembly over the chromosomeMycobacterium tuberculosis ClpX interacts with FtsZ and interferes with FtsZ assemblyA metabolic sensor governing cell size in bacteriaLarge ring polymers align FtsZ polymers for normal septum formationA moonlighting enzyme links Escherichia coli cell size with central metabolismA flexible C-terminal linker is required for proper FtsZ assembly in vitro and cytokinetic ring formation in vivoSimple modeling of FtsZ polymers on flat and curved surfaces: correlation with experimental in vitro observations.Nucleotide-dependent conformations of FtsZ dimers and force generation observed through molecular dynamics simulations.In vivo organization of the FtsZ-ring by ZapA and ZapB revealed by quantitative super-resolution microscopyCytokinesis in bacteriaSB-RA-2001 inhibits bacterial proliferation by targeting FtsZ assembly.Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinCDesign, synthesis and evaluation of novel 2,5,6-trisubstituted benzimidazoles targeting FtsZ as antitubercular agents.Novel trisubstituted benzimidazoles, targeting Mtb FtsZ, as a new class of antitubercular agents.Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils.The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization.The pH dependence of polymerization and bundling by the essential bacterial cytoskeletal protein FtsZGTP-dependent heteropolymer formation and bundling of chloroplast FtsZ1 and FtsZ2.Assembly dynamics of the bacterial cell division protein FTSZ: poised at the edge of stabilityAssembly of an FtsZ mutant deficient in GTPase activity has implications for FtsZ assembly and the role of the Z ring in cell divisionZipA binds to FtsZ with high affinity and enhances the stability of FtsZ protofilaments.Drug discovery targeting cell division proteins, microtubules and FtsZ.Imaging-based identification of a critical regulator of FtsZ protofilament curvature in Caulobacter.A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus.SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over Chromosomes in E. coli.Glutamate 83 and arginine 85 of helix H3 bend are key residues for FtsZ polymerization, GTPase activity and cellular viability of Escherichia coli: lateral mutations affect FtsZ polymerization and E. coli viability.Direct observation of the enhancement of noncooperative protein self-assembly by macromolecular crowding: indefinite linear self-association of bacterial cell division protein FtsZ.Adenine nucleotide-dependent regulation of assembly of bacterial tubulin-like FtsZ by a hypermorph of bacterial actin-like FtsA.The Kil peptide of bacteriophage λ blocks Escherichia coli cytokinesis via ZipA-dependent inhibition of FtsZ assemblyPhysics of bacterial morphogenesis.Cytoplasmic Domain of MscS Interacts with Cell Division Protein FtsZ: A Possible Non-Channel Function of the Mechanosensitive Channel in Escherichia Coli.The Cell Division Protein FtsZ from Streptococcus pneumoniae Exhibits a GTPase Activity Delay.Mutations in the bacterial cell division protein FtsZ highlight the role of GTP binding and longitudinal subunit interactions in assembly and function.NDK Interacts with FtsZ and Converts GDP to GTP to Trigger FtsZ Polymerisation--A Novel Role for NDKExtreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins.Studies on the dissociation and urea-induced unfolding of FtsZ support the dimer nucleus polymerization mechanism.Characterization of Caulobacter crescentus FtsZ protein using dynamic light scattering
P2860
Q24646706-C7F9E7A3-A807-48CF-8DA5-9BC2801F9A22Q27694716-7E647CEB-4E97-413A-9609-878EA93602CEQ28344388-C07DD8AD-1C5A-425E-951D-E0742F684347Q28486179-2EBCEC40-6484-4CB1-AA0C-619C63C5728CQ28487426-05093E59-A218-4FC1-9B18-63228A35858AQ28488934-26A2BC30-17DE-43A3-B14C-0FD5DB6DA9E2Q28489014-CC1BB559-E1A1-4870-B38B-7AE30082F8FFQ28534852-B16EC1B3-FC2F-42C3-ACD9-6D5EFB2D1C01Q28679156-9157B016-424F-493A-B1EA-E250F758CBF2Q30491638-7742B1F6-745B-42AC-9517-8BDF480E2D50Q30519199-154EBF17-3799-417A-A35F-11FCF258B768Q30565381-F9D30839-1BB5-4298-96E9-10C2D1D7F4B4Q33186319-BEADDD61-6432-472C-BAD7-764AB9FBD66EQ33609157-7EEE4BC6-59BF-48D1-8C82-05852D4AF2A0Q33658863-C1DCAFAB-8418-4F0B-B88A-59D54C2BDDFDQ33711825-A1151B81-E9F0-4E7E-AB65-0F9CD6675D17Q33761632-22C4D0CD-85E5-46DE-A3DD-7C815677EF10Q33837672-5AA53A85-DA6E-4257-8F21-8E6D6A5FEEB8Q33884803-20D5C2A8-5056-41DA-87CA-66F89E3E3073Q33954519-94227590-EF74-421D-BCE8-6F62F3ECAB95Q33966926-8807FBA7-128B-48BE-9AEC-C2E33AA0E381Q33972949-9F970CBF-099D-427E-973B-F149AD6F8BBCQ33997241-2532E497-D2EA-449D-B13E-359056C38801Q34099117-55A8836B-383A-44E4-96AC-3E02EEFE1129Q34143487-720744C0-C87A-44E2-B413-A4303D87AC31Q34155531-0C372717-AB01-4084-8139-FA17E01A5A09Q34188556-CD72F203-DE93-4E28-95E4-373D40811D92Q34421472-40232C62-8A29-4E4D-AAAE-DCB32B52CA97Q34577628-05691548-BA14-44E5-A955-A344157938BDQ34706788-B72E5CA9-3FBB-4F9D-A92C-B6FEF8B6E2F6Q34964917-E2C96300-583F-4575-95DD-29678F45E073Q35126034-3506B2A8-2114-4B91-8DFB-EB8898C15901Q35598316-4E6BDF3B-F8A7-402A-96FE-864E5485A312Q35634455-56B3A42D-D2F0-473D-AC79-09C79B828E5FQ35761881-07080C87-55C1-4C05-B420-A0E2C6DEDD55Q35805434-48BFBF44-D01C-453C-9696-4134450C1FB5Q35859134-6F39661A-BF86-49A5-8036-715B8DF9D201Q35879448-9234B991-55B3-47D3-A5CD-04F42DF4F54EQ35926214-6A3CEF7F-1818-4AF7-A1EE-D51ED03ED9F5Q36078863-7D21C2A1-2A5E-4D47-BCBF-D437D660C158
P2860
Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations.
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Analysis of FtsZ assembly by l ...... ole of divalent metal cations.
@ast
Analysis of FtsZ assembly by l ...... ole of divalent metal cations.
@en
type
label
Analysis of FtsZ assembly by l ...... ole of divalent metal cations.
@ast
Analysis of FtsZ assembly by l ...... ole of divalent metal cations.
@en
prefLabel
Analysis of FtsZ assembly by l ...... ole of divalent metal cations.
@ast
Analysis of FtsZ assembly by l ...... ole of divalent metal cations.
@en
P2860
P1476
Analysis of FtsZ assembly by l ...... role of divalent metal cations
@en
P2093
A Mukherjee
J Lutkenhaus
P2860
P304
P407
P577
1999-02-01T00:00:00Z