Isolation and characterization of a beta-lactamase-inhibitory protein from Streptomyces clavuligerus and cloning and analysis of the corresponding gene
about
Three decades of beta-lactamase inhibitorsStructural Basis of Outer Membrane Protein Biogenesis in BacteriaAnalysis of the Binding Forces Driving the Tight Interactions between -Lactamase Inhibitory Protein-II (BLIP-II) and Class A -LactamasesWeighted protein residue networks based on joint recurrences between residuesDesign of generic biosensors based on green fluorescent proteins with allosteric sites by directed evolution.New beta -lactamase inhibitory protein (BLIP-I) from Streptomyces exfoliatus SMF19 and its roles on the morphological differentiation.Design of potent beta-lactamase inhibitors by phage display of beta-lactamase inhibitory protein.Display of functional beta-lactamase inhibitory protein on the surface of M13 bacteriophage.Fine mapping of the sequence requirements for binding of beta-lactamase inhibitory protein (BLIP) to TEM-1 beta-lactamase using a genetic screen for BLIP function.Identification and characterization of beta-lactamase inhibitor protein-II (BLIP-II) interactions with beta-lactamases using phage display.Investigation of the Streptomyces clavuligerus cephamycin C gene cluster and its regulation by the CcaR protein.Identification of a β-lactamase inhibitory protein variant that is a potent inhibitor of Staphylococcus PC1 β-lactamase.Genes specific for the biosynthesis of clavam metabolites antipodal to clavulanic acid are clustered with the gene for clavaminate synthase 1 in Streptomyces clavuligerusUse of periplasmic target protein capture for phage display engineering of tight-binding protein-protein interactions.The complex extracellular biology of Streptomyces.Molecular analysis of a beta-lactam resistance gene encoded within the cephamycin gene cluster of Streptomyces clavuligerus.Characteristics of beta-lactamase-inhibiting proteins from Streptomyces exfoliatus SMF19Heterologous expression and secretion of a Streptomyces scabies esterase in Streptomyces lividans and Escherichia coliSystematic substitutions at BLIP position 50 result in changes in binding specificity for class A β-lactamases.Identification of the β-lactamase inhibitor protein-II (BLIP-II) interface residues essential for binding affinity and specificity for class A β-lactamasesTranscriptomic analysis of Streptomyces clavuligerus ΔccaR::tsr: effects of the cephamycin C-clavulanic acid cluster regulator CcaR on global regulation.Avoidance of suicide in antibiotic-producing microbes.Identification of residues in beta-lactamase critical for binding beta-lactamase inhibitory protein.Contributions of aspartate 49 and phenylalanine 142 residues of a tight binding inhibitory protein of beta-lactamases.Binding properties of a peptide derived from beta-lactamase inhibitory protein.Characterization of a novel, antifungal, chitin-binding protein from Streptomyces tendae Tü901 that interferes with growth polarity.THz frequency spectrum of protein-solvent interaction energy using a recurrence plot-based Wiener-Khinchin method.Resistance to beta-lactamase inhibitor protein does not parallel resistance to clavulanic acid in TEM beta-lactamase mutants.CcaR is an autoregulatory protein that binds to the ccaR and cefD-cmcI promoters of the cephamycin C-clavulanic acid cluster in Streptomyces clavuligerus.A regulatory gene (ccaR) required for cephamycin and clavulanic acid production in Streptomyces clavuligerus: amplification results in overproduction of both beta-lactam compounds.The bla gene of the cephamycin cluster of Streptomyces clavuligerus encodes a class A beta-lactamase of low enzymatic activity.Engineering Specificity from Broad to Narrow: Design of a β-Lactamase Inhibitory Protein (BLIP) Variant That Exclusively Binds and Detects KPC β-Lactamase.Genes for a beta-lactamase, a penicillin-binding protein and a transmembrane protein are clustered with the cephamycin biosynthetic genes in Nocardia lactamduransBLIP-II is a highly potent inhibitor of Klebsiella pneumoniae carbapenemase (KPC-2).A novel chimeric peptide with antimicrobial activity.Role of β-lactamase residues in a common interface for binding the structurally unrelated inhibitory proteins BLIP and BLIP-II.Determinants of binding affinity and specificity for the interaction of TEM-1 and SME-1 beta-lactamase with beta-lactamase inhibitory protein.Dissecting the protein-protein interface between beta-lactamase inhibitory protein and class A beta-lactamases.Detecting transitions in protein dynamics using a recurrence quantification analysis based bootstrap method.The adaptive nature of protein residue networks.
P2860
Q24646623-3DD0650D-1803-4001-8054-80510A1827C8Q27667873-8037D6F2-AA8F-4D04-8CCE-B327D015762DQ27670891-F50F1ECD-1701-4162-A7B6-9DFE5144C352Q30374934-F73A177E-BE98-4186-9779-DD345274C718Q30733665-D7AD5FB4-AA82-43EA-8622-45646BCE87C1Q30854268-3A0076D3-7EE0-474C-9891-1901A0091DF3Q30854317-00C21815-69A5-4D5C-822E-955C1218A3C1Q31984838-C30D7F31-FE34-47C7-9432-5FEE11724AB8Q33434215-4BB644B1-E1A8-4B49-B924-1408A607F86AQ33544102-6F351A9F-91EB-4356-B953-A85E76FA9DB2Q33735488-ACBC4844-66BC-4CFF-8387-D22411F3697FQ33794586-E222E8B8-7CF1-4555-B70F-99F51586739CQ33976323-430B40D5-CFAB-4194-A0A0-7668A68E93C5Q34013420-4143C836-F9D7-40A9-8189-6A7C4D057F9CQ34093836-76B6EA08-B595-4FFA-A643-34C198457820Q35615686-C9D3AA64-3FA0-45F6-842A-015801550949Q36053574-F345EE75-5ED8-4FF3-992D-77A743EB5F61Q36110815-2D58E9AF-6D9E-4C36-9C7A-697E1AC0D643Q36298671-00C37EB0-14D1-4346-BDD7-CCEF8E01AB51Q36928945-85F6C294-17A8-459B-8FF7-65A2C9D2FA40Q37710756-FDEB862B-5057-4B8F-BEE4-408473099B0BQ37743270-6E96990D-A555-4DD5-8A5A-1D3F6B002A4EQ38327464-2E8CEE70-5D06-46FC-95FD-E5DE24ADC52FQ38329362-3B3C116F-507A-49D5-99E6-12C3658068F9Q39479019-3DFA4D72-954A-40A2-8C2C-321DC415FF73Q39498095-D04C4B30-F1A0-4406-A9AD-F44BD6279612Q39644236-7255AC05-1CE0-4590-8F40-A7B0821F6590Q39657859-AD4382DD-525B-44E1-9106-BC3E003D7C62Q39679130-A355E1FA-354E-4F06-891D-D0F96DBCC88AQ39844989-10CEA56A-FEC3-4264-B062-29FE9417BDC0Q39847342-C87FB0F5-AC25-4AB2-8504-5165FF4E41A6Q40532268-2E83BCBE-60B5-4E97-98D9-7443734204DFQ40871998-240C4F7F-5468-4438-A4B4-A02A6AEB7D16Q41440519-66EC3603-DAD4-453B-B96D-515960032F02Q41537062-AF179F40-788C-4FE7-90E0-D9C3B51E051FQ42550799-BFC9CF19-1048-4EEB-ABE3-31296ED167AFQ44559371-5FC02309-AAAC-4FED-84DC-0DACC708E157Q45000448-BE163A7B-B4E6-4D94-8737-8AD49B4388CFQ47134706-491E768B-83AF-4153-A4DE-AD565B1907DDQ48268370-12DEFBE5-AC8C-408C-A132-846BCC84110E
P2860
Isolation and characterization of a beta-lactamase-inhibitory protein from Streptomyces clavuligerus and cloning and analysis of the corresponding gene
description
1990 nî lūn-bûn
@nan
1990 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Isolation and characterization ...... ysis of the corresponding gene
@ast
Isolation and characterization ...... ysis of the corresponding gene
@en
Isolation and characterization ...... ysis of the corresponding gene
@nl
type
label
Isolation and characterization ...... ysis of the corresponding gene
@ast
Isolation and characterization ...... ysis of the corresponding gene
@en
Isolation and characterization ...... ysis of the corresponding gene
@nl
prefLabel
Isolation and characterization ...... ysis of the corresponding gene
@ast
Isolation and characterization ...... ysis of the corresponding gene
@en
Isolation and characterization ...... ysis of the corresponding gene
@nl
P2093
P2860
P1476
Isolation and characterization ...... ysis of the corresponding gene
@en
P2093
B K Leskiw
S Aippersbach
S E Jensen
P2860
P304
P356
10.1128/JB.172.9.4909-4918.1990
P407
P577
1990-09-01T00:00:00Z