Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry. - Wikidata - awgldk - TriplyDB

Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry.

Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry.

http://www.wikidata.org/entity/Q36483177

about

Analyzing the molecular mechanism of lipoprotein localization in Brucella Structure and function of BamE within the outer membrane and the β-barrel assembly machine The Crystal Structure of BamB Suggests Interactions with BamA and Its Role within the BAM Complex Structural Basis of Outer Membrane Protein Biogenesis in Bacteria High-resolution structure of a new crystal form of BamA POTRA4–5 fromEscherichia coli Crystal Structure of BamB from Pseudomonas aeruginosa and Functional Evaluation of Its Conserved Structural Features Structure of Escherichia coli BamB and its interaction with POTRA domains of BamA Structural basis for the interaction of BamB with the POTRA3-4 domains of BamA Reversal of the ΔdegP phenotypes by a novel rpoE allele of Escherichia coli The β-barrel assembly machinery in motion.Flexibility in the Periplasmic Domain of BamA Is Important for Function.Mitochondrial-bacterial hybrids of BamA/Tob55 suggest variable requirements for the membrane integration of β-barrel proteins.Structural snapshots of the β-barrel assembly machinery.Dynamic periplasmic chaperone reservoir facilitates biogenesis of outer membrane proteins.BamA POTRA Domain Interacts with a Native Lipid Membrane Surface Classifying β-Barrel Assembly Substrates by Manipulating Essential Bam Complex Members.Outer membrane protein biogenesis in Gram-negative bacteria Crystal structure of BamB bound to a periplasmic domain fragment of BamA, the central component of the β-barrel assembly machine In vivo roles of BamA, BamB and BamD in the biogenesis of BamA, a core protein of the β-barrel assembly machine of Escherichia coli.The activity and specificity of the outer membrane protein chaperone SurA are modulated by a proline isomerase domain.Predicting functionally informative mutations in Escherichia coli BamA using evolutionary covariance analysis.Deciphering the roles of BamB and its interaction with BamA in outer membrane biogenesis, T3SS expression and virulence in Salmonella SurA is involved in the targeting to the outer membrane of a Tat signal sequence-anchored protein.Conserved residues of the putative L6 loop of Escherichia coli BamA play a critical role in the assembly of β-barrel outer membrane proteins, including that of BamA itself A peptide based on homologous sequences of the β-barrel assembly machinery component BamD potentiates antibiotic susceptibility of Pseudomonas aeruginosa.The bacterial outer membrane β-barrel assembly machinery.Genetic, biochemical, and molecular characterization of the polypeptide transport-associated domain of Escherichia coli BamA.Making a beta-barrel: assembly of outer membrane proteins in Gram-negative bacteria.Assembly of the β-Barrel Outer Membrane Proteins in Gram-Negative Bacteria, Mitochondria, and Chloroplasts.Assembly of Outer Membrane β-Barrel Proteins: the Bam Complex.Substitutions in the BamA β-barrel domain overcome the conditional lethal phenotype of a ΔbamB ΔbamE strain of Escherichia coli The Bam machine: a molecular cooper.The fimbrial usher FimD follows the SurA-BamB pathway for its assembly in the outer membrane of Escherichia coli Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain.Crystallization and preliminary X-ray data collection of the Escherichia coli lipoproteins BamC, BamD and BamE Dissection of β-barrel outer membrane protein assembly pathways through characterizing BamA POTRA 1 mutants of Escherichia coli.Involvement and necessity of the Cpx regulon in the event of aberrant beta-barrel outer membrane protein assembly.A modular BAM complex in the outer membrane of the alpha-proteobacterium Caulobacter crescentus.Borrelia burgdorferi locus BB0795 encodes a BamA orthologue required for growth and efficient localization of outer membrane proteins The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane {beta}-barrel proteins in Caulobacter crescentus.

P2860

Q27003985-71EDAD53-B3EB-4EE6-9A79-ED33A70732E7 Q27666508-9F11B9C5-B048-4AD3-BBBD-BA9592C09AFF Q27666768-DDF08E80-8462-4905-96AC-715D2F2F98F1 Q27667873-E6C8245C-19B4-4385-9389-E83FD2DEA61F Q27671054-0CD4B5BF-92CE-4133-BD0F-D90F73555D30 Q27675288-920ADAE7-58BC-437B-92E5-80C1B6AEA968 Q27682136-127855BF-2A7C-4BB1-AD6F-45B7F0BB8760 Q27704054-BED8E8EA-AE85-4523-874C-B80332D05A74 Q28731266-49816338-D3E7-449F-8B11-85641D6015A7 Q30152662-501EF204-3C63-4CCF-BD4D-476B5DE3C690 Q30152683-AEEA46BE-896D-461C-85A6-E01A7D946EED Q30152684-4FF54A91-11EC-4973-BFC5-1F945CE529D3 Q30152701-736F030A-66F0-4748-BD52-FF14ADCA006C Q30152747-E5D11A1F-1FF0-486D-B262-85102959F3E3 Q30152768-5D4D003D-C06C-4802-9D20-97B7733E11B5 Q30152788-8C5E7784-A9D2-4DD4-9062-FE8E17F96C84 Q30152824-C744979E-FF03-46C1-931B-604050B0D46A Q30153283-B0503650-CD96-4FC0-830E-E766A72D98D4 Q30153401-9C4CAC7C-A402-43E2-A250-D52489190C71 Q30153532-8413465C-2EAF-4C69-A3E2-9E053EB96D46 Q30153535-51BF4690-23D5-470E-877E-4121B877353D Q30155183-EB79D499-9F73-4345-944F-FBCDF1D5A3E5 Q30155235-290E524E-F2C4-4789-84FD-1CDE8F72244B Q30155278-CB45D553-7910-44B1-AC32-3141A66547BE Q30155308-1AC4A887-C28D-4707-BD5F-CA716080C569 Q30155322-023125B6-565D-4BAA-BC90-0C4D4153C442 Q30155324-678BA47A-6D70-4CE7-BE19-4DF70B7B96F6 Q30155397-48FA0EA2-6E67-466D-BB3A-EED4EE46EBE2 Q30155403-25F3AE23-145B-4EAC-AD5C-66CE51AADA7E Q30155422-4BA13D21-EB12-47FB-8C72-3F6D85F9166A Q30155441-9034BA16-E371-4FF4-A64C-CBC23CA20B2A Q30155481-E7185FC6-D4D9-4ECF-916C-F0F236E4DB9A Q30155510-3DA18560-67FF-48B6-92EA-F46D68B308E6 Q30155536-BE8488FB-2DC8-4775-A72F-64E352923BAE Q30155933-9B3F6119-4A4D-425E-AEC1-FDBF5F65F9DB Q30156805-9526D6D0-A2EB-4817-BD82-D9672D3667F4 Q30156852-767A2201-836B-453C-87D5-4B69ACF1F5BE Q30156997-A20D81BC-370C-4597-BF91-40F180C71D6D Q30157011-ABC0BCA4-938E-4CCF-B291-73BE039593CB Q30157034-F86B9BBA-478C-4BC8-A7E5-193A2C92FDE0

P2860

Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry.

http://www.wikidata.org/entity/Q36483177

description

2007 nî lūn-bûn

@nan

2007年の論文

@ja

2007年学术文章

@wuu

2007年学术文章

@zh-cn

2007年学术文章

@zh-hans

2007年学术文章

@zh-my

2007年学术文章

@zh-sg

2007年學術文章

@yue

2007年學術文章

@zh

2007年學術文章

@zh-hant

name

Analysis of YfgL and YaeT inte ...... mutagenesis, and biochemistry.

@ast

Analysis of YfgL and YaeT inte ...... mutagenesis, and biochemistry.

@en

type

label

Analysis of YfgL and YaeT inte ...... mutagenesis, and biochemistry.

@ast

Analysis of YfgL and YaeT inte ...... mutagenesis, and biochemistry.

@en

prefLabel

Analysis of YfgL and YaeT inte ...... mutagenesis, and biochemistry.

@ast

Analysis of YfgL and YaeT inte ...... mutagenesis, and biochemistry.

@en

P1433

Q36483177-BA76DA0D-1B7B-4CF9-858C-03338F57B9C1

P1476

Q36483177-8CD081CB-0E98-4DC7-B87B-73B9E276E8B5

P2093

Q36483177-1AFCD7F6-7152-4BF7-BF48-344CAB3FF436

Q36483177-23931FCD-9A8B-4B78-B216-EB18FCF02EA2

Q36483177-27E39A6B-FBF0-4F25-9DA5-9C28C84C0235

Q36483177-77B6966F-EFCA-420C-BD14-CCA47915B9D2

Q36483177-BAD956F9-FC24-4D7B-9D4C-93114477D6CE

P2860

Q36483177-0014ACDF-5199-4278-9251-892C6BD48802

Q36483177-00983FF1-F904-418B-B965-F3D4294E7B86

Q36483177-05BCEDB5-6D73-4A0A-BFC7-3EAC34E80C5A

Q36483177-0927A258-FC65-4679-9353-8D037F91F2AC

Q36483177-09782064-F47C-4501-A43E-CDA7FC5B7E6A

Q36483177-21043772-0E19-447F-80F6-0FA2E64B65AF

Q36483177-254C303E-A80D-43D7-AE4B-2B02123FD09B

Q36483177-30293DA6-5E6A-458C-9D55-FEAFFD3DF32E

Q36483177-41D13341-AE40-4618-82D2-DF6BAC2DA80C

Q36483177-4597B3AB-05AA-46EF-996E-E7069B7DC680

P304

Q36483177-EA3D5670-459B-4902-89C2-6EB6AE62DE6E

P31

Q36483177-FBC0424F-5028-46EB-BB82-53C9401464DD

P356

Q36483177-927E691F-AD80-4FC1-8D28-F15B65C54C59

P407

Q36483177-C56B0DBF-4520-4CF9-BA23-94E989EB3E0F

P433

Q36483177-5FD9225D-CB14-4A3F-8229-F322B2244DC1

P478

Q36483177-EC443373-F98E-4784-9394-9FC6FCE428B2

P577

Q36483177-70CCC344-3CAA-445C-8A93-0FB6434110ED

P698

Q36483177-776028CA-B440-46D9-9DD4-18F81023E168

P921

Q36483177-31F5A542-AF17-4D62-9470-268F69065E73

P932

Q36483177-84781523-09A0-4990-AFEB-092F63CD4C61

P356

P1433

Journal of Bacteriology

P1476

Analysis of YfgL and YaeT inte ...... mutagenesis, and biochemistry.

@en

P2093

Danielle Frost

http://www.w3.org/2001/XMLSchema#string

Drew Bennion

http://www.w3.org/2001/XMLSchema#string

Jeremy Mantei

http://www.w3.org/2001/XMLSchema#string

Phu Vuong

http://www.w3.org/2001/XMLSchema#string

Rajeev Misra

http://www.w3.org/2001/XMLSchema#string

P2860

ExPASy: The proteomics server for in-depth protein knowledge and analysis

Multiple sequence alignment with the Clustal series of programs

Structure and function of an essential component of the outer membrane protein assembly machine

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

Role of a highly conserved bacterial protein in outer membrane protein assembly

SMART 4.0: towards genomic data integration

The complete general secretory pathway in gram-negative bacteria

Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli.

The N-terminal domain of Tob55 has a receptor-like function in the biogenesis of mitochondrial beta-barrel proteins.

Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif.

P304

1507-1517

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1128/JB.01477-07

http://www.w3.org/2001/XMLSchema#string

P407

P433

5

http://www.w3.org/2001/XMLSchema#string

P478

190

http://www.w3.org/2001/XMLSchema#string

P577

2007-12-28T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

18165306

http://www.w3.org/2001/XMLSchema#string

P921

P932

2258660

http://www.w3.org/2001/XMLSchema#string