Laboratory evolution of fast-folding green fluorescent protein using secretory pathway quality control.
about
Genetically encoded green fluorescent Ca2+ indicators with improved detectability for neuronal Ca2+ signalsDirected evolution of bright mutants of an oxygen-independent flavin-binding fluorescent protein from Pseudomonas putidaDevelopment of cysteine-free fluorescent proteins for the oxidative environmentRestoring methicillin-resistant Staphylococcus aureus susceptibility to β-lactam antibioticsDirected evolution of Mycobacterium tuberculosis β-lactamase reveals gatekeeper residue that regulates antibiotic resistance and catalytic efficiencyFutile protein folding cycles in the ER are terminated by the unfolded protein O-mannosylation pathway.Commitment to lysogeny is preceded by a prolonged period of sensitivity to the late lytic regulator Q in bacteriophage λ.Optimizing recombinant antibodies for intracellular function using hitchhiker-mediated survival selectionProduction of secretory and extracellular N-linked glycoproteins in Escherichia coli.Construction of improved tools for protein localization studies in Streptococcus pneumoniaeCharacterization of flavin-based fluorescent proteins: an emerging class of fluorescent reportersSuperfolder GFP is fluorescent in oxidizing environments when targeted via the Sec transloconCharacterization of a novel small molecule that potentiates β-lactam activity against gram-positive and gram-negative pathogens.Using superfolder green fluorescent protein for periplasmic protein localization studies.Characterization of camel nanobodies specific for superfolder GFP fusion proteins.Spatial fluctuations in expression of the heterocyst differentiation regulatory gene hetR in Anabaena filamentsEfficient expression of codon-adapted affinity tagged super folder green fluorescent protein for synchronous protein localization and affinity purification studies in Tetrahymena thermophila.MreC and MreD Proteins Are Not Required for Growth of Staphylococcus aureus.SMC condensation centers in Bacillus subtilis are dynamic structuresFluorescent proteins for live-cell imaging with super-resolution.Engineered fluorescent proteins illuminate the bacterial periplasmIlluminating Messengers: An Update and Outlook on RNA Visualization in Bacteria.A rapid protein folding assay for the bacterial periplasm.Differential localization of LTA synthesis proteins and their interaction with the cell division machinery in Staphylococcus aureus.A dual reporter system for detecting RNA interactions in bacterial cells.Broad host range vectors for expression of proteins with (Twin-) Strep-tag, His-tag and engineered, export optimized yellow fluorescent protein.Genetically encoded fluorescent tags.Characterization of Annexin V Fusion with the Superfolder GFP in Liposomes Binding and Apoptosis Detection.Optimizing heterologous protein production in the periplasm of E. coli by regulating gene expression levels.Experimental evolution of a green fluorescent protein composed of 19 unique amino acids without tryptophan.Expression in E. coli and purification of the fibrillogenic fusion proteins TTR-sfGFP and β2M-sfGFP.Staphylococcus aureus requires at least one FtsK/SpoIIIE protein for correct chromosome segregation.Characterization of Split Fluorescent Protein Variants and Quantitative Analyses of Their Self-Assembly Process.
P2860
Q21133806-33846323-9344-4C2C-BDE7-6EE6136BAD31Q21202060-00162FE5-4AA9-4C64-B931-161E6A83E591Q27302354-7182B29E-5102-4617-AA5F-7206D482B820Q27678160-566D0C5A-D59F-408D-92B5-DBA57979B64DQ27679915-BF95EF22-1853-49AD-B385-4B5590FEC78CQ27932449-3821EAFB-A026-4652-AB9C-85D68566DA6BQ34297864-6D0D0145-D7E6-4BA7-B10F-5A1836BA5562Q34313188-1EA78E71-B9E7-4C6E-9625-70B9E8CE58FDQ34528682-02D728F8-61A4-474F-BC81-2728DCFDBC9EQ34563609-DFDDBA19-B444-4DFD-A012-911378FA83F6Q34760785-B5764674-F081-418C-891B-665360007876Q34816912-B0B92478-9C1C-45B9-82CF-17D3A873BB13Q35169071-9C3B7C70-EDB4-4250-9B90-09378A008E83Q35192447-68E5AE47-7AF4-4095-8AD1-960FFCE6FDC1Q35217452-B6796BD1-EA90-4DEF-A43B-6C7E4010DFEAQ35242778-E664ECA3-4390-496E-9971-677F19A0DADEQ35607508-05347D9D-4874-43E2-BEC0-7C15715B25E5Q35808886-380D8B9B-A4A3-4CDE-B972-6C032162ADE8Q36833104-2CDC205E-CBE3-417B-B378-604138209C40Q38140622-03F76F7C-020F-4943-9555-D344F3F733F5Q38201033-856503DA-AE4B-49B9-854D-BE10ACDD5A5FQ39424515-1205389C-1E58-4BE0-BE52-42AF7550FD51Q40497455-3636B55A-6461-4285-AA87-A2A975F64E9DQ40948901-5B426820-6A5F-4F64-8941-72E8E04753F3Q41682984-49FFCEBB-9FE0-4076-A208-79112338D0CBQ42151670-BAF414A1-77F3-4678-8707-6EDDF57FB7DFQ42213757-B7622DAB-29EF-47B5-8017-591A86F3E05EQ42256585-3BA4EE06-22AC-4BB4-8DC1-177F0732CAF4Q43220567-2245BAFA-5981-46C8-B8C1-8E55D7D67E21Q44331574-16F4235A-E37E-47A2-A3A8-D2B6CD164452Q50510800-EF5E8BB4-C877-4EC6-9055-F492D8212101Q51304032-6F69A304-D327-4738-96D6-FF0D6C1FD84FQ55197845-F899EEEC-E92B-430D-ACFB-79B6FFE75986
P2860
Laboratory evolution of fast-folding green fluorescent protein using secretory pathway quality control.
description
2008 nî lūn-bûn
@nan
2008 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Laboratory evolution of fast-f ...... etory pathway quality control.
@ast
Laboratory evolution of fast-f ...... etory pathway quality control.
@en
type
label
Laboratory evolution of fast-f ...... etory pathway quality control.
@ast
Laboratory evolution of fast-f ...... etory pathway quality control.
@en
prefLabel
Laboratory evolution of fast-f ...... etory pathway quality control.
@ast
Laboratory evolution of fast-f ...... etory pathway quality control.
@en
P2860
P921
P1433
P1476
Laboratory evolution of fast-f ...... etory pathway quality control.
@en
P2093
Adam C Fisher
P2860
P356
10.1371/JOURNAL.PONE.0002351
P407
P577
2008-06-11T00:00:00Z