About: Rapid protein-folding assay using green fluorescent protein

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в липні 1999 (uk) im Juli 1999 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q56902199-CE7A9520-53E0-4A88-AC6D-003EF9406B30
publication date	1999-07-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q56902199-BDD69398-57CB-4522-94AD-E0D39069C09B
language of work or name	English
exact match	wds:Q56902199-52C85C05-8C57-44F7-A840-77035383A9B6
exact match	https://scigraph.springernature.com/pub.10.1038/10904
cites work	wds:Q56902199-01990330-17DE-41D6-B22B-37A03302F6D9 wds:Q56902199-0BFCBCD6-2716-46DD-8ECC-06A3D705AB9D wds:Q56902199-0C1ECC85-1828-499B-ACFA-40D018D961D9 wds:Q56902199-12BC5CC3-E77C-43CA-8CBA-98AB2C0B4F3F wds:Q56902199-1BE96C18-9DBA-4018-9643-8F7A20179BA2 wds:Q56902199-203D37CF-7FE9-486D-A3FA-E1FD8822DB70 wds:Q56902199-212D3A46-291F-4C01-9918-4AD653DCEC10 wds:Q56902199-2E51A1FA-7CA4-4A84-B724-0D2C82812786 wds:Q56902199-36C27332-C6EE-44AD-8297-D28D338BDAAB wds:Q56902199-3C299093-C052-4CB4-A361-948AF4C14D89 wds:Q56902199-445D979A-42CD-4CB3-B70B-E75E06936833 wds:Q56902199-569366F3-4A53-4DCF-BCC5-75A79A04712F wds:Q56902199-78B024C1-BA62-40EF-8F8F-33C6D265187A wds:Q56902199-80305D6D-DA2D-4F90-B8D7-D166F120872A wds:Q56902199-99EC560A-FA29-4462-BF7C-72241F6E10D1 wds:Q56902199-A1C8D5E5-B1F4-4621-A4AC-8F2D0A7292BD wds:Q56902199-A40E7CB5-74D4-4AAB-8276-A4C58D180917 wds:Q56902199-ACD45C0F-2231-42E3-86B1-CA90602CFF5E wds:Q56902199-C77FB78A-8F21-4C48-8561-BF33E7B62387 wds:Q56902199-E8A308BA-9139-404F-B75B-23EC774B78EF wds:Q56902199-EA752514-AABE-43A2-BA5A-4D2671E0D312 wds:Q56902199-F882059E-8C5F-40C1-9A06-AE0D05FEDC64 wds:Q56902199-FA02AF43-2F4E-4969-BAB7-2C2940A916F3 wds:Q56902199-FF970124-4CF9-4B68-B3F9-725A226BA90C
cites work	Chromophore formation in green fluorescent protein. Loop mutations can cause a substantial conformational change in the carboxy terminus of the ferritin protein Expression of an antibody fragment at high levels in the bacterial cytoplasm. Antibody scFv fragments without disulfide bonds made by molecular evolution Optimization of DNA shuffling for high fidelity recombination Rapid evolution of a protein in vitro by DNA shuffling Principles that govern the folding of protein chains The ferritins: molecular properties, iron storage function and cellular regulation Wavelength mutations and posttranslational autoxidation of green fluorescent protein A fosmid-based genomic map and identification of 474 genes of the hyperthermophilic archaeon Pyrobaculum aerophilum Contact order, transition state placement and the refolding rates of single domain proteins. Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein FACS-optimized mutants of the green fluorescent protein (GFP) Redesigning enzyme topology by directed evolution Improved green fluorescent protein by molecular evolution using DNA shuffling. Cotranslational protein folding In vitro synthesis of protein in microbial systems Improved green fluorescence Class-directed structure determination: foundation for a protein structure initiative Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates. Expression of eukaryotic proteins in soluble form in Escherichia coli Chaperonin-mediated folding of green fluorescent protein. Directed evolution: Creating biocatalysts for the future In vivo characterization of mutants of the bacteriophage f1 gene V protein isolated by saturation mutagenesis
author name string	wds:Q56902199-78E4717A-E702-4AF7-ACFE-A4A2B0DBBDC0 wds:Q56902199-7BE318D7-4069-443D-AF2F-38EB0DC8C222 wds:Q56902199-DE303324-7ABF-4AAD-A562-DCFECC20438C wds:Q56902199-F6E7FBD7-4E6B-48F4-A74C-984F16530A54
author name string	J Berendzen T C Terwilliger G S Waldo B M Standish
rdfs:label	Rapid protein-folding assay using green fluorescent protein (en) Rapid protein-folding assay using green fluorescent protein (nl)
skos:prefLabel	Rapid protein-folding assay using green fluorescent protein (en) Rapid protein-folding assay using green fluorescent protein (nl)
name	Rapid protein-folding assay using green fluorescent protein (en) Rapid protein-folding assay using green fluorescent protein (nl)
title	wds:Q56902199-DA8B580C-96BD-4899-A304-D9AAA06088E2
title	Rapid protein-folding assay using green fluorescent protein (en)
page(s)	wds:Q56902199-3029517B-0875-4A23-9817-E0680EB55E43
page(s)	691-5
instance of	wds:Q56902199-861523E7-CCB7-4F37-A2AA-CD5CC551FB5A
instance of	scholarly article
main subject	wds:Q56902199-FD16A24E-3560-40E2-B8A6-9D800FE71C0D
main subject	protein folding
PubMed ID	wds:Q56902199-45B0DF88-3E68-40B6-BEE3-80065ED6EEF2
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10404163
PubMed ID	10404163
published in	wds:Q56902199-15B09BDD-DF5D-443C-BA02-EEFFC53BFEC9
published in	Nature Biotechnology
issue	wds:Q56902199-28FA5F47-2BE1-4998-A02B-B28E95E51FBE
volume	wds:Q56902199-806A6CA8-EE70-4947-AB2B-D966C5C644E0
issue	7
volume	17
DOI	wds:Q56902199-D3683A22-34B9-4FE8-B36A-5AAA8028C4E7
DOI	http://dx.doi.org/10.1038/10904
DOI	10.1038/10904
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q56902199
is cites work of	Rapid topology mapping of Escherichia coli inner-membrane proteins by prediction and PhoA/GFP fusion analysis Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein Structural proteomics: prospects for high throughput sample preparation Rapid determination of protein stability and ligand binding by differential scanning fluorimetry of GFP-tagged proteins Directed evolution of ATP binding proteins from a zinc finger domain by using mRNA display Development of a molecularly evolved, highly sensitive CaMKII FRET sensor with improved expression pattern Rapid in vitro protein synthesis pipeline: a promising tool for cost-effective protein array design.

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