Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli. - Wikidata - awgldk - TriplyDB

Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli.

Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli.

http://www.wikidata.org/entity/Q37536158

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Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons Adaptation of bird hemoglobins to high altitudes: demonstration of molecular mechanism by protein engineering Development of recombinant hemoglobin-based oxygen carriers A recombinant polymeric hemoglobin with conformational, functional, and physiological characteristics of an in vivo O2 transporter Isolated dystrophin molecules as seen by electron microscopy Ubiquitin fusion augments the yield of cloned gene products in Escherichia coli.Expression of fully functional tetrameric human hemoglobin in Escherichia coli Factor Xa subsite mapping by proteome-derived peptide libraries improved using WebPICS, a resource for proteomic identification of cleavage sites.Cysteines beta93 and beta112 as probes of conformational and functional events at the human hemoglobin subunit interfaces.High-level expression of sperm whale myoglobin in Escherichia coli The N-terminal peptide of mammalian GTP cyclohydrolase I is an autoinhibitory control element and contributes to binding the allosteric regulatory protein GFRP.Hemoglobin βCys93 is essential for cardiovascular function and integrated response to hypoxia.Recent advances in the development of haemoglobin-based blood substitutes.Analysis of specific binding involved in genomic packaging of the double-stranded-RNA bacteriophage phi6.Identification of the putative RNA polymerase of Cryphonectria hypovirus in a solubilized replication complex.Strategies for achieving high-level expression of genes in Escherichia coli.Biochemical characterization of the Drosophila dpp protein, a member of the transforming growth factor beta family of growth factors Role of reticuloendotheliosis virus envelope glycoprotein in superinfection interference.Spleen necrosis virus gag polyprotein is necessary for particle assembly and release but not for proteolytic processing Fish hemoglobins.S-nitrosylation of beta-arrestin regulates beta-adrenergic receptor trafficking.Autoxidation and oxygen binding properties of recombinant hemoglobins with substitutions at the αVal-62 or βVal-67 position of the distal heme pocket Hemoglobin S-nitrosylation plays an essential role in cardioprotection.Antigenicity of recombinant maltose binding protein-Mycobacterium avium subsp. paratuberculosis fusion proteins with and without factor Xa cleaving.Enhanced polymerization of recombinant human deoxyhemoglobin beta 6 Glu----Ile.Purification and characterization of the bacteriophage P4 delta protein.Protein engineering. The design, synthesis and characterization of factitious proteins.The purification of eukaryotic polypeptides synthesized in Escherichia coli.Sp1-mediated transcriptional activation is repressed by Sp3 Kinetic and spectroscopic properties of the cyanide complexes of ferrous haemoglobins I and IV from trout blood.Properties of a recombinant human hemoglobin double mutant: sickle hemoglobin with Leu-88(beta) at the primary aggregation site substituted by Ala.Chloroplast envelope protein encoded by chloroplast genome.Polymerization and solubility of recombinant hemoglobins alpha 2 beta 2 (6Val) (Hb S) and alpha 2 beta 2(6Leu) (Hb Leu).Conformational changes in hemoglobin S (betaE6V) imposed by mutation of the beta Glu7-beta Lys132 salt bridge and detected by UV resonance Raman spectroscopy.Haemoglobin alpha 2 beta 2 23Val----Ile produced in Escherichia coli facilitates Hb S polymerization.Pharmacologic Targeting of Red Blood Cells to Improve Tissue Oxygenation.The cytoplasmic localization of the catalytic site of CSLF6 supports a channeling model for the biosynthesis of mixed-linkage glucan.Overproduction of alpha chains provides a proton-insensitive component to the bluefish hemoglobin system.Membrane transport piece by piece: production of transmembrane peptides for structural and functional studies.Tetrameric hemoglobin expressed in Escherichia coli. Evidence of heterogeneous subunit assembly.

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P2860

Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli.

http://www.wikidata.org/entity/Q37536158

description

1985 nî lūn-bûn

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1985年の論文

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1985年学术文章

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1985年学术文章

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1985年学术文章

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1985年学术文章

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1985年学术文章

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1985年學術文章

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1985年學術文章

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1985年學術文章

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name

Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli.

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Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli.

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type

label

Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli.

@en

Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli.

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Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli.

@en

Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli.

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Proceedings of the National Academy of Sciences of the United States of America

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Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli.

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P2860

The crystal structure of human deoxyhaemoglobin at 1.74 A resolution

The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers

X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin

Cloning, expression in Escherichia coli, and reconstitution of human myoglobin.

Structure and function of haemoglobin.

Regulation of oxygen affinity of hemoglobin: influence of structure of the globin on the heme iron.

Hemoglobin Abruzzo (beta143 (H21) His replaced by Arg). Consequences of altering the 2,3-diphosphoglycerate binding site.

Role of the alpha-amino groups of the alpha and beta chains of human hemoglobin in oxygen-linked binding of carbon dioxide.

Synthesis in yeast of a functional oxidation-resistant mutant of human alpha-antitrypsin.

Resonance Raman evidence for cleavage of the Fe-N epsilon(His-F8) bond in the alpha subunit of the T-structure nitrosylhemoglobin.

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