about
L13a blocks 48S assembly: role of a general initiation factor in mRNA-specific translational controlNucleic acid chaperons: a theory of an RNA-assisted protein foldingDecoding mechanisms by which silent codon changes influence protein biogenesis and functionTwo heme-binding domains of heme-regulated eukaryotic initiation factor-2alpha kinase. N terminus and kinase insertionDirectionality in protein fold prediction.Ribosomes containing mutants of L4 ribosomal protein from Thermus thermophilus display multiple defects in ribosomal functions and sensitivity against erythromycin.Cell-free immunology: construction and in vitro expression of a PCR-based library encoding a single-chain antibody repertoire.Protein folding by domain V of Escherichia coli 23S rRNA: specificity of RNA-protein interactionsThe role of alpha-hemoglobin stabilizing protein in redox chemistry, denaturation, and hemoglobin assembly.A new class of repression modules is critical for heme regulation of the yeast transcriptional activator Hap1.Ribosome release factor RF4 and termination factor RF3 are involved in dissociation of peptidyl-tRNA from the ribosome.Role of α-globin H helix in the building of tetrameric human hemoglobin: interaction with α-hemoglobin stabilizing protein (AHSP) and heme moleculeBirth, life and death of nascent polypeptide chains.AHSP (α-haemoglobin-stabilizing protein) stabilizes apo-α-haemoglobin in a partially folded stateRegulation of protein synthesis by the heme-regulated eIF2alpha kinase: relevance to anemias.Tritium planigraphy: from the accessible surface to the spatial structure of a protein.Mechanistic Insight into the Reactivation of BCAII Enzyme from Denatured and Molten Globule States by Eukaryotic Ribosomes and Domain V rRNAsComputational evidence that fast translation speed can increase the probability of cotranslational protein folding.The Proteomic Code: a molecular recognition code for proteins.Synonymous mutations and ribosome stalling can lead to altered folding pathways and distinct minima.Chaperoning erythropoiesis.Folding of proteins with a flavodoxin-like architecture.A mutation that improves soluble recombinant hemoglobin accumulation in Escherichia coli in heme excess.Stabilization of apoglobin by low temperature increases yield of soluble recombinant hemoglobin in Escherichia coli.Processing mutations located throughout the human multidrug resistance P-glycoprotein disrupt interactions between the nucleotide binding domains.Cotranslational protein folding.Indications that "codon boundaries" are physico-chemically defined and that protein-folding information is contained in the redundant exon bases.Effective cotranslational folding of firefly luciferase without chaperones of the Hsp70 family.The potential role of cell penetrating peptides in the intracellular delivery of proteins for therapy of erythroid related disorders.Using SecM arrest sequence as a tool to isolate ribosome bound polypeptides.His92 and His110 selectively affect different heme centers of adrenal cytochrome b(561).Unraveling co-translational protein folding: Concepts and methods.A newly synthesized, ribosome-bound polypeptide chain adopts conformations dissimilar from early in vitro refolding intermediates.Co-translational protein targeting facilitates centrosomal recruitment of PCNT during centrosome maturation in vertebrates.Homogeneous stalled ribosome nascent chain complexes produced in vivo or in vitro.Co-translational Folding of an Eukaryotic Multidomain Protein in a Prokaryotic Translation System
P2860
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P2860
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Cotranslational folding of globin.
@en
type
label
Cotranslational folding of globin.
@en
prefLabel
Cotranslational folding of globin.
@en
P2093
P2860
P356
P1476
Cotranslational folding of globin.
@en
P2093
Krasheninnikov IA
P2860
P304
10646-10651
P356
10.1074/JBC.272.16.10646
P407
P577
1997-04-01T00:00:00Z