Tryptophan

heat shock protein family D (Hsp60) member 1 ; Homo sapiens







13 Article(s)
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Title
Pub. Year
#Total Relationships
1 34845604 Purification and Handling of the Chaperonin GroEL. 2022 1
2 14734563 Stopped-flow fluorescence analysis of the conformational changes in the GroEL apical domain: relationships between movements in the apical domain and the quaternary structure of GroEL. 2004 Apr 16 1
3 15123431 Phi value analysis of an allosteric transition of GroEL based on a single-pathway model. 2004 May 21 2
4 12614617 Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy. 2003 Mar 14 1
5 10404227 GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism. 1999 Jul 1
6 10543958 A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL. 1999 Oct 29 1
7 9585518 Transient kinetic analysis of adenosine 5'-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL. 1998 May 19 1
8 9686605 Homogeneous Escherichia coli chaperonin 60 induces IL-1 beta and IL-6 gene expression in human monocytes by a mechanism independent of protein conformation. 1998 Aug 1 4
9 8810258 Nucleotides reveal polynucleotide phosphorylase activity from conventionally purified GroEL. 1996 Oct 11 1
10 8943246 Intrinsic fluorescence studies of the chaperonin GroEL containing single Tyr --> Trp replacements reveal ligand-induced conformational changes. 1996 Dec 13 2
11 7737993 Reversal by GroES of the GroEL preference from hydrophobic amino acids toward hydrophilic amino acids. 1995 May 5 1
12 8096465 A comment on: 'The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60): evidence for the presence of a single tryptophan', by N.C. Price, S.M. Kelly, S. Wood and A. auf der Mauer (1991) FEBS Lett. 292, 9-12. 1993 Mar 29 2
13 1360012 Characterization of a stable, reactivatable complex between chaperonin 60 and mitochondrial rhodanese. 1992 Dec 5 1