Zobrazeno 1 - 7
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pro vyhledávání: '"P V, Haydock"'
Publikováno v:
The Journal of biological chemistry. 267(33)
Filaggrin is an intermediate filament-associated protein which functions to aggregate keratin intermediate filaments in the stratum corneum of mammalian epidermis. It is synthesized as a large precursor protein, profilaggrin, that consists of multipl
Publikováno v:
Journal of Biological Chemistry. 260:16383-16394
Trp repressor of Escherichia coli K-12 is a dimeric protein (monomer size, 108 amino acids) that acquires high affinity for certain operator targets in double-stranded DNA upon interaction with L-tryptophan. High titer antiserum directed against E. c
Autor:
P V Haydock, B A Dale
Publikováno v:
Journal of Biological Chemistry. 261:12520-12525
Filaggrin is the histidine-rich basic protein that aggregates keratin filaments in fully differentiated cells of the epidermis. Filaggrin is synthesized in the granular cell layer as a high molecular weight precursor protein (profilaggrin) that consi
Publikováno v:
Journal of molecular biology. 170(4)
The interaction of Trp repressor protein with partial trp operators was studied in vitro and in vivo. At high ratios of protein to DNA, Trp holorepressor formed stable complexes with DNA molecules containing half operators. When plasmids conferring t
Publikováno v:
Journal of bacteriology. 153(2)
Escherichia coli cells harboring a non-attenuated trp-lac operon fusion were used to evaluate the effects of indolmycin on the initiation of transcription at the trp promoter. Indolmycin caused repression in trpR+ strains and in trpR deletion mutants
Autor:
P V, Haydock, B A, Dale
Publikováno v:
The Journal of biological chemistry. 261(27)
Filaggrin is the histidine-rich basic protein that aggregates keratin filaments in fully differentiated cells of the epidermis. Filaggrin is synthesized in the granular cell layer as a high molecular weight precursor protein (profilaggrin) that consi
Publikováno v:
The Journal of biological chemistry. 260(30)
Trp repressor of Escherichia coli K-12 is a dimeric protein (monomer size, 108 amino acids) that acquires high affinity for certain operator targets in double-stranded DNA upon interaction with L-tryptophan. High titer antiserum directed against E. c