Domain Architecture of a High Mobility Group A-type Bacterial Transcriptional Factor

Domain Architecture of a Bacterial HMGA-like Protein DOMAIN ARCHITECTURE OF AN HMGA-TYPE BACTERIAL TRANSCRIPTIONAL FACTOR*

the investigation of the relationship between type a and type b personalities and quality of translation

چکیده ندارد.

High mobility group proteins of amphibian oocytes: a large storage pool of a soluble high mobility group-1-like protein and involvement in transcriptional events

Oocytes of several amphibian species (Xenopus laevis, Rana temporaria, and Pleurodeles waltlii) contained a relatively large pool of nonchromatin-bound, soluble high mobility group (HMG) protein with properties similar to those of calf thymus proteins HMG-1 and HMG-2 (protein HMG-A; A, amphibian). About half of this soluble HMG-A was located in the nuclear sap, the other half was recovered in e...

High-mobility group A1 proteins inhibit expression of nucleotide excision repair factor xeroderma pigmentosum group A.

Cells that overexpress high-mobility group A1 (HMGA1) proteins exhibit deficient nucleotide excision repair (NER) after exposure to DNA-damaging agents, a condition ameliorated by artificially lowering intracellular levels of these nonhistone proteins. One possible mechanism for this NER inhibition is down-regulation of proteins involved in NER, such as xeroderma pigmentosum complimentation gro...

SEPARATION OF NONHISTONE HIGH MOBILITY GROUP (HMG) FROM HUMAN LYMPHOCYTES BY HIGH PERFORMANCE LIQUID CHROMATOGRAPHY

The high mobility group (HMG) of nonhistone proteins have been investigated using two high performance liquid chromatographic techniques (HPLC). Reversed-phase HPLC under conditions of 50 mM triethylamine adjusted to pH 2.2 with phosphoric acid (solvent A) and 95% acetonitrile in water (solvent B) was used to separate proteins primarily on the basis of differences in the overall hydrophobi...