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Biomedical subjects

T A Brown

Publications and source records attributed to T A Brown.

6 recordsLinked to original sources
PubMed1992

Comorbidity among anxiety disorders: implications for treatment and DSM-IV.

Research on comorbidity among psychological disorders is relatively new. Yet, comorbidity data have fundamental significance for classification and treatment. This significance is particularly apparent in the anxiety disorders, which, prior to DSM-III-R, were subsumed under disorders considered more significant (e.g., psychotic and depressive disorders). After considering definitional, methodological, and theoretical issues of comorbidity, data on comorbidity among the anxiety disorders are reviewed as well as data on comorbidity of anxiety disorders with the depressive, personality, and substance use disorders. Treatment implications are presented with preliminary data on the effects of psychosocial treatment of panic disorder on co-morbid generalized anxiety disorder. Implications of comorbidity for research on the nature of psychopathology and the ultimate integration of dimensional and categorical features in our nosology are considered.

Anxiety Disorders↗
PubMed1992

Specificities of protein-protein and protein-DNA interaction of GABP alpha and two newly defined ets-related proteins.

The ets-related protein GABP alpha interacts with the four ankyrin-type (ANK) repeats of GABP beta to form a high-affinity DNA-binding complex that recognizes a site important for herpes simplex virus type I immediate early gene activation. To investigate the selectivity and specificity of the GABP complex, we have isolated two new ETS family members, termed ER81 and ER71. ER81 and GABP alpha were present in most tissues of adult mice, whereas ER71 was restricted to testis. We have compared the DNA-binding specificities of these proteins by binding site selection. GABP alpha, ER71, and ER81 recognized the common pentanucleotide DNA sequence 5'-CGGAA/T-3'. Although subtle differences were observed for nucleotide preferences flanking this pentanucleotide core, the overall similarity of the selected sequences was most striking. Given the observation that GABP alpha interaction with GABP beta requires its intact ETS domain, we further compared the ability of GABP beta to interact with other ETS proteins. GABP beta did not augment the DNA-binding activity of the highly similar ETS domains of ER81, ER71, or Ets-1. Moreover, probing of total tissue extracts with radiolabeled GABP beta demonstrated its exceedingly stringent specificity for GABP alpha. Given that the DNA-binding specificities of these ETS proteins are similar and that the protein-protein interactions between GABP beta and GABP alpha are highly specific, we conclude that the protein interactions determine the target site selection by GABP alpha.

Amino Acid Sequence↗
PubMed1979

Chemical, immunochemical, and structural studies of the cross-reactive antigens of Streptococcus mutans AHT and B13.

Two antigenic polysaccharides were extracted from cell walls of the cross-reactive strains Streptococcus mutans AHT (a) and S. mutans B13 (d). The antigens extracted from walls by the hot formamide method, were purified by affinity chromatography on columns containing the galactose-specific lectin from the castor bean and were found to be diheteroglycans consisting of galactose and glucose. Antigenic specificities of both the serotype-specific and the cross-reactive sites on each polymer were studied: the AHT (a) antigen is determined by D-galactose linked 1 leads to 6 to adjacent sugar, the B13 (d) antigen is determined by D-glucose similarly linked to o its neighbor, and the cross-reactive (a--d) site present on both polymers consists of D-galactose linked 1 leads to 6 to a subterminal sugar moiety. Methylation analysis revealed structural similarities between the purified polysaccharides that may reflect the nature of the cross-reactive sites and differences that may reflect the natures of the specific haptenic regions. Based on these studies, a partial hypothetical structural model is proposed.

Antigens, Bacterial↗