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Biomedical subjects

J W Fox

Publications and source records attributed to J W Fox.

140 records · Page 8Linked to original sources
PubMed1976

The fan flap: an adjunct to ear reconstruction.

The development of a fan-shaped flap of temporal myo-fascia and cranial periosteum for use in construction or reconstruction of the external ear is described. This adjunct to ear reconstruction decreases the incidence of exposure of the framework and does not add operative steps. The flap adds pleasing bulk to the helix while maintaining the delicate contours of the framework. Since we have been using this flap, we have had no early or late exposures of these frameworks.

Child, Preschool↗
PubMedDate not supplied

Raman studies on bradykinin and a cyclic bradykinin.

Laser Raman spectra of bradykinin in water, deuterium oxide, and the solid phase were recorded. From the spectra it was concluded that bradykinin conformation is comprised of ordered and unordered structure. The ordered structure appears to be some form of reverse turn. Furthermore, it seems that there is an enhancement of the turn structure in the solid phase. A cyclic cystine containing analog of bradykinin was also examined with Raman spectroscopy. The cyclic bradykinin analog gives a Raman spectrum very similar to that of the linear bradykinin and therefore must share similar conformational forms with bradykinin. The restrictive Cys-Cys disulfide in the cyclic bradykinin must serve to maintain a conformation acceptable to bradykinin receptors since the cyclic peptide exhibits biological activity.

Bradykinin↗
PubMedDate not supplied

Snake venom metalloproteinases: structure, function and relationship to the ADAMs family of proteins.

A large number of zinc metalloproteinases of varying mol. wts and biological functions has been isolated from crotalid and viperid venoms. Over the past few years, structural studies on these proteinases have suggested their organization into four classes, P-I to P-IV. These proteinases are synthesized in the venom gland as zymogens which are subsequently processed to the active form. The signal and pro-sequences of the proteins are highly conserved. Within the pro-domain lies a consensus sequence which probably functions in a manner similar to the cysteine switch in mammalian collagenases. The proteinase domain is represented by two forms: a two-disulfide and a three-disulfide structure. Crystallographic and modeling studies suggest that the two forms share very similar tertiary structures. The larger venom metalloproteinases (P-II, III and IV) have additional domains on the carboxy side of the proteinase domain. The additional domains that have been identified include disintegrin and disintegrin-like domains, a high-cysteine domain and a lectin-binding domain. It appears that these non-enzymatic domains function to modulate the biological properties of the proteinases. Recently, a family of homologues of the venom zinc metalloproteinases has been described from a variety of organisms including mammals, reptiles and invertebrates. This family of proteins has been termed the ADAMs, for A Disintegrin-like And Metalloproteinase-containing protein. They differ from the venom proteinases in that some of them may not have proteolytic activity. In addition to the domain structure described for the P-III class of venom proteins, the ADAMs have an epidermal growth factor-like domain, a transmembrane domain and a cytoplasmic domain. A description of venom metalloproteinase structure will be outlined in this review, along with the similarities and differences among the venom proteins and the ADAMs family of proteins.

Amino Acid Sequence↗