scispace - formally typeset
J

John Hempel

Researcher at University of Pittsburgh

Publications -  52
Citations -  2470

John Hempel is an academic researcher from University of Pittsburgh. The author has contributed to research in topics: Aldehyde dehydrogenase & Dehydrogenase. The author has an hindex of 25, co-authored 52 publications receiving 2366 citations.

Papers
More filters
Journal ArticleDOI

The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold.

TL;DR: Sequence comparisons of the class 3 ALDH with other ALDHs indicate a similar polypeptide fold, novel NAD-binding mode and catalytic site for this family, and a mechanism for enzymatic specificity and activity is postulated.
Journal ArticleDOI

Relationships within the aldehyde dehydrogenase extended family.

TL;DR: Phylogenetic analysis of these aldehyde dehydrogenase‐related sequences indicates at least 13 ALDH families, most of which have previously been identified but not grouped separately by alignment, which cluster into seven sequence motifs conserved in almost all ALDHs.
Journal ArticleDOI

Aldehyde dehydrogenases: Widespread structural and functional diversity within a shared framework

TL;DR: Sequences of 16 NAD and/or NADP‐linked aldehyde oxidoreductases are aligned, including representative examples of all alde Hyde dehydrogenase forms with wide substrate preferences as well as additional types with distinct specificities for certain metabolic aldehydes.
Journal ArticleDOI

Characterization of an alarm pheromone secreted by amphibian tadpoles that induces behavioral inhibition and suppression of the neuroendocrine stress axis.

TL;DR: It is shown that an alarm pheromone is produced by ranid tadpole skin cells, is released into the medium via an active secretory process upon predator attack, and signals predator presence to conspecifics, and a neuroendocrine mechanism is provided by which the behavioral inhibition caused by exposure to the alarms is maintained until the threat subsides.
Journal ArticleDOI

Structural transitions during bacteriophage HK97 head assembly.

TL;DR: Using the mobility shift in agarose gel to monitor expansion and SDS/gel electrophoresis to monitor cross-linking in vitro, it is found that expansion precedes and is required for cross-Linking, and it is proposed that expansion triggers the cross- linking reaction.