Biomedical subjects

P Scherer

Publications and source records attributed to P Scherer.

At least 19 recordsLinked to original sources

PubMed1997

Alternate finger tapping test in patients with migraine.

Migraine patients are thought to show some cognitive dysfunction and slight structural abnormalities in the white matter of the brain, whereas most patients with multiple sclerosis (MS) are known to have numerous white matter lesions, often affecting the corpus callosum. To demonstrate psychomotor dysfunction, an alternate finger tapping task (a-FTT) on a PC was administered to controls (n = 41), migraine patients (n = 25), and multiple sclerosis patients (n = 22). Five MS patients with secondary callosal atrophy detected by MRI were also investigated as a separate group. Significant slowing was demonstrated in migraine (P = 0.0005) and MS (P<0.0001). The poorest test results were found in patients with callosal atrophy. In summary, a-FTT on a PC is able to detect minimal psychomotor dysfunction in migraine.

Adolescent↗

PubMed1995

Cloning and characterization of a murine SIL gene.

The human SIL gene is disrupted by a site-specific interstitial deletion in 25% of children with T-cell acute lymphoblastic leukemia. Since transcriptionally active genes are prone to recombination events, the recurrent nature of this lesion suggests that the SIL gene product is transcriptionally active in the cell type that undergoes this interstitial deletion and that the SIL gene product may play a role in normal lymphoid development. To facilitate studies of SIL gene function, we have cloned and characterized a murine SIL gene. The predicted murine SIL protein is 75% identical to the human gene, with good homology throughout the open reading frame. An in vitro translated SIL cDNA generated a protein slightly larger than the predicted 139-kDa protein. Although a prior report detected SIL mRNA expression exclusively in hematopoietic tissues, a sensitive RT-PCR assay demonstrated SIL expression to be ubiquitous, detectable in all tissues examined. Since the RT-PCR assay suggested that SIL mRNA expression was higher in rapidly proliferating tissues, we assayed SIL mRNA expression using a murine erythroleukemia model of terminal differentiation and found it to be dramatically decreased in conjunction with terminal differentiation. These studies demonstrate that the human SIL gene product is quite well conserved in rodents and suggest that the SIL gene product may play a role in cell proliferation.

Base Sequence↗

PubMed1994

Wound healing and wound management: focus on debridement. An interdisciplinary round table, September 18, 1992, Jackson Hole, WY.

A multidisciplinary panel of experts convened to discuss the basic concepts of prevention and treatment of pressure ulcers. Special emphasis was placed on four types of debridement: mechanical, surgical, autolystic, and enzymatic. Debridement of burns was also discussed. Team management by informed practitioners is vital to successful wound care and all treatments should be based on a holistic appraisal of patients and their individualized plans of care.

Debridement↗

PubMed1993

Protein import into yeast mitochondria: the inner membrane import site protein ISP45 is the MPI1 gene product.

Protein import across both mitochondrial membranes is mediated by the cooperation of two distinct protein transport systems, one in the outer and the other in the inner membrane. Previously we described a 45 kDa yeast mitochondrial inner membrane protein (ISP45) that can be cross-linked to a partially translocated precursor protein (Scherer et al., 1992). We have now purified ISP45 to homogeneity and identified it as the product of the nuclear MPI1 gene. Identity of ISP45 with the MPI1 gene product was shown by microsequencing of three tryptic ISP45 peptides and by demonstrating that an antibody against an Mpi1p-beta-galactosidase fusion protein specifically recognizes ISP45. Antibodies monospecific for ISP45 inhibited protein import into right-side-out mitochondrial inner membrane vesicles, but not into intact mitochondria. On solubilizing mitochondria, ISP45 was rapidly converted to a 40 kDa proteolytic fragment unless mitochondria were first denatured with trichloroacetic acid. The combined genetic and biochemical evidence identifies ISP45/Mpi1p as a component of the protein import system of the yeast mitochondrial inner membrane.

Amino Acid Sequence↗

PubMed1991

Quantum eigenvalues from classical periodic orbits.

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Journal Article↗

PubMed1991

Inner membrane protease I, an enzyme mediating intramitochondrial protein sorting in yeast.

Several precursors transported from the cytoplasm to the intermembrane space of yeast mitochondria are first cleaved by the MAS-encoded protease in the matrix space and then by additional proteases that have not been characterized. We have now developed a specific assay for one of these other proteases. The enzyme is an integral protein of the inner membrane; it requires divalent cations and acidic phospholipid for activity, and is defective in yeast mutant pet ts2858 which accumulates an incompletely processed cytochrome b2 precursor. The protease contains a 21.4 kd subunit whose C-terminal part is exposed on the outer face of the inner membrane. An antibody against this polypeptide inhibits the activity of the protease. As overproduction of the polypeptide does not increase the activity of the protease in mitochondria, the enzyme may be a hetero-oligomer. This 'inner membrane protease I' shares several key features with the leader peptidase of Escherichia coli and the signal peptidase of the endoplasmic reticulum.

Amino Acid Sequence↗

PubMed1990