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At least 325 records · Page 18Linked to original sources
PubMed1996

[Detection of perfusion of kidney transplants. Comparison between color-coded and amplitude-coded Doppler ultrasound].

OBJECTIVE: To evaluate the efficiency of colour Doppler energy (CDE) in comparison to conventional colour Doppler sonography (CDI) in the detection of renal blood flow signals in asymptomatic patients after renal transplantation. SUBJECTS AND METHODS: Fifteen asymptomatic volunteer patients after renal transplantation were examined with CDI and CDE. The examination parameters were kept constant; only the Doppler-receiver gain was varied. Assessment and comparison of blood flow signals were obtained with a self defined score system. RESULTS: CDI showed Doppler signals in the main stem vessels, segmental and interlobar vessels in all patients; in the arcuate arteries blood flow signals were detected in only 11 of 15 patients. There was no Doppler signal in peripherally located medullary and cortical vessels. CDE showed blood flow signals in the main stem, segmental and interlobar vessels and additionally in the arcuate, interlobular and medullary as well as in the cortical vessels in all patients. CONCLUSION: CDE is more sensitive than CDI and improves the detection of blood flow signals in peripheral medullary and cortical vessels of renal transplants.

Adult↗
PubMed2000

A novel human gene similar to the protein kinase (PK) coding domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) codes for a serine-threonine PK and is expressed in melanoma cells.

The large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) is a multifunctional protein that contains a serine-threonine protein kinase (PK) activity (Nelson, J. W., Zhu, J. , Smith, C. C., Kulka, M., and Aurelian, L. (1996) J. Biol. Chem. 271, 17021-17027). Phylogenetic analyses indicated that ICP10 PK belongs to a distinct subfamily of growth factor receptor serine-threonine PKs that are characterized by their ability to function with a limited number of conserved catalytic motifs (Hunter, J. C. R., Smith, C. C., and Aurelian, L. (1995) Int. J. Onc. 7, 515-522). Here, we report the isolation and characterization of a novel gene, designated H11, that contains an open reading frame of 588 nucleotides, which encodes a protein similar to ICP10 PK. The H11 protein has Mn(2+)-dependent serine-threonine-specific PK activity as determined with a GST-H11 fusion protein and by immununocomplex PK/immunoblotting assays of 293 cells transfected with a H11 eukaryotic expression vector. PK activity is ablated by mutation of Lys(113) within the presumtive catalytic motif II (invariant Lys). 293 cells stably transfected with H11 acquire anchorage-independent growth. Endogenous H11 RNA and the H11 phosphoprotein are expressed in melanoma cell lines and primary melanoma tissues at levels higher than in normal melanocytes and in benign nevi. Melanoma cell proliferation is inhibited by treatment with antisense oligonucleotides that inhibit H11 translation, suggesting that H11 expression is associated with cell growth.

Amino Acid Sequence↗
PubMed1993

Mouse neurofibromatosis type 1 cDNA sequence reveals high degree of conservation of both coding and non-coding mRNA segments.

To identify evolutionary conserved domains and facilitate the recognition of potentially significant mutations in NF1 patients or tumors, we have determined the complete approximately 12 kb sequence of mouse neurofibromatosis type 1 mRNA. The sequence predicts a 2841 amino acid protein that is more than 98% identical to human neurofibromin. All but 9 of the 45 amino acid differences between mouse and human neurofibromin occur in the N-terminal half of the protein, with 16 changes clustered just upstream of the IRA-related segment. Given the high degree of sequence identity, virtually any sequence alteration in NF1 patients or tumors is potentially significant. We have also found that the 3' untranslated segment of NF1 mRNA is highly conserved, suggesting that this region may also be a target for mutations in NF1 patients.

Amino Acid Sequence↗
PubMed2006

Association of nucleoid proteins with coding and non-coding segments of the Escherichia coli genome.

The Escherichia coli chromosome is condensed into an ill-defined structure known as the nucleoid. Nucleoid-associated DNA-binding proteins are involved in maintaining this structure and in mediating chromosome compaction. We have exploited chromatin immunoprecipitation and high-density microarrays to study the binding of three such proteins, FIS, H-NS and IHF, across the E.coli genome in vivo. Our results show that the distribution of these proteins is biased to intergenic parts of the genome, and that the binding profiles overlap. Hence some targets are associated with combinations of bound FIS, H-NS and IHF. In addition, many regions associated with FIS and H-NS are also associated with RNA polymerase.

Bacterial Proteins↗