Browsing
     by title


0-9 A B C D E F G H I J K L M N O P Q R S T U V W X Y Z

or enter first few letters:   
OK
Peer Reviewed
See detailNucleotide sequence of a human gene coding for a polypeptide hormone
Seeburg, P. H.; Shine, J.; Martial, Joseph ULg et al

in Transactions of the Association of American Physicians (1977), 90

In summary, a general approach is presented to purify and sequence DNA fragments of a specific gene starting with a heterogeneous mixture of mRNAs. The methodology has been applied to the determination of ... [more ▼]

In summary, a general approach is presented to purify and sequence DNA fragments of a specific gene starting with a heterogeneous mixture of mRNAs. The methodology has been applied to the determination of the DNA sequence of a portion of the gene for human chorionic somatomammotropin. Most of the possible translation codons of the genetic code were found to be used. Some selectivity in the codon choices was found, and this may be important for RNA or gene regulation or structure. The stop codon UAG was found and a second stop codon in the same reading frame was found nine bases farther down. Finally, a "palindrome" sequence was detected in the 3' noncoding region. [less ▲]

Detailed reference viewed: 12 (0 ULg)
Peer Reviewed
See detailNucleotide sequence of part of the gene for human chorionic somatomammotropin: purification of DNA complementary to predominant mRNA species
Seeburg, Peter H; Shine, John; Martial, Joseph ULg et al

in Cell (1977), 12(1), 157-65

A novel purification procedure for DNA complementary to individual mRNA species has been developed by using restriction endonuclease cleavage of cDNA transcribed from a complex mixture of mRNAs. This ... [more ▼]

A novel purification procedure for DNA complementary to individual mRNA species has been developed by using restriction endonuclease cleavage of cDNA transcribed from a complex mixture of mRNAs. This procedure has allowed us to isolate and analyze DNA fragments complementary to the mRNA coding for the human peptide hormone chorionic somatomammotropin (HCS). The mRNA for this hormone is a major constituent of placental polyadenylated RNA as shown by in vitro translation of placental RNA and by nucleic acid hybridization using HCS cDNA as a specific probe. The purification of HCS cDNA was achieved by Hae III and Hha I restriction endonuclease cleavage of single-stranded cDNA synthesized in vitro from total polyadenylated placental RNA. Polyacrylamide gel electrophoresis of the products allowed detection and purification of discrete DNA fragments. A comparison of the nucleotide sequence of these fragments with that predicted from the amino acid sequence of HCS demonstrated that the fragments are transcripts of HCS mRNA, containing most of the translated and 3′ untranslated regions. The latter region is characterized by a UAG termination codon immediately adjacent to the translated region (a second in phase UAG occurs 9 nucleotides away) and a palindromic sequence (GUGACCCCUCCCCAGUG) centered 27 nucleotides from the termination codon. The purification scheme outlined for HCS cCNA should be applicable to DNA sequences complementary to mRNA species which represent at least 2% of any polyadenylated RNA preparation. This was demonstrated by restriction endonuclease cleavage of cDNA synthesized from a mixture of purified rabbit globin and total polyadenylated human placental RNAs. [less ▲]

Detailed reference viewed: 25 (3 ULg)
Peer Reviewed
See detailThe Nucleotide Sequence Of Saccharomyces Cerevisiae Chromosome Vii
Tettelin, H.; Carbone, Mla.; Albermann, K. et al

in Nature (1997), 387(6632),

Detailed reference viewed: 49 (12 ULg)
Peer Reviewed
See detailThe Nucleotide Sequence Of Saccharomyces Cerevisiae Chromosome XII
Johnston, M.; Hillier, L.; Riles, L. et al

in Nature (1997), 387(6632),

Detailed reference viewed: 53 (3 ULg)
Peer Reviewed
See detailThe Nucleotide Sequence Of Saccharomyces Cerevisiae Chromosome Xv
Dujon, B.; Albermann, K.; Aldea, M. et al

in Nature (1997), 387(6632),

Detailed reference viewed: 33 (2 ULg)
Full Text
Peer Reviewed
See detailNucleotide sequence of the bovine cyclic-AMP responsive DNA binding protein (CREB2) cDNA.
Willems, Luc ULg; Kettmann, Richard ULg; Chen, G. et al

in DNA Sequence : The Journal of DNA Sequencing & Mapping (1991), 1(6),

Detailed reference viewed: 6 (1 ULg)
Full Text
Peer Reviewed
See detailNucleotide sequence of the bovine P53 tumor-suppressor cDNA.
Dequiedt, Franck ULg; Willems, Luc ULg; Burny, A. et al

in DNA Sequence : The Journal of DNA Sequencing & Mapping (1995), 5(4),

Detailed reference viewed: 23 (10 ULg)
Peer Reviewed
See detailNucleotide sequence of the bovine viral diarrhoea virus Osloss strain: comparison with related viruses and identification of specific DNA probes in the 5' untranslated region
De Moerlooze, L.; Lecomte, C.; Brown-Shimmer, S. et al

in Journal of General Virology (The) (1993), 74

The nucleotide sequence of the cytopathic Osloss isolate of bovine viral diarrhoea virus (BVDV) was deduced from overlapping cDNA clones and from PCR products. The Osloss genome is an RNA molecule of ... [more ▼]

The nucleotide sequence of the cytopathic Osloss isolate of bovine viral diarrhoea virus (BVDV) was deduced from overlapping cDNA clones and from PCR products. The Osloss genome is an RNA molecule of positive polarity containing 12480 nucleotides and having the capacity to code for a polyprotein of 3975 amino acids. The presence of the previously described internal stop codon in this viral sequence was disproved after direct sequencing of the appropriate PCR-amplified fragment. Except for the previously reported insertion of a sequence coding for a ubiquitin-like protein, the viral genome shares great similarity with those of three other strains of the pestivirus genus. Computer-assisted sequence analyses and comparisons of known pestiviral genomic sequences led us to identify selected PCR primers in the 5' untranslated region. These primers were used successfully to amplify 18 distinct pestivirus isolates and potential DNA probes were noted from the deduced sequences. The possible use of a well conserved 26 base fragment as a diagnostic probe was confirmed in hybridization experiments. The 5' untranslated region was further studied and compared with those of other members of the Flaviviridae family, which includes the flaviviruses and the hepatitis C virus group. These sequence analyses support the possibility of discrimination amongst the closely related ruminant pestiviruses, border disease virus and BVDV. [less ▲]

Detailed reference viewed: 15 (1 ULg)
Full Text
Peer Reviewed
See detailNucleotide sequence of the gene encoding the active-site serine β-lactamase from Actinomadura R39
Houba, Simone; Willem, Sabine; Duez, Colette ULg et al

in FEMS Microbiology Letters (1989), 65(3), 241-246

The gene encoding the extracellular, active-site serine beta-lactamase of Actinomadura R39, previously cloned into Streptomyces lividans, has the information for the synthesis of a 304 amino acid protein ... [more ▼]

The gene encoding the extracellular, active-site serine beta-lactamase of Actinomadura R39, previously cloned into Streptomyces lividans, has the information for the synthesis of a 304 amino acid protein, the amino terminal region of which has the characteristic features of a signal peptide. The Actinomadura R39 beta-lactamase is another member of the class A beta-lactamases. In particular, it shows high homology with the beta-lactamase of Bacillus licheniformis. [less ▲]

Detailed reference viewed: 14 (1 ULg)
Full Text
Peer Reviewed
See detailNucleotide sequence of the gene encoding the Streptomyces albus G β-lactamase precursor
Dehottay, Philippe; Dusart, Jean; De Meester, Fabien et al

in European Journal of Biochemistry (1987), 166(2), 345-350

A 1400-base DNA fragment, which contains the gene encoding the extracellular active-site serine beta-lactamase of Streptomyces albus G previously cloned into Streptomyces lividans [Dehottay et al. (1986 ... [more ▼]

A 1400-base DNA fragment, which contains the gene encoding the extracellular active-site serine beta-lactamase of Streptomyces albus G previously cloned into Streptomyces lividans [Dehottay et al. (1986) Gene 42, 31-36], was sequenced. The gene codes for a 314-amino-acid precursor, the N-terminal region of which has the characteristics of a signal peptide. The beta-lactamase as excreted by the host strain S. lividans PD6 has a ragged N-terminus, indicating either the presence of a leader peptidase of poor specificity or the action of an aminopeptidase. The primary structure (as deduced from the nucleotide sequence) was confirmed by amino acid sequencing of a 16-residue stretch at the amino terminus of the protein, a 12-residue stretch containing the active-site serine [De Meester et al. (1987) Biochem. J. 244, 427-432] and a 23-residue stretch obtained by trypsin digestion of the protein. The beta-lactamase belongs to class A, has three half-cystine residues (one of which occurs on the amino side of the active-site serine) and is inactivated by thiol reagents. Putative ribosome binding site and terminator region were identified. [less ▲]

Detailed reference viewed: 7 (0 ULg)
Full Text
Peer Reviewed
See detailNucleotide Sequence of the Lipase Gene Lip2 from the Antarctic Psychrotroph Moraxella Ta144 and Site-Specific Mutagenesis of the Conserved Serine and Histidine Residues
Feller, Georges ULg; Thiry, M.; Gerday, Charles ULg

in DNA & Cell Biology (1991), 10(5), 381-8

The lip2 gene from the antarctic psychotroph Moraxella TA144 was sequenced. The primary structure of the Lip2 preprotein deduced from the nucleotide sequence is composed of 433 amino acids with a ... [more ▼]

The lip2 gene from the antarctic psychotroph Moraxella TA144 was sequenced. The primary structure of the Lip2 preprotein deduced from the nucleotide sequence is composed of 433 amino acids with a predicted Mr of 47,222. This enzyme contains a Ser-centered consensus sequence and a conserved His-Gly dipeptide found in most lipase amino-terminal domains. These sequences are involved in the lipase active site conformation since substitution of the conserved Ser or His residues by Ala and Gln, respectively, results in the loss of both lipase and esterase activities. Structural factors that would allow proper enzyme flexibility at low temperatures are discussed. It is suggested that only subtle changes in the primary structure of these psychrotrophic enzymes can account for their ability to catalyze lipolysis at temperatures close to 0 degrees C. [less ▲]

Detailed reference viewed: 19 (2 ULg)
Full Text
Peer Reviewed
See detailNucleotide Sequence of the Lipase Gene Lip3 from the Antarctic Psychotroph Moraxella Ta144
Feller, Georges ULg; Thiry, M.; Gerday, Charles ULg

in Biochimica et Biophysica Acta (1991), 1088(2), 323-4

A lipase gene (lip3) from the psychotrophic strain Moraxella TA144 has been cloned and sequenced. The deduced primary structure of the lipase preprotein is composed of 315 amino acids with a predicted Mr ... [more ▼]

A lipase gene (lip3) from the psychotrophic strain Moraxella TA144 has been cloned and sequenced. The deduced primary structure of the lipase preprotein is composed of 315 amino acids with a predicted Mr of 34,772. This enzyme contains two consensus peptides showing cluster of glycine residues that may be involved in domain flexibility. The cloned gene product conserves the low temperature activity and the thermolability properties of the wild enzyme. [less ▲]

Detailed reference viewed: 8 (0 ULg)
Full Text
Peer Reviewed
See detailNucleotide sequence of the ovine P53 tumor-suppressor cDNA and its genomic organization.
Dequiedt, Franck ULg; Kettmann, Richard ULg; Burny, A. et al

in DNA Sequence : The Journal of DNA Sequencing & Mapping (1995), 5(4),

Detailed reference viewed: 22 (7 ULg)
Peer Reviewed
See detailNucleotide sequence of the proline permease gene PUT4 of Saccharomyces cerevisiae.
Vandenbol, Micheline ULg; Hidalgo, E.; Vissers, S. et al

Poster (1987)

Detailed reference viewed: 4 (0 ULg)
Full Text
Peer Reviewed
See detailNucleotide sequences of the pbpX genes encoding the penicillin-binding proteins 2x from Streptococcus pneumoniae R6 and a cefotaxime-resistant mutant, C506
Laible, G.; Hakenbeck, R.; Sicard, M. A. et al

in Molecular Microbiology (1989), 3(10), 1337-1348

Development of penicillin resistance in Streptococcus pneumoniae is due to successive mutations in penicillin-binding proteins (PBPs) which reduce their affinity for beta-lactam antibiotics. PBP2x is one ... [more ▼]

Development of penicillin resistance in Streptococcus pneumoniae is due to successive mutations in penicillin-binding proteins (PBPs) which reduce their affinity for beta-lactam antibiotics. PBP2x is one of the high-Mr PBPs which appears to be altered both in resistant clinical isolates, and in cefotaxime-resistant laboratory mutants. In this study, we have sequenced a 2564 base-pair chromosomal fragment from the penicillin-sensitive S. pneumoniae strain R6, which contains the PBP2x gene. Within this fragment, a 2250 base-pair open reading frame was found which coded for a protein having an Mr of 82.35kD, a value which is in good agreement with the Mr of 80-85 kD measured by SDS-gel electrophoresis of the PBP2x protein itself. The N-terminal region resembled an unprocessed signal peptide and was followed by a hydrophobic sequence that may be responsible for membrane attachment of PBP2x. The corresponding nucleotide sequence of the PBP2x gene from C504, a cefotaxime-resistant laboratory mutant obtained after five selection steps, contained three nucleotide substitutions, causing three amino acid alterations within the beta-lactam binding domain of the PBP2x protein. Alterations affecting similar regions of Escherichia coli PBP3 and Neisseria gonorrhoeae PBP2 from beta-lactam-resistant strains are known. The penicillin-binding domain of PBP2x shows highest homology with these two PBPs and S. pneumoniae PBP2b. In contrast, the N-terminal extension of PBP2x has the highest homology with E. coli PBP2 and methicillin-resistant Staphylococcus aureus PBP2'. No significant homology was detected with PBP1a or PBP1b of Escherichia coli, or with the low-Mr PBPs. [less ▲]

Detailed reference viewed: 5 (0 ULg)
Peer Reviewed
See detailNude athymic syndrom in a calf
Leroy, Pascal ULg; Hanset, R.; Doizé, Cécile ULg

(1980)

Detailed reference viewed: 11 (0 ULg)
Full Text
Peer Reviewed
See detailNudging acne by topical beta-lipohydroxy acid (LHA), a new comedolytic agent.
Pierard, Gérald ULg; Rougier, A.

in European Journal of Dermatology (2002), 12(4), -

Detailed reference viewed: 19 (0 ULg)
Full Text
Peer Reviewed
See detailNudging epidermal field cancerogenesis by imiquimod.
Uhoda, Isabelle; Quatresooz, Pascale ULg; Pierard, Claudine ULg et al

in Dermatology : International Journal for Clinical & Investigative Dermatology (2003), 206(4), 357-60

BACKGROUND: The coexistence of malignancies close to each other on the skin has been occasionally reported. The concept of field cancerogenesis applies to such cases. Given the purported mechanism of ... [more ▼]

BACKGROUND: The coexistence of malignancies close to each other on the skin has been occasionally reported. The concept of field cancerogenesis applies to such cases. Given the purported mechanism of action of imiquimod, it should not be surprising that this treatment could inhibit epidermal field cancerogenesis. AIM: To assess the effect of imiquimod applied twice weekly on incipient bowenoid changes disclosed in the vicinity of basal cell carcinomas. MATERIALS AND METHOD: Biopsies were taken before treatment and after 4-6 weeks and 12 weeks of imiquimod treatment. RESULTS: Large atypical bowenoid keratinocytes and dyskeratotic cells were cleared in time while factor-XIIIa-positive dermal dendrocytes appeared boosted and admixed with a brisk lymphocytic infiltration. CONCLUSION: Epidermal field cancerogenesis appears to be controlled by imiquimod. Dermal dendrocytes might play a pivotal role in this regression phenomenon. [less ▲]

Detailed reference viewed: 17 (2 ULg)
Full Text
Peer Reviewed
See detailNudging hair shedding by antidandruff shampoos. A comparison of 1% ketoconazole, 1% piroctone olamine and 1% zinc pyrithione formulations.
Franchimont, Claudine ULg; Goffin, Véronique ULg; Henry, Frédérique ULg et al

in International Journal of Cosmetic Science (2002), 24(5), 249-56

Hair shedding and hair thinning have been reported to be affected by dandruff and seborrhoeic dermatitis. The present study was conducted in 150 men presenting with telogen effluvium related to androgenic ... [more ▼]

Hair shedding and hair thinning have been reported to be affected by dandruff and seborrhoeic dermatitis. The present study was conducted in 150 men presenting with telogen effluvium related to androgenic alopecia associated with dandruff. They were randomly allocated to three groups receiving each one of the three shampoos in the market containing either 1% ketoconazole (KTZ), 1% piroctone olamine (PTO) or 1% zinc pyrithione (ZPT). Shampoos had to be used 2-3 times a week for 6 months. Hair shedding during shampoo was evaluated semiquantitatively. Hair density on the vertex was evaluated on photographs using a Dermaphot. Trichograms were used for determining the anagen hair percentage and the mean proximal hair shaft diameter using computerized image analysis. The sebum excretion rate (SER, mug cm(-2) h(-1)) was also measured using a Sebumeter((R)). The three treatments cleared pruritus and dandruff rapidly. At end point, hair density was unchanged, although hair shedding was decreased (KTZ: -17.3%, PTO: -16.5%, ZPT: -10.1%) and the anagen hair percentage was increased (KTZ: 4.9%, PTO: 7.9%, ZPT: 6.8%). The effect on the mean hair shaft diameter was contrasted between the three groups of volunteers (KTZ: 5.4%, PTO: 7.7%, ZPT: -2.2%). In conclusion, telogen effluvium was controlled by KTZ, PTO and ZPT shampoos at 1% concentration. In addition, KTZ and PTO increased the mean hair shaft thickness while discretely decreasing the sebum output at the skin surface. [less ▲]

Detailed reference viewed: 115 (0 ULg)