نتایج جستجو برای: cleavage sites

تعداد نتایج: 320451  

Journal: :Nucleic acids research 1997
D Winter N Polacek I Halama B Streicher A Barta

Ribosomes have long been known to require divalent metal ions for their functional integrity. Pb2+-induced cleavage of the sugar-phosphate backbone has now been used to probe for metal binding sites in rRNA. Only three prominent Pb2+cleavages have been detected, with cleavage sites 5' of G240 in 16S rRNA and two sites 5' of A505 and C2347 in 23S rRNA. All cleavages occur in non-paired regions o...

Journal: :Journal of cell science. Supplement 1987
R H Symons C J Hutchins A C Forster P D Rathjen P Keese J E Visvader

Viroids are infectious, circular RNA molecules of 246 to 375 nucleotides found in plants. Virusoids are of similar size and structure but they are dependent on, and encapsidated in, a helper virus. A rolling circle mechanism of replication is considered to account for the presence of greater-than-unit-length plus and minus RNAs of both viroids and virusoids found in infected plants. An essentia...

Journal: :Protein science : a publication of the Protein Society 1996
N Blom J Hansen D Blaas S Brunak

Picornaviral proteinases are responsible for maturation cleavages of the viral polyprotein, but also catalyze the degradation of cellular targets. Using graphical visualization techniques and neural network algorithms, we have investigated the sequence specificity of the two proteinases 2Apro and 3Cpro. The cleavage of VP0 (giving rise to VP2 and VP4), which is carried out by a so-far unknown p...

2011
Sebastian Hogl Peer-Hendrik Kuhn Alessio Colombo Stefan F. Lichtenthaler Koichi M. Iijima

Regulated intramembrane proteolysis of the amyloid precursor protein (APP) by the protease activities a-, band csecretase controls the generation of the neurotoxic amyloid b peptide. APLP2, the amyloid precursor-like protein 2, is a homolog of APP, which shows functional overlap with APP, but lacks an amyloid b domain. Compared to APP, less is known about the proteolytic processing of APLP2, in...

Journal: :Journal of virology 1994
R Bartenschlager L Ahlborn-Laake J Mous H Jacobsen

Recombinant vaccinia viruses were used to study the processing of hepatitis C virus (HCV) nonstructural polyprotein precursor. HCV-specific proteins and cleavage products were identified by size and by immunoprecipitation with region-specific antisera. A polyprotein beginning with 20 amino acids derived from the carboxy terminus of NS2 and ending with the NS5B stop codon (amino acids 1007 to 30...

Journal: :The Biochemical journal 1986
D Jacobs N L Brown

The modification enzyme (M.EaeI) corresponding to the restriction endonuclease EaeI was partially purified from Enterobacter aerogenes PW201. The M.EaeI enzyme methylates the innermost cytosine residue in each strand of the family of related sequences that constitute the EaeI recognition site to give: 5'-Y-G-G-5mC-C-R-3' where 5mC is 5-methylcytosine. M.EaeI protects these sites against cleavag...

Journal: :Journal of virology 2011
Xiaohong Wang Craig Meyers Hsu-Kun Wang Louise T Chow Zhi-Ming Zheng

Human papillomavirus type 18 (HPV18) is the second most common oncogenic HPV genotype, responsible for ∼15% of cervical cancers worldwide. In this study, we constructed a full HPV18 transcription map using HPV18-infected raft tissues derived from primary human vaginal or foreskin keratinocytes. By using 5' rapid amplification of cDNA ends (RACE), we mapped two HPV18 transcription start sites (T...

Journal: :The Journal of biological chemistry 1992
K Nakayama T Watanabe T Nakagawa W S Kim M Nagahama M Hosaka K Hatsuzawa K Kondoh-Hashiba K Murakami

Many peptide hormones and neuropeptides are produced from larger, inactive precursors through endoproteolysis at sites usually marked by paired basic residues (primarily Lys-Arg and Arg-Arg), or occasionally by a monobasic residue (primarily Arg). Based upon data concerning processing of prorenin and its mutants around the native Lys-Arg cleavage site expressed in mouse pituitary AtT-20 cells, ...

Journal: :Cell 1992
A J Newman C Norman

U5 snRNA is an essential pre-mRNA splicing factor whose function remains enigmatic. Specific mutations in a conserved single-stranded loop sequence in yeast U5 snRNA can activate cleavage of G1----A mutant pre-mRNAs at aberrant 5' splice sites and facilitate processing of dead-end lariat intermediates to mRNA. Activation of aberrant 5' cleavage sites involves base pairing between U5 snRNA and n...

Journal: :Bioinformatics 2007
Lawrence J. K. Wee Tin Wee Tan Shoba Ranganathan

UNLABELLED Caspases belong to a unique class of cysteine proteases which function as critical effectors of apoptosis, inflammation and other important cellular processes. Caspases cleave substrates at specific tetrapeptide sites after a highly conserved aspartic acid residue. Prediction of such cleavage sites will complement structural and functional studies on substrates cleavage as well as di...

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