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Journal Article
Journal Article
Current Pharmaceutical Design, ISSN 1381-6128, 02/2007, Volume 13, Issue 4, pp. 349 - 366
Journal Article
European Journal of Neuroscience, ISSN 0953-816X, 11/2019, Volume 50, Issue 9, pp. 3502 - 3519
Neuropeptides are processed from larger preproproteins by a dedicated set of enzymes. The molecular and biochemical mechanisms underlying preproprotein... 
direct mass spectrometric profiling | M14 carboxypeptidases | proprotein processing | peptidomics | fruit fly behaviour | Larvae | Enzymes | Starvation | Peptides | Hyperactivity | Neuropeptides | Nervous system | Carboxypeptidase E | Genomes | Lethality | Carboxypeptidase D | Mammals | Insects | Carboxypeptidase A | Locomotor activity
Journal Article
FEBS Letters, ISSN 0014-5793, 2004, Volume 577, Issue 3, pp. 422 - 426
We undertook a growth‐based screen exploiting the degradation of CTL*, a chimeric membrane‐bound ERAD substrate derived from soluble lumenal CPY*. We screened... 
ERAD | Protein degradation | Endoplasmic reticulum | Yos9p | Quality control | Glycoprotein | CPY, carboxypeptidase Y | CTL, mutated carboxypeptidase Y transmembrane domain – Leu2p | CPY, mutated carboxypeptidase Y | GPI, glycosyl phosphatidyl inositol | PDI, protein disulfide isomerase | UPR, unfolded protein response | ER, endoplasmic reticulum | CTG, mutated carboxypeptidase Y transmembrane domain – GFP | ERAD, endoplasmic reticulum associated degradation | MRH, mannose-6-phosphate receptor homology | CTG, mutated carboxypeptidase Y transmembrane domain - GFP | CTL, mutated carboxypeptidase Y transmembrane domain - Leu2p | CARBOXYPEPTIDASE YSCY | quality control | BIOCHEMISTRY & MOLECULAR BIOLOGY | QUALITY-CONTROL | ENDOPLASMIC-RETICULUM DEGRADATION | SACCHAROMYCES-CEREVISIAE | SECRETORY PATHWAY | CELL BIOLOGY | YEAST | BIOPHYSICS | GENE | MISFOLDED GLYCOPROTEINS | glycoprotein | MANNOSIDASE-LIKE PROTEIN | endoplasmic reticulum | protein degradation | UBIQUITIN-PROTEASOME PATHWAY | Glycoproteins - genetics | Protein Structure, Tertiary | Temperature | Methionine - metabolism | Saccharomyces cerevisiae - genetics | Glycoproteins - metabolism | Endoplasmic Reticulum - metabolism | Substrate Specificity | Sulfur Radioisotopes | Genetic Complementation Test | Plasmids - metabolism | Precipitin Tests | Saccharomyces cerevisiae - metabolism | Carrier Proteins - metabolism | Models, Biological | Gene Deletion | Saccharomyces cerevisiae Proteins - metabolism | Carrier Proteins - chemistry | Cell Membrane - metabolism | Kinetics | Saccharomyces cerevisiae - growth & development | Quality Control | Saccharomyces cerevisiae Proteins - chemistry
Journal Article
Acta Crystallographica Section F, ISSN 2053-230X, 10/2018, Volume 74, Issue 10, pp. 638 - 643
A site‐directed mutagenesis method has been used to obtain the G215S/A251G/T257A/D260G/T262D mutant of carboxypeptidase T from Thermoactinomyces vulgaris... 
metallocarboxypeptidase B | metallocarboxypeptidase T | Thermoactinomyces vulgaris | substrate selectivity | S1′ subsite | X‐ray crystallography | X-ray crystallography | S1 ' subsite | SITE | CHYMOTRYPSIN | CALCIUM-IONS | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | DETERMINANT | X-RAY-DIFFRACTION | CRYSTALLOGRAPHY | PRINCIPLES | PRIMARY SPECIFICITY POCKET | SUBSTRATE-SPECIFICITY | BIOPHYSICS | CONVERTING TRYPSIN | LOOPS | Carboxypeptidase B - genetics | Carboxypeptidase B - chemistry | Bacterial Proteins - chemistry | Substrate Specificity | Crystallography, X-Ray | Thermodynamics | Swine | Protein Engineering | Carboxypeptidases - chemistry | Protein Interaction Domains and Motifs | Thermoactinomyces - enzymology | Pancreas - enzymology | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Catalytic Domain | Gene Expression | Mutagenesis, Site-Directed | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Carboxypeptidases - genetics | Recombinant Proteins - genetics | Carboxypeptidase B - metabolism | Animals | Protein Conformation, beta-Strand | Hydrophobic and Hydrophilic Interactions | Protein Binding | Bacterial Proteins - metabolism | Carboxypeptidases - metabolism | Thermoactinomyces - chemistry | Structural Homology, Protein | Kinetics | Mutation | Pancreas - chemistry | Amino Acid Substitution | Enzymes | Residues | Crystallization | Selectivity | Hydrophobicity | Crystallography | Substrates | Mutagenesis | Carboxypeptidase B | Carboxypeptidase A | Substrate specificity | Pancreas | Crystal structure
Journal Article
Journal Article
Journal Article
Journal Article
Biotechnology and Bioengineering, ISSN 0006-3592, 10/2016, Volume 113, Issue 10, pp. 2100 - 2106
Journal Article