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Prolyl Oligopeptidase
article from 1998
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instance of
scholarly article
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title
Prolyl Oligopeptidase
(English)
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author name string
Vilmos Fülöp
series ordinal
1
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Zsolt Böcskei
series ordinal
2
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László Polgár
series ordinal
3
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language of work or name
English
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publication date
July 1998
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published in
Cell
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volume
94
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issue
2
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page(s)
161-170
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cites work
In vitro and in vivo inhibition of prolyl endopeptidase
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Cytochrome cd1 structure: unusual haem environments in a nitrite reductase and analysis of factors contributing to beta-propeller folds
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ALSCRIPT: a tool to format multiple sequence alignments
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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
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The CCP4 suite: programs for protein crystallography
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Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins
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Cloning of proline-specific endopeptidase gene from Flavobacterium meningosepticum: expression in Escherichia coli and purification of the heterologous protein.
1 reference
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1.8 A crystal structure of the C-terminal domain of rabbit serum haemopexin
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Colocalization of prolyl endopeptidase and amyloid beta-peptide in brains of senescence-accelerated mouse
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The anatomy of a bifunctional enzyme: structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1
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Convergence of active center geometries
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The purification, characterization and analysis of primary and secondary-structure of prolyl oligopeptidase from human lymphocytes. Evidence that the enzyme belongs to the alpha/beta hydrolase fold family.
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Improved methods for building protein models in electron density maps and the location of errors in these models
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Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods.
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The 2.0 A crystal structure of a heterotrimeric G protein
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Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller
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Lower serum prolyl endopeptidase enzyme activity in major depression: further evidence that peptidases play a role in the pathophysiology of depression.
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Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family.
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Proline residues in the maturation and degradation of peptide hormones and neuropeptides
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Raster3D Version 2.0. A program for photorealistic molecular graphics
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Increase in the septal vasopressin content by prolyl endopeptidase inhibitors in rats
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Porcine muscle prolyl endopeptidase and its endogenous substrates.
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G protein heterodimers: new structures propel new questions
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The alpha/beta hydrolase fold
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Refined structure of dienelactone hydrolase at 1.8 A
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pH-dependent mechanism in the catalysis of prolyl endopeptidase from pig muscle
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Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting
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7 January 2021
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Unusual secondary specificity of prolyl oligopeptidase and the different reactivities of its two forms toward charged substrates
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7 January 2021
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Structural relationship between lipases and peptidases of the prolyl oligopeptidase family
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7 January 2021
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Prolyl oligopeptidase catalysis. Reactions with thiono substrates reveal substrate-induced conformational change to be the rate-limiting step
1 reference
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7 January 2021
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New prolyl endopeptidase inhibitors: in vitro and in vivo activities of azabicyclo[2.2.2]octane, azabicyclo[2.2.1]heptane, and perhydroindole derivatives
1 reference
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Improved Fourier coefficients for maps using phases from partial structures with errors
1 reference
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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6
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7 January 2021
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cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue
1 reference
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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6
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7 January 2021
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The anatomy and taxonomy of protein structure
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7 January 2021
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Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels
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Specific inhibitor for prolyl endopeptidase suppresses the generation of amyloid beta protein in NG108-15 cells.
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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6
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7 January 2021
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Crystal structure of a G-protein beta gamma dimer at 2.1A resolution
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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6
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7 January 2021
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Cloning and sequence analysis of the gene encoding human lymphocyte prolyl endopeptidase
1 reference
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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6
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7 January 2021
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The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2
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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6
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A comparison of the properties and enzymatic activities of three angiotensin processing enzymes: angiotensin converting enzyme, prolyl endopeptidase and neutral endopeptidase 24.11.
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Prolyl endopeptidase
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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6
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7 January 2021
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Specific inhibitors for prolyl endopeptidase and their anti-amnesic effect
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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6
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7 January 2021
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Prolyl Endopeptidase from Flavobacterium meningosepticum: Cloning and Sequencing of the Enzyme Gene1
1 reference
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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6
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Identifiers
DOI
10.1016/S0092-8674(00)81416-6
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