Prolyl Oligopeptidase (Q56593808)

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article from 1998

Language	Label	Description	Also known as
English	Prolyl Oligopeptidase	article from 1998

Statements

scholarly article

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Prolyl Oligopeptidase (English)

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author name string

Vilmos Fülöp

1

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Zsolt Böcskei

2

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László Polgár

3

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language of work or name

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publication date

July 1998

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94

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2

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161-170

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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.

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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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7 January 2021

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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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7 January 2021

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Porcine muscle prolyl endopeptidase and its endogenous substrates.

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7 January 2021

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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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7 January 2021

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Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting

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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6

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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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6

7 January 2021

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Structural relationship between lipases and peptidases of the prolyl oligopeptidase family

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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6

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

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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

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7 January 2021

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Improved Fourier coefficients for maps using phases from partial structures with errors

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cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue

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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6

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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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6

7 January 2021

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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

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

7 January 2021

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Cloning and sequence analysis of the gene encoding human lymphocyte prolyl endopeptidase

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6

7 January 2021

based on heuristic

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The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2

1 reference

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7 January 2021

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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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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6

7 January 2021

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Prolyl endopeptidase

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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6

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

7 January 2021

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Prolyl Endopeptidase from Flavobacterium meningosepticum: Cloning and Sequencing of the Enzyme Gene1

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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981416-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

10.1016/S0092-8674(00)81416-6

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