Pig kidney legumain: an asparaginyl endopeptidase with restricted specificity. - Test2 - elhamkhani - TriplyDB

Pig kidney legumain: an asparaginyl endopeptidase with restricted specificity.

Pig kidney legumain: an asparaginyl endopeptidase with restricted specificity.

http://www.wikidata.org/entity/Q42993530

about

Activation of human prolegumain by cleavage at a C-terminal asparagine residue Inhibition of distant caspase homologues by natural caspase inhibitors Characterization of legumain.Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile.Asparagine endopeptidase is an innovative therapeutic target for neurodegenerative diseases.Asparaginyl endopeptidase: case history of a class II MHC compartment protease.The TvLEGU-1, a legumain-like cysteine proteinase, plays a key role in Trichomonas vaginalis cytoadherence Proteomic analysis of mouse models of Niemann-Pick C disease reveals alterations in the steady-state levels of lysosomal proteins within the brain.Pepsin is a positive regulator of Ac-cathB-2 involved in the rat gut penetration of Angiostrongylus cantonensis Asparaginyl endopeptidase promotes the invasion and metastasis of gastric cancer through modulating epithelial-to-mesenchymal transition and analysis of their phosphorylation signaling pathways A large and accurate collection of peptidase cleavages in the MEROPS database.MiRNA-3978 regulates peritoneal gastric cancer metastasis by targeting legumain.Development of a selected reaction monitoring mass spectrometry-based assay to detect asparaginyl endopeptidase activity in biological fluids Molecular-dynamics-simulation-driven design of a protease-responsive probe for in-vivo tumor imaging.Prothymosin alpha is processed to thymosin alpha 1 and thymosin alpha 11 by a lysosomal asparaginyl endopeptidase.Activation of progelatinase A by mammalian legumain, a recently discovered cysteine proteinase.Distinct Roles of Catalytic Cysteine and Histidine in the Protease and Ligase Mechanisms of Human Legumain As Revealed by DFT-Based QM/MM Simulations.Legumain forms from plants and animals differ in their specificity.Identification and functional characterization of legumain in amphioxus Branchiostoma belcheri.Expression of both poly r(C) binding protein 1 (PCBP1) and miRNA-3978 is suppressed in peritoneal gastric cancer metastasis.Proteomic Analysis of Brain and Cerebrospinal Fluid from the Three Major Forms of Neuronal Ceroid Lipofuscinosis Reveals Potential Biomarkers.An asparaginyl endopeptidase mediates in vivo protein backbone cyclization.Regulates Tumorigenesis and Chemoresistance During Peritoneal Metastasis of Gastric Cancer

P2860

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P2860

Pig kidney legumain: an asparaginyl endopeptidase with restricted specificity.

http://www.wikidata.org/entity/Q42993530

description

1999 nî lūn-bûn

@nan

1999年の論文

@ja

1999年学术文章

@wuu

1999年学术文章

@zh

1999年学术文章

@zh-cn

1999年学术文章

@zh-hans

1999年学术文章

@zh-my

1999年学术文章

@zh-sg

1999年學術文章

@yue

1999年學術文章

@zh-hant

name

Pig kidney legumain: an asparaginyl endopeptidase with restricted specificity.

@en

Pig kidney legumain: an asparaginyl endopeptidase with restricted specificity.

@nl

type

label

Pig kidney legumain: an asparaginyl endopeptidase with restricted specificity.

@en

Pig kidney legumain: an asparaginyl endopeptidase with restricted specificity.

@nl

prefLabel

Pig kidney legumain: an asparaginyl endopeptidase with restricted specificity.

@en

Pig kidney legumain: an asparaginyl endopeptidase with restricted specificity.

@nl

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0264-6021:3390743

P1433

Biochemical Journal

P1476

Pig kidney legumain: an asparaginyl endopeptidase with restricted specificity

@en

P2093

Dando PM

http://www.w3.org/2001/XMLSchema#string

Fortunato M

http://www.w3.org/2001/XMLSchema#string

Knight CG

http://www.w3.org/2001/XMLSchema#string

McKendrick JE

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Smith L

http://www.w3.org/2001/XMLSchema#string

P2860

The alpha-macroglobulin bait region. Sequence diversity and localization of cleavage sites for proteinases in five mammalian alpha-macroglobulins

Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase

Cloning and expression of mouse legumain, a lysosomal endopeptidase

The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1998.

Characterization of the bacterial metalloendopeptidase pitrilysin by use of a continuous fluorescence assay.

An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation.

Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases.

Three high molecular weight protease inhibitors of rat plasma. Isolation, characterization, and acute phase changes.

The electrophoretically 'slow' and 'fast' forms of the alpha 2-macroglobulin molecule.

The biogenesis of the MHC class II compartment in human I-cell disease B lymphoblasts.

P304

743-749

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scholarly article

P356

10.1042/0264-6021:3390743

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10.1042/BJ3390743

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P407

P478

339 ( Pt 3)

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P50

Alan J. Barrett

P577

1999-05-01T00:00:00Z

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P5875

13082007

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P698

10215615

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P932

1220212

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