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MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

http://www.wikidata.org/entity/Q24623108

about

Genome sequencing of four Aureobasidium pullulans varieties: biotechnological potential, stress tolerance, and description of new species Comparative Genome Analysis of Trichophyton rubrum and Related Dermatophytes Reveals Candidate Genes Involved in Infection The genome of the hydatid tapeworm Echinococcus granulosus A comprehensive view of the web-resources related to sericulture Tackling Unwanted Proteolysis in Plant Production Hosts Used for Molecular Farming Involvement of Kallikrein-Related Peptidases in Normal and Pathologic Processes Innate Immune Response in Brain, NF-Kappa B Signaling and Cystatins Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triad Bacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulence Thrombin inhibition by the serpins Antigenic peptide trimming by ER aminopeptidases--insights from structural studies The genome of tolypocladium inflatum: evolution, organization, and expression of the cyclosporin biosynthetic gene cluster RNA-seq-based metatranscriptomic and microscopic investigation reveals novel metalloproteases of Neobodo sp. as potential virulence factors for soft tunic syndrome in Halocynthia roretzi Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector Structural and functional analysis of the CspB protease required for Clostridium spore germination Ultratight crystal packing of a 10 kDa protein Porphyromonas gingivalis Virulence Factor Gingipain RgpB Shows a Unique Zymogenic Mechanism for Cysteine Peptidases Insights into Substrate Specificity and Metal Activation of Mammalian Tetrahedral Aspartyl Aminopeptidase X-ray Structure Analysis and Characterization of AFUEI, an Elastase Inhibitor from Aspergillus fumigatus Crystal Structures of the Viral Protease Npro Imply Distinct Roles for the Catalytic Water in Catalysis A Novel Family of Soluble Minimal Scaffolds Provides Structural Insight into the Catalytic Domains of Integral Membrane Metallopeptidases Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation Buckwheat trypsin inhibitor with helical hairpin structure belongs to a new family of plant defence peptides Ultrahigh and High Resolution Structures and Mutational Analysis of Monomeric Streptococcus pyogenes SpeB Reveal a Functional Role for the Glycine-rich C-terminal Loop The Tick-Derived Anticoagulant Madanin Is Processed by Thrombin and Factor Xa Matrix Metalloproteinase-10/TIMP-2 Structure and Analyses Define Conserved Core Interactions and Diverse Exosite Interactions in MMP/TIMP Complexes The Structure of Classical Swine Fever Virus Npro: A Novel Cysteine Autoprotease and Zinc-Binding Protein Involved in Subversion of Type I Interferon Induction Development and binding characteristics of phosphonate inhibitors of SplA protease from Staphylococcus aureus Functional and Structural Characterization of Vibrio cholerae Extracellular Serine Protease B, VesB High-resolution structure of the M14-type cytosolic carboxypeptidase fromBurkholderia cenocepaciarefined exploitingPDB_REDOstrategies Structural and enzymatic characterization of a host-specificity determinant fromSalmonella Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65 Proteolytic Activation of Human Cathepsin A MpaA is a murein-tripeptide-specific zinc carboxypeptidase that functions as part of a catabolic pathway for peptidoglycan-derived peptides in γ-proteobacteria Crystal structure of greglin, a novel non-classical Kazal inhibitor, in complex with subtilisin Structural basis for the evolution of vancomycin resistance D,D-peptidases The malaria parasite egress protease SUB1 is a calcium-dependent redox switch subtilisin Structure of theArabidopsis thalianaTOP2 oligopeptidase S46 Peptidases are the First Exopeptidases to be Members of Clan PA The structural basis of ZMPSTE24-dependent laminopathies

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MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

http://www.wikidata.org/entity/Q24623108

description

2012 nî lūn-bûn

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2012 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

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MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

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MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

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type

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MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

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MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

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MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

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MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

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MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

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MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

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Nucleic Acids Research

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MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

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A probabilistic model of local sequence alignment that simplifies statistical significance estimation

Evolutionary families of peptidases

Evolutionary families of peptidase inhibitors

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

Database resources of the National Center for Biotechnology Information

The RCSB Protein Data Bank: redesigned web site and web services

MEROPS: the peptidase database

Chemical Entities of Biological Interest: an update

DrugBank: a knowledgebase for drugs, drug actions and drug targets

Improved tools for biological sequence comparison.

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scholarly article

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89969

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10.1093/NAR/GKR987

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Database issue

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40

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Alan J. Barrett

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2012-01-01T00:00:00Z

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