Sialidase-like Asp-boxes: sequence-similar structures within different protein folds - Test2 - elhamkhani - TriplyDB

Sialidase-like Asp-boxes: sequence-similar structures within different protein folds

Sialidase-like Asp-boxes: sequence-similar structures within different protein folds

http://www.wikidata.org/entity/Q24644728

about

Profile-profile comparisons by COMPASS predict intricate homologies between protein families Structure of a signaling-competent reelin fragment revealed by X-ray crystallography and electron tomography Structural Insights into Reelin Function: Present and Future Sialidases from gut bacteria: a mini-review Molecular Basis of Arabinobio-hydrolase Activity in Phytopathogenic Fungi: CRYSTAL STRUCTURE AND CATALYTIC MECHANISM OF FUSARIUM GRAMINEARUM GH93 EXO- -L-ARABINANASE Evolutionary Origins of a Bioactive Peptide Buried within Preproalbumin A vocabulary of ancient peptides at the origin of folded proteins Evolution of outer membrane beta-barrels from an ancestral beta beta hairpin.Identification of a linear epitope in sortilin that partakes in pro-neurotrophin binding.Sequence and structural analysis of the Asp-box motif and Asp-box beta-propellers; a widespread propeller-type characteristic of the Vps10 domain family and several glycoside hydrolase families Transcriptome analysis of the Cryptocaryon irritans tomont stage identifies potential genes for the detection and control of cryptocaryonosis.Identification of biofilm matrix-associated proteins from an acid mine drainage microbial community.Abrogation of neuraminidase reduces biofilm formation, capsule biosynthesis, and virulence of Porphyromonas gingivalis.Genomic analyses, gene expression and antigenic profile of the trans-sialidase superfamily of Trypanosoma cruzi reveal an undetected level of complexity.β-Propeller blades as ancestral peptides in protein evolution.New insights on the sialidase protein family revealed by a phylogenetic analysis in metazoa.The genome sequence of Mannheimia haemolytica A1: insights into virulence, natural competence, and Pasteurellaceae phylogeny More than the sum of their parts: on the evolution of proteins from peptides.Sialidase and sialoglycoproteases can modulate virulence in Porphyromonas gingivalis.Sequence diversity of the Trypanosoma cruzi complement regulatory protein family.Sialic acid: a sweet swing between mammalian host and Trypanosoma cruzi Evidence for recombination between a sialidase (nanH) of Actinomyces naeslundii and Actinomyces oris, previously named 'Actinomyces naeslundii genospecies 1 and 2'.A surface-exposed neuraminidase affects complement resistance and virulence of the oral spirochaete Treponema denticola.Classification of proteins with shared motifs and internal repeats in the ECOD database.Genetic characterization of ØVC8 lytic phage for Vibrio cholerae O1.Heterozygous reelin mutations cause autosomal-dominant lateral temporal epilepsy.Molecular cloning and biochemical characterization of sialidases from zebrafish (Danio rerio).CPDadh: a new peptidase family homologous to the cysteine protease domain in bacterial MARTX toxins.Expression, mutagenesis and kinetic analysis of recombinant K1E endosialidase to define the site of proteolytic processing and requirements for catalysis.Listeria phage A511, a model for the contractile tail machineries of SPO1-related bacteriophages.Identification and analysis of four candidate symbiosis genes from 'Chlorochromatium aggregatum', a highly developed bacterial symbiosis.Including Functional Annotations and Extending the Collection of Structural Classifications of Protein Loops (ArchDB).Molecular characterization of a Penicillium chrysogenum exo-1,5-alpha-L-arabinanase that is structurally distinct from other arabinan-degrading enzymes.Novel pH-dependent regulation of human cytosolic sialidase 2 (NEU2) activities by siastatin B and structural prediction of NEU2/siastatin B complex.Structural and biochemical characterization of the Cutibacterium acnes exo-β-1,4-mannosidase that targets the N-glycan core of host glycoproteins

P2860

Q24646993-E101A52C-E1BE-428E-9237-D664F8F8FB72 Q24680479-490382F3-B0A0-4C3B-943A-94C8549D4D3B Q26746042-BECEC6F4-94E8-4FC0-9A7F-2EB62316BB5F Q26767157-4675C9DF-E368-463B-8F21-B1E5825F2979 Q27654035-421C27F6-D2AD-44B3-A1FD-877A7062B8A0 Q27682640-EE0D0254-A636-4C31-9377-8E31C1F36F4C Q28601400-C3442278-74D6-46E0-A389-ADE5A812FBFF Q30156980-9C6619B8-1E4A-4AC7-A3BF-6A5C74D09B65 Q30977865-4D2001B6-DE59-4B17-AA0A-D77D89FB2216 Q33481318-517245A8-35D9-4CB8-BDB4-AA1F650354C9 Q33527557-E42CB136-B2A8-4A78-AADA-E737C9CB9D73 Q33936133-40C0D37C-7A10-40B6-88A9-B313C2B93A49 Q34057081-908F69FA-936A-4B03-AFBB-464A4E469336 Q34062280-03A03017-B6A5-4CCB-8E3C-AAD5FF26D94F Q34379045-A8C7A1DB-B32F-4DD0-BC1E-1B4A1193A49C Q34406409-3CC36C55-0649-4ED7-9ADB-BD2B86DF5CA3 Q35130117-A8161A0E-994F-418E-859E-29FCF0E200F3 Q35206011-C11CA800-122B-4E5D-85C3-EC735296500F Q35328858-EC951413-6C9F-4136-AC23-CA288B933A0B Q36421495-360B754A-61F0-4A61-B1B2-22E3A2457733 Q36449555-D7299DC5-1283-433F-8929-D2D0A6ED521A Q37154334-04C79AAF-7931-4E49-9617-F0531B5A33B5 Q37283979-9D07630D-5940-418E-8D1A-0D3539B12EE4 Q38718907-54C5B7E5-7DB1-48DD-8BE4-4CC0B126FC9F Q39323730-2AF7415E-128A-41A1-B9B7-C1B2128463DE Q40866479-2C77A357-871C-4E7C-986D-9F940330B88D Q41826097-971A043A-E391-4FA9-BA0E-CBB307D977C0 Q41856688-5D845682-3F74-4B55-85B5-3CAC231DEC73 Q41892061-28D0CEEC-4D7B-4EF5-A69F-0318832EBC7B Q42228724-2F4F1CC1-D8F0-4E88-ADAA-96A26C6AA186 Q42594731-FF70AABB-5E8B-49D6-BB2E-FAA20F47D821 Q42959523-B017C0CE-7F70-4E3B-B804-599A876D8F8E Q44779091-F861DBD8-4B59-466E-990E-7A9487A286B0 Q46020642-501809A9-6603-4788-85A5-E08AD11D5AD2 Q58691505-3D43B591-95EC-4631-BEDB-8C8C3DF74F85

P2860

Sialidase-like Asp-boxes: sequence-similar structures within different protein folds

http://www.wikidata.org/entity/Q24644728

description

2001 nî lūn-bûn

@nan

2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2001年の論文

@ja

2001年論文

@yue

2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

@zh-mo

2001年論文

@zh-tw

2001年论文

@wuu

name

Sialidase-like Asp-boxes: sequence-similar structures within different protein folds

@ast

Sialidase-like Asp-boxes: sequence-similar structures within different protein folds

@en

Sialidase-like Asp-boxes: sequence-similar structures within different protein folds

@nl

type

label

Sialidase-like Asp-boxes: sequence-similar structures within different protein folds

@ast

Sialidase-like Asp-boxes: sequence-similar structures within different protein folds

@en

Sialidase-like Asp-boxes: sequence-similar structures within different protein folds

@nl

prefLabel

Sialidase-like Asp-boxes: sequence-similar structures within different protein folds

@ast

Sialidase-like Asp-boxes: sequence-similar structures within different protein folds

@en

Sialidase-like Asp-boxes: sequence-similar structures within different protein folds

@nl

P1433

Q24644728-9DF943BC-5722-4DC6-A4EA-FA46BBAE5DCA

P1476

Q24644728-CB8DA2E2-FCBA-431C-AFC9-811A7D68DC60

P2093

Q24644728-5AD004D3-0662-4E22-9CCB-66F0FF7D1ABC

Q24644728-6BE096D4-2462-4BD9-A59B-E484A4F00C26

Q24644728-7B47C692-5211-4BED-B9B7-75068BA751A4

P2860

Q24644728-03588A74-8008-45C4-974E-959E263BBD5A

Q24644728-0CBFF278-51F7-45E0-8A4A-99D15BB9E44B

Q24644728-134E13B7-D6CE-4018-BCCF-77801E11CEFC

Q24644728-1B860672-8AB1-4264-BEEC-6B8AD3FE35C6

Q24644728-25F146CA-7C74-4B20-A812-84E4084F662C

Q24644728-2D344267-5456-4D02-9A93-772381CF1E5F

Q24644728-39ECFE14-FF8F-4200-850B-EF0C22E3FEDF

Q24644728-3B53CD35-9251-4090-A7D1-93AC34AD5D62

Q24644728-3BE46514-C2EA-4698-A944-64D71C869F8F

Q24644728-4A9D6E50-61F9-404B-8DB7-73F63FF00B11

P304

Q24644728-D282AE1A-1D8A-4C00-9787-35C0F8F78AED

P31

Q24644728-70474BD0-A594-47AE-AE42-74636B352D10

P3181

Q24644728-C6C7A897-96F9-4A2F-BE09-A733A32E87F6

P356

Q24644728-91E559C9-63F7-4870-9553-0D04E3456892

P407

Q24644728-164C87B6-3B4B-49E2-B039-01D0BABBBD45

P433

Q24644728-4BA1E5C7-2064-42E5-BFCC-2BD31FB88A09

P478

Q24644728-900F2562-25F9-4C70-A5D9-75966FE552A8

P577

Q24644728-410F075D-3F49-4B11-8420-C0328924114C

P5875

Q24644728-AFB0434D-B044-445A-AE76-9183C09DAA75

P698

Q24644728-A0DAB708-A186-4CB9-A0FA-F4BC9D3E2457

P921

Q24644728-0B51469D-C09E-41C1-A072-9E751EE2750F

P932

Q24644728-57F4B26B-46CC-416A-95AD-39A5E5C856E7

P3181

P356

P1433

Protein Science

P1476

Sialidase-like Asp-boxes: sequence-similar structures within different protein folds

@en

P2093

C P Ponting

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

R B Russell

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

R R Copley

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

P2860

The 100-kDa neurotensin receptor is gp95/sortilin, a non-G-protein-coupled receptor

Reelin is a ligand for lipoprotein receptors

Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Conserved water molecules in a large family of microbial ribonucleases

Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold

Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A

The Pfam protein families database.

Mapping the protein universe

Chain reversals in proteins

P304

285-92

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

P31

scholarly article

P3181

1221509

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

P356

10.1110/PS.31901

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

P407

P433

2

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

P478

10

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

P577

2001-02-01T00:00:00Z

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

P5875

12065648

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

P698

11266614

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

P921

protein folding

P932

2373934

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