NlpC/P60 domain-containing proteins of Mycobacterium avium subspecies paratuberculosis that differentially bind and hydrolyze peptidoglycan. - Test2 - elhamkhani - TriplyDB

NlpC/P60 domain-containing proteins of Mycobacterium avium subspecies paratuberculosis that differentially bind and hydrolyze peptidoglycan.

NlpC/P60 domain-containing proteins of Mycobacterium avium subspecies paratuberculosis that differentially bind and hydrolyze peptidoglycan.

http://www.wikidata.org/entity/Q37085726

about

Transcriptomic analysis of human norovirus NS1-2 protein highlights a multifunctional role in murine monocytes Identification of sero-reactive antigens for the early diagnosis of Johne's disease in cattle.

P2860

Q30397112-6FBD8A40-9577-427E-A65B-D8198C782C62 Q40070611-8771D411-5D1E-404F-B5B7-04068DB353DC

P2860

NlpC/P60 domain-containing proteins of Mycobacterium avium subspecies paratuberculosis that differentially bind and hydrolyze peptidoglycan.

http://www.wikidata.org/entity/Q37085726

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 22 January 2016

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

NlpC/P60 domain-containing pro ...... d and hydrolyze peptidoglycan.

@en

NlpC/P60 domain-containing pro ...... d and hydrolyze peptidoglycan.

@nl

type

label

NlpC/P60 domain-containing pro ...... d and hydrolyze peptidoglycan.

@en

NlpC/P60 domain-containing pro ...... d and hydrolyze peptidoglycan.

@nl

prefLabel

NlpC/P60 domain-containing pro ...... d and hydrolyze peptidoglycan.

@en

NlpC/P60 domain-containing pro ...... d and hydrolyze peptidoglycan.

@nl

P1433

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Q37085726-B267CD33-4CEA-46CB-B135-9303CA800F13

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Q37085726-0E8F5446-B4B8-45C9-9375-4A44AD60EF4F

Q37085726-1AB702DE-8AB0-4F6F-88BE-9788AD77D58E

Q37085726-4989C2A1-BFD8-4F52-83BF-FB21BB427F3E

Q37085726-9AC8A833-4AB1-4297-819F-5275DBD52D89

Q37085726-BAE78924-4805-411F-81FC-A4A5A92B1005

Q37085726-BB40F02C-CA3C-4001-A6A3-53439D237F4F

Q37085726-D6DD44D7-BC97-47A5-8DE2-AFA9507B142A

P2860

Q37085726-055553DA-B6A6-4C8B-ADB1-4F5743D938D9

Q37085726-06189B54-958D-4F07-856E-ECF25EB959D1

Q37085726-0A76F4D2-2A9B-44E8-9E2E-DE7BEA93FED9

Q37085726-16316620-9185-491B-932A-09724096396F

Q37085726-17BE91B3-388D-4D8F-AB1A-0EEE182F3FDD

Q37085726-1B760A9B-77B0-49A6-BEBD-70786377D4D8

Q37085726-1FD10835-48E5-4CA1-A084-5AB1CC6996A5

Q37085726-1FD1DB25-9C35-4D8B-B5FA-E7E5A25BD2DB

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Q37085726-F98BD5B5-FE33-4E5A-8DE9-574BF38EF65E

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Q37085726-FC79FD10-D7A0-4F0E-9BCA-FB41919BAF89

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Q37085726-A45A19FA-650C-4D51-89C6-B1887DA74BC8

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Q37085726-FF0B6D9D-C570-4DB3-A0B0-C0595CE266CD

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Q37085726-DF000C46-A445-4E08-B953-60FA0541D0B5

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P1433

Protein Science

P1476

NlpC/P60 domain-containing pro ...... d and hydrolyze peptidoglycan.

@en

P2093

Brian V Geisbrecht

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

Cari K Lingle

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

Judith R Stabel

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

Kasra X Ramyar

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

Philip R Adam

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

William D Picking

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

William J McWhorter

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

P2860

The complete genome sequence of Mycobacterium avium subspecies paratuberculosis

Thiopurine drugs azathioprine and 6-mercaptopurine inhibit Mycobacterium paratuberculosis growth in vitro

Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes

Processing of X-ray diffraction data collected in oscillation mode

Structure of the γ- D -glutamyl- L -diamino acid endopeptidase YkfC from Bacillus cereus in complex with L -Ala-γ- D -Glu: insights into substrate recognition by NlpC/P60 cysteine peptidases

Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli: structural evidence for a novel cysteine peptidase catalytic triad

Peptidoglycan remodeling in Mycobacterium tuberculosis: comparison of structures and catalytic activities of RipA and RipB

Identification of the bile salt binding site on IpaD from Shigella flexneri and the influence of ligand binding on IpaD structure.

Structural and Biochemical Analyses of Mycobacterium tuberculosis N-Acetylmuramyl-L-alanine Amidase Rv3717 Point to a Role in Peptidoglycan Fragment Recycling

RipD (Rv1566c) from Mycobacterium tuberculosis: adaptation of an NlpC/p60 domain to a non-catalytic peptidoglycan-binding function

P304

840-851

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P31

scholarly article

P356

10.1002/PRO.2884

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P433

4

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P478

25

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P50

John P. Bannantine

P577

2016-01-22T00:00:00Z

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26799947

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4941221

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