The structures of the PII proteins from the cyanobacteria Synechococcus sp. PCC 7942 and Synechocystis sp. PCC 6803

The structures of the PII proteins from the cyanobacteria Synechococcus sp. PCC 7942 and Synechocystis sp. PCC 6803

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http://www.wikidata.org/entity/Q27642669
Inhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96 AStructure of GlnK1 with bound effectors indicates regulatory mechanism for ammonia uptakeThe crystal structure of the Escherichia coli AmtB-GlnK complex reveals how GlnK regulates the ammonia channelThe 2.2 Å resolution crystal structure ofBacillus cereusNif3-family protein YqfO reveals a conserved dimetal-binding motif and a regulatory domainThe crystal structure of the complex of PII and acetylglutamate kinase reveals how PII controls the storage of nitrogen as arginineStructure of putative CutA1 fromHomo sapiensdetermined at 2.05 Å resolutionCrystal structures of the apo and ATP bound Mycobacterium tuberculosis nitrogen regulatory PII proteinMechanism of 2-oxoglutarate signaling by the Synechococcus elongatus PII signal transduction proteinStructural Basis and Target-specific Modulation of ADP Sensing by the Synechococcus elongatus PII Signaling ProteinComplex structure and biochemical characterization of the Staphylococcus aureus cyclic diadenylate monophosphate (c-di-AMP)-binding protein PstA, the founding member of a new signal transduction protein family.Interactions between the nitrogen signal transduction protein PII and N-acetyl glutamate kinase in organisms that perform oxygenic photosynthesis.From PII signaling to metabolite sensing: a novel 2-oxoglutarate sensor that details PII-NAGK complex formation.A PII-Like Protein Regulated by Bicarbonate: Structural and Biochemical Studies of the Carboxysome-Associated CPII Protein.Identification of Rhodospirillum rubrum GlnB variants that are altered in their ability to interact with different targets in response to nitrogen status signals.Population shift of binding pocket size and dynamic correlation analysis shed new light on the anticooperative mechanism of PII proteinStructure of the PII signal transduction protein of Neisseria meningitidis at 1.85 A resolution.Coordinating carbon and nitrogen metabolic signaling through the cyanobacterial global repressor NdhR.
P2860

The structures of the PII proteins from the cyanobacteria Synechococcus sp. PCC 7942 and Synechocystis sp. PCC 6803

Item
http://www.wikidata.org/entity/Q27642669
description
2003 nî lūn-bûn
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2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
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2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված
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2003年の論文
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2003年論文
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2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
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name
The structures of the PII prot ...... and Synechocystis sp. PCC 6803
@ast
The structures of the PII prot ...... and Synechocystis sp. PCC 6803
@en
The structures of the PII prot ...... and Synechocystis sp. PCC 6803
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type
label
The structures of the PII prot ...... and Synechocystis sp. PCC 6803
@ast
The structures of the PII prot ...... and Synechocystis sp. PCC 6803
@en
The structures of the PII prot ...... and Synechocystis sp. PCC 6803
@nl
prefLabel
The structures of the PII prot ...... and Synechocystis sp. PCC 6803
@ast
The structures of the PII prot ...... and Synechocystis sp. PCC 6803
@en
The structures of the PII prot ...... and Synechocystis sp. PCC 6803
@nl
P1433
P1476
P2093
P304
P31
P433
P478
P50
P577
P698
P921
P1433
P1476
The structures of the PII prot ...... and Synechocystis sp. PCC 6803
@en
P2093
P304
P31
P433
P478
P50
P577
P698
P921