Escherichia coli PII protein: purification, crystallization and oligomeric structure. - Wikidata - awgldk - TriplyDB

Escherichia coli PII protein: purification, crystallization and oligomeric structure.

Escherichia coli PII protein: purification, crystallization and oligomeric structure.

http://www.wikidata.org/entity/Q36761212

about

Structure of GlnK1 with bound effectors indicates regulatory mechanism for ammonia uptake Nitrogen assimilation in Escherichia coli: putting molecular data into a systems perspective The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction P(II) signal transduction proteins, pivotal players in microbial nitrogen control Coexistence of two structurally similar but functionally different PII proteins in Azospirillum brasilense.The Escherichia coli signal transducers PII (GlnB) and GlnK form heterotrimers in vivo: fine tuning the nitrogen signal cascade.P(II) signal transduction proteins: nitrogen regulation and beyond.The role of the T-loop of the signal transducing protein PII from Escherichia coli.Purification of P(II) and P(II)-UMP and in vitro studies of regulation of glutamine synthetase in Rhodospirillum rubrum.Uridylylation of the P(II) protein in the photosynthetic bacterium Rhodospirillum rubrum Nitrogen control in bacteria.Transposon mutations in the 5' end of glnD, the gene for a nitrogen regulatory sensor, that suppress the osmosensitive phenotype caused by otsBA lesions in Escherichia coli.The structure of the PII-ATP complex.The novel protein phosphatase PphA from Synechocystis PCC 6803 controls dephosphorylation of the signalling protein PII.

P2860

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P2860

Escherichia coli PII protein: purification, crystallization and oligomeric structure.

http://www.wikidata.org/entity/Q36761212

description

1994 nî lūn-bûn

@nan

1994年の論文

@ja

1994年論文

@yue

1994年論文

@zh-hant

1994年論文

@zh-hk

1994年論文

@zh-mo

1994年論文

@zh-tw

1994年论文

@wuu

1994年论文

@zh

1994年论文

@zh-cn

name

Escherichia coli PII protein: purification, crystallization and oligomeric structure.

@ast

Escherichia coli PII protein: purification, crystallization and oligomeric structure.

@en

type

label

Escherichia coli PII protein: purification, crystallization and oligomeric structure.

@ast

Escherichia coli PII protein: purification, crystallization and oligomeric structure.

@en

prefLabel

Escherichia coli PII protein: purification, crystallization and oligomeric structure.

@ast

Escherichia coli PII protein: purification, crystallization and oligomeric structure.

@en

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0014-5793(94)80203-3

P1433

P1476

Escherichia coli PII protein: purification, crystallization and oligomeric structure

@en

P2093

C Gedye

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

D L Ollis

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

E Cheah

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

P D Carr

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

P D Jeffrey

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

P M Suffolk

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

S G Vasudevan

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

P2860

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Solvent content of protein crystals

Matrix-assisted laser desorption ionization mass spectrometry with 2-(4-hydroxyphenylazo)benzoic acid matrix.

Covalent modification of the glnG product, NRI, by the glnL product, NRII, regulates the transcription of the glnALG operon in Escherichia coli.

Modulation of glutamine synthetase adenylylation and deadenylylation is mediated by metabolic transformation of the P II -regulatory protein.

Photosynthetic electron transport controls nitrogen assimilation in cyanobacteria by means of posttranslational modification of the glnB gene product.

Activation of Klebsiella pneumoniae and Rhizobium meliloti nitrogenase promoters by gln (ntr) regulatory proteins.

Current approaches to macromolecular crystallization.

Reversible phosphorylation of an enhancer binding protein regulates the transcription of bacterial nitrogen utilization genes.

P304

255-258

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P31

scholarly article

P356

10.1016/0014-5793(94)80203-3

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P433

3

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P478

337

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P50

Nicholas E. Dixon

P577

1994-01-01T00:00:00Z

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P5875

14905109

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P698

8293810

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