Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase.

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Insights into the Phosphoryl Transfer Mechanism of Human Ubiquitous Mitochondrial Creatine Kinase Relating structure to mechanism in creatine kinase.The generation of the oxidized form of creatine kinase is a negative regulation on muscle creatine kinase.

P2860

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P2860

Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase.

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http://www.wikidata.org/entity/Q41954583

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2003 nî lūn-bûn

@nan

2003年の論文

@ja

2003年論文

@yue

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

@wuu

2003年论文

@zh

2003年论文

@zh-cn

name

Asparagine 285 plays a key rol ...... rabbit muscle creatine kinase.

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type

Item

label

Asparagine 285 plays a key rol ...... rabbit muscle creatine kinase.

@en

prefLabel

Asparagine 285 plays a key rol ...... rabbit muscle creatine kinase.

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P1476

Asparagine 285 plays a key rol ...... rabbit muscle creatine kinase

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P2093

Charles L Borders

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

Elikem R K Gbeddy

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

Guy B Mulligan

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

Katherine M MacGregor

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

Michael J Thomenius

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

Paul L Edmiston

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P2860

Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis

Crystal structure of brain-type creatine kinase at 1.41 Å resolution

Crystal structure of human ubiquitous mitochondrial creatine kinase

The three-dimensional structure of cytosolic bovine retinal creatine kinase

Structure of human muscle creatine kinase

Structure of mitochondrial creatine kinase

Transition state structure of arginine kinase: implications for catalysis of bimolecular reactions

Crystal structure of rabbit muscle creatine kinase

Induced fit in arginine kinase.

Structural changes induced by substrates and anions at the active site of creatine kinase. Electron paramagnetic resonance and nuclear magnetic relaxation rate studies of the manganous complexes.

P304

532-537

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scholarly article

P356

10.1110/PS.0230403

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P433

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

P478

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

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Mark J Snider

P577

2003-03-01T00:00:00Z

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P5875

8207784

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P698

12592023

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P932

2312435

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Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase.

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P2860

P2860

Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase.

description

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type

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P1433

P1476

P2093

P2860

P304

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P356

P433

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P5875

P698

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P1476

P2093

P2860

P304

P31

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P433

P478

P50

P577

P5875

P698

P932