Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.

about

Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure.Structure, function, and mechanism of proline utilization A (PutA).The science is in the data.A universal mammalian vaccine cell line substrate.The Proline Cycle As a Potential Cancer Therapy Target.

P2860

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P2860

Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.

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http://www.wikidata.org/entity/Q38930501

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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name

Resolving the cofactor-binding ...... ine-5-carboxylate reductase 1.

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type

Item

label

Resolving the cofactor-binding ...... ine-5-carboxylate reductase 1.

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Resolving the cofactor-binding ...... ine-5-carboxylate reductase 1.

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P1476

Resolving the cofactor-binding ...... line-5-carboxylate reductase 1

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P2093

Ashley C Campbell

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

Donald F Becker

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

Emily M Christensen

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

Kurt L Krause

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

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7233-7243

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scholarly article

P356

10.1074/JBC.M117.780288

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English

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P478

292

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P50

David A. Korasick

John J Tanner

Sagar M Patel

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2017-03-03T00:00:00Z

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28258219

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5409489

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Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.

about

P2860

P2860

Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932