The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding.

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The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding.

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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年学术文章

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2017年學術文章

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The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding.

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The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding.

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The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding.

@en

The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding.

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The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding.

@en

The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding.

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P1476

The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding.

@en

P2093

Caroline Rajiv

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Elan Z Eisenmesser

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S RaElle Jackson

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Simon Cocklin

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P2860

Classification of intrinsically disordered regions and proteins

The crystal structure of PPIL1 bound to cyclosporine A suggests a binding mode for a linear epitope of the SKIP protein

Identification of a PRPF4 loss-of-function variant that abrogates U4/U6.U5 tri-snRNP integration and is associated with retinitis pigmentosa

The 20kD protein of human [U4/U6.U5] tri-snRNPs is a novel cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD proteins

Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression

A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs

Two protein-protein interaction sites on the spliceosome-associated human cyclophilin CypH

A detailed history of intron-rich eukaryotic ancestors inferred from a global survey of 100 complete genomes

Origin and evolution of spliceosomal introns

Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide

P304

3689-3704

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P31

scholarly article

P356

10.1042/BCJ20170366

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P407

English

P433

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P478

474

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P50

Tara L. Davis

P577

2017-09-21T00:00:00Z

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P698

28935721

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P921

Spliceosome

P932

5682932

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