The Stoichiometric Interaction of the Hsp90-Sgt1-Rar1 Complex by CD and SRCD Spectroscopy.

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The Stoichiometric Interaction of the Hsp90-Sgt1-Rar1 Complex by CD and SRCD Spectroscopy.

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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年学术文章

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2017年學術文章

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The Stoichiometric Interaction ...... x by CD and SRCD Spectroscopy.

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The Stoichiometric Interaction ...... x by CD and SRCD Spectroscopy.

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Item

label

The Stoichiometric Interaction ...... x by CD and SRCD Spectroscopy.

@en

The Stoichiometric Interaction ...... x by CD and SRCD Spectroscopy.

@nl

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The Stoichiometric Interaction ...... x by CD and SRCD Spectroscopy.

@en

The Stoichiometric Interaction ...... x by CD and SRCD Spectroscopy.

@nl

P1476

The Stoichiometric Interaction ...... x by CD and SRCD Spectroscopy.

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P2093

Giuliano Siligardi

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

Minghao Zhang

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P2860

Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes

SGT1 is essential for Nod1 activation

The 'active life' of Hsp90 complexes

Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain

Structural Basis for Assembly of Hsp90-Sgt1-CHORD Protein Complexes: Implications for Chaperoning of NLR Innate Immunity Receptors

Coiled-coil domain-dependent homodimerization of intracellular barley immune receptors defines a minimal functional module for triggering cell death

Structural and Functional Analysis of a Plant Resistance Protein TIR Domain Reveals Interfaces for Self-Association, Signaling, and Autoregulation

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

Structural and functional analysis of SGT1-HSP90 core complex required for innate immunity in plants.

Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p.

P304

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scholarly article

P356

10.3389/FMOLB.2017.00095

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P478

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P50

Chrisostomos Prodromou

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2017-01-01T00:00:00Z

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P698

29387685

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P932

5776081

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