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AAA+ proteins: have engine, will work.

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TLDR
The structural organization of AAA+ proteins, the conformational changes they undergo, the range of different reactions they catalyse, and the diseases associated with their dysfunction are reviewed.
Abstract
The AAA+ (ATPases associated with various cellular activities) family is a large and functionally diverse group of enzymes that are able to induce conformational changes in a wide range of substrate proteins. The family's defining feature is a structurally conserved ATPase domain that assembles into oligomeric rings and undergoes conformational changes during cycles of nucleotide binding and hydrolysis. Here, we review the structural organization of AAA+ proteins, the conformational changes they undergo, the range of different reactions they catalyse, and the diseases associated with their dysfunction.

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SNAREs--engines for membrane fusion.

TL;DR: A fascinating picture of these robust nanomachines is emerging, which seems to be conserved and adaptable for fusion reactions as diverse as those involved in cell growth, membrane repair, cytokinesis and synaptic transmission.
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The type III secretion injectisome.

TL;DR: The principal structural components of the injectisome, from the base located in the bacterial cytosol to the tip of the needle protruding from the cell surface, have been investigated in detail.
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The apoptosome: signalling platform of cell death

TL;DR: The formation of the apoptosome and the activation of its effector, caspase-9, reveals a sophisticated mechanism that might be more common than was initially thought.
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Chaperone machines for protein folding, unfolding and disaggregation

TL;DR: The structural basis of their mechanism of action is being unravelled and typically involves massive displacements of 20–30 kDa domains over distances of 20-50 Å and rotations of up to 100°.
Journal ArticleDOI

Function of Nod-like receptors in microbial recognition and host defense.

TL;DR: The role of Nod1 and Nod2 in host defense is focused on and recent finding regarding the role ofNlrc4, Nlpr1, and Nlrp3 inflammasomes in caspase‐1 activation and subsequent release of proinflammatory cytokines such as interleukin‐1β is discussed.
References
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Book

Membrane Fusion

Jan Wilschut
Journal ArticleDOI

AAA+: A Class of Chaperone-Like ATPases Associated with the Assembly, Operation, and Disassembly of Protein Complexes

TL;DR: Whole-genome analysis indicates that this class of proteins is ancient and has undergone considerable functional divergence prior to the emergence of the major divisions of life.
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The Ras-RasGAP Complex: Structural Basis for GTPase Activation and Its Loss in Oncogenic Ras Mutants

TL;DR: The structural arrangement in the active site is consistent with a mostly associative mechanism of phosphoryl transfer and provides an explanation for the activation of Ras by glycine-12 and glutamine-61 mutations.
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Hsp104, Hsp70, and Hsp40: A Novel Chaperone System that Rescues Previously Aggregated Proteins

TL;DR: It is concluded that Hsp104 has a protein remodeling activity that acts on trapped, aggregated proteins and requires specific interactions with conventional chaperones to promote refolding of the intermediates it produces.
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Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein.

TL;DR: Identification of VCP as causing IBMPFD has important implications for other inclusion-body diseases, including myopathies, dementias and Paget disease of bone (PDB), as it may define a new common pathological ubiquitin-based pathway.
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