The subcortical maternal complex protein Nlrp4f is involved in cytoplasmic lattice formation and organelle distribution

The production of void lattices in metals as a result of displacement damage associated with high energy and heavy ion bombardment is now well documented. More recently, Murr has shown that a void lattice can be developed in natural (colored) fluorites observed in the transmission electron microscope. These were the first observations of a void lattice in an irradiated nonmetal, and the first, direct observations of color-center aggregates. Clinard, et al. have also recently observed a void lattice (described as a high density of aligned "pores") in neutron irradiated Al2O3 and Y2O3. In this latter work, itwas pointed out that in order that a cavity be formed,a near-stoichiometric ratio of cation and anion vacancies must aggregate. It was reasoned that two other alternatives to explain the pores were cation metal colloids and highpressure anion gas bubbles.Evans has proposed that void lattices result from the presence of a pre-existing impurity lattice, and predicted that the formation of a void lattice should restrict swelling in irradiated materials because it represents a state of saturation.

Nuclear Pore Complex Protein Nup98

10.32388/b1of6f ◽

2020 ◽

Author(s):

Keyword(s):

Nuclear Pore Complex ◽

Nuclear Pore ◽

Complex Protein

Faculty Opinions recommendation of Characterisation of the gene encoding a protective antigen from Babesia microti identified it as eta subunit of chaperonin containing T-complex protein 1.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1002445.27154 ◽

2001 ◽

Author(s):

David Persing

Keyword(s):

Protective Antigen ◽

Babesia Microti ◽

Gene Encoding ◽

T Complex ◽

Complex Protein

Faculty Opinions recommendation of Carrier ampholyte-free solution isoelectric focusing as a prefractionation method for the proteomic analysis of complex protein mixtures.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1015856.198857 ◽

2003 ◽

Author(s):

Visith Thongboonkerd

Keyword(s):

Isoelectric Focusing ◽

Proteomic Analysis ◽

Free Solution ◽

Carrier Ampholyte ◽

Complex Protein

Faculty Opinions recommendation of Allergenicity resulting from functional mimicry of a Toll-like receptor complex protein.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1139090.604420 ◽

2009 ◽

Author(s):

Philipp M Lepper ◽

Kathy Triantafilou

Keyword(s):

Receptor Complex ◽

Toll Like Receptor ◽

Complex Protein

Faculty Opinions recommendation of Crystal structure of γ-tubulin complex protein GCP4 provides insight into microtubule nucleation.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.11917958.13033056 ◽

2011 ◽

Author(s):

Berl R Oakley

Keyword(s):

Crystal Structure ◽

Microtubule Nucleation ◽

Complex Protein ◽

Insight Into

Faculty Opinions recommendation of A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.718145210.793485392 ◽

2013 ◽

Author(s):

Cheng-Ming Chiang

Keyword(s):

Nuclear Pore Complex ◽

Nuclear Pore ◽

Complex Protein

Faculty Opinions recommendation of Linear motif-mediated interactions have contributed to the evolution of modularity in complex protein interaction networks.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.720591107.793501202 ◽

2015 ◽

Author(s):

Gary Bader ◽

Mohamed Helmy

Keyword(s):

Protein Interaction ◽

Protein Interaction Networks ◽

Interaction Networks ◽

Linear Motif ◽

Complex Protein

Mechanism of the small ATP-independent chaperone Spy is substrate specific

Nature Communications ◽

10.1038/s41467-021-21120-8 ◽

2021 ◽

Vol 12 (1) ◽

Author(s):

Rishav Mitra ◽

Varun V. Gadkari ◽

Ben A. Meinen ◽

Carlo P. M. van Mierlo ◽

Brandon T. Ruotolo ◽

...

Keyword(s):

Relative Affinity ◽

Complex Protein ◽

Partially Unfolded ◽

Substrate Proteins ◽

Partially Unfolded States

AbstractATP-independent chaperones are usually considered to be holdases that rapidly bind to non-native states of substrate proteins and prevent their aggregation. These chaperones are thought to release their substrate proteins prior to their folding. Spy is an ATP-independent chaperone that acts as an aggregation inhibiting holdase but does so by allowing its substrate proteins to fold while they remain continuously chaperone bound, thus acting as a foldase as well. The attributes that allow such dual chaperoning behavior are unclear. Here, we used the topologically complex protein apoflavodoxin to show that the outcome of Spy’s action is substrate specific and depends on its relative affinity for different folding states. Tighter binding of Spy to partially unfolded states of apoflavodoxin limits the possibility of folding while bound, converting Spy to a holdase chaperone. Our results highlight the central role of the substrate in determining the mechanism of chaperone action.

Breakdown of Filamentous Myofibrils by the UPS–Step by Step

Biomolecules ◽

10.3390/biom11010110 ◽

2021 ◽

Vol 11 (1) ◽

pp. 110

Author(s):

Dina Aweida ◽

Shenhav Cohen

Keyword(s):

Protein Quality ◽

Protein Structures ◽

Ubiquitin Proteasome System ◽

Surface Proteins ◽

Catalytic Core ◽

Complex Protein ◽

Ubiquitin Proteasome ◽

Aaa Atpases

Protein degradation maintains cellular integrity by regulating virtually all biological processes, whereas impaired proteolysis perturbs protein quality control, and often leads to human disease. Two major proteolytic systems are responsible for protein breakdown in all cells: autophagy, which facilitates the loss of organelles, protein aggregates, and cell surface proteins; and the ubiquitin-proteasome system (UPS), which promotes degradation of mainly soluble proteins. Recent findings indicate that more complex protein structures, such as filamentous assemblies, which are not accessible to the catalytic core of the proteasome in vitro, can be efficiently degraded by this proteolytic machinery in systemic catabolic states in vivo. Mechanisms that loosen the filamentous structure seem to be activated first, hence increasing the accessibility of protein constituents to the UPS. In this review, we will discuss the mechanisms underlying the disassembly and loss of the intricate insoluble filamentous myofibrils, which are responsible for muscle contraction, and whose degradation by the UPS causes weakness and disability in aging and disease. Several lines of evidence indicate that myofibril breakdown occurs in a strictly ordered and controlled manner, and the function of AAA-ATPases is crucial for their disassembly and loss.