scholarly journals Role of the nucleotide-binding domain, leucine rich containing (NLR) proteins in glioblastoma angiogenesis

IBRO Reports ◽  
2019 ◽  
Vol 6 ◽  
pp. S307-S308
Author(s):  
Shivanjali Saxena ◽  
Sushmita Jha
FEBS Journal ◽  
2015 ◽  
Vol 282 (19) ◽  
pp. 3799-3807 ◽  
Author(s):  
Yanhui Cao ◽  
Dongsheng Fei ◽  
Mingwei Chen ◽  
Miao Sun ◽  
Jun Xu ◽  
...  

2017 ◽  
Vol 11 (2) ◽  
pp. 57-72 ◽  
Author(s):  
Brian M. Inouye ◽  
Francis M. Hughes,Jr ◽  
Stephanie J. Sexton ◽  
J. Todd Purves

Irritative voiding symptoms (e.g. increased frequency and urgency) occur in many common pathologic conditions such as urinary tract infections and bladder outlet obstruction, and these conditions are well-established to have underlying inflammation that directly triggers these symptoms. However, it remains unclear as to how such diverse stimuli individually generate a common inflammatory process. Jürg Tschopp provided substantial insight into this conundrum when, working with extracts from THP-1 cells, he reported the existence of the inflammasome. He described it as a structure that senses multiple diverse signals from intracellular/extracellular sources and pathogens and triggers inflammation by the maturation and release of the pro-inflammatory cytokines interleukin-1β and interleukin-18. Recently, many of these sensors were found in the bladder and the nucleotide-binding domain, leucine-rich-containing family, pyrin domain-containing-3, has been shown to be a central mediator of inflammation in several urological diseases. In this review, we introduce the nucleotide-binding domain, leucine-rich-containing family, pyrin domaincontaining-3 inflammasome, highlight its emerging role in several common urologic conditions, and speculate on the potential involvement of other inflammasomes in bladder pathology.


2011 ◽  
Vol 17 (3) ◽  
pp. 361-373 ◽  
Author(s):  
Łukasz Nowicki ◽  
Paweł Leźnicki ◽  
Ewa Morawiec ◽  
Natalia Litwińczuk ◽  
Krzysztof Liberek

Toxins ◽  
2019 ◽  
Vol 11 (3) ◽  
pp. 172 ◽  
Author(s):  
Daniel Pinos ◽  
María Martínez-Solís ◽  
Salvador Herrero ◽  
Juan Ferré ◽  
Patricia Hernández-Martínez

ABC proteins are primary-active transporters that require the binding and hydrolysis of ATP to transport substrates across the membrane. Since the first report of an ABCC2 transporter as receptor of Cry1A toxins, the number of ABC transporters known to be involved in the mode of action of Cry toxins has increased. In Spodoptera exigua, a mutation in the SeABCC2 gene is described as genetically linked to resistance to the Bt-product XentariTM. This mutation affects an intracellular domain involved in ATP binding, but not the extracellular loops. We analyzed whether this mutation affects the role of the SeABCC2 as a functional receptor to Cry1A toxins. The results show that Sf21 cells expressing the truncated form of the transporter were susceptible to Cry1A toxins. Moreover, specific Cry1Ac binding was observed in those cells expressing the truncated SeABCC2. Additionally, no differences in the irreversible Cry1Ac binding component (associated with the toxin insertion into the membrane) were observed when tested in Sf21 cells expressing either the full-length or the truncated form of the SeABCC2 transporter. Therefore, our results point out that the partial lack of the nucleotide binding domain II in the truncated transporter does not affect its functionality as a Cry1A receptor.


Inflammation ◽  
2020 ◽  
Vol 43 (4) ◽  
pp. 1561-1571 ◽  
Author(s):  
Minghao Luo ◽  
Jiayu Meng ◽  
Jianghong Yan ◽  
Feifei Shang ◽  
Ting Zhang ◽  
...  

2010 ◽  
Vol 66 (9) ◽  
pp. 979-987 ◽  
Author(s):  
Matthias Haffke ◽  
Anja Menzel ◽  
Yvonne Carius ◽  
Dieter Jahn ◽  
Dirk W. Heinz

The human ATP-binding cassette (ABC) transporter ABCB6 is involved in haem-precursor transport across the mitochondrial membrane. The crystal structure of its nucleotide-binding domain (NBD) has been determined in the apo form and in complexes with ADP, with ADP and Mg2+ and with ATP at high resolution. The overall structure is L-shaped and consists of two lobes, consistent with other reported NBD structures. Nucleotide binding is mediated by the highly conserved Tyr599 and the Walker A motif, and induces notable structural changes. Structural comparison with other structurally characterized NBDs and full-length ABC transporters gives the first insight into the possible catalytic mechanism of ABCB6 and the role of the N-terminal helix α1 in full-length ABCB6.


1983 ◽  
Vol 258 (10) ◽  
pp. 6450-6457 ◽  
Author(s):  
P Argos ◽  
M Hanei ◽  
J M Wilson ◽  
W N Kelley

Sign in / Sign up

Export Citation Format

Share Document