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In: Adelphi series, Band 61, Heft 490-492, S. 6-6
ISSN: 1944-558X
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In: Adelphi series, Band 61, Heft 490-492, S. 6-6
ISSN: 1944-558X
In: Current anthropology, Band 62, Heft 5, S. 657-667
ISSN: 1537-5382
In: Journal of the International AIDS Society, Band 24, Heft S7
ISSN: 1758-2652
In: A Current Bibliography on African Affairs, Band 54, Heft 2, S. 167-177
ISSN: 2376-6662
In: Journal of the International AIDS Society, Band 24, Heft S6
ISSN: 1758-2652
In: Journal of the International AIDS Society, Band 24, Heft S5
ISSN: 1758-2652
In: A Current Bibliography on African Affairs, Band 54, Heft 1, S. 65-75
ISSN: 2376-6662
In: Journal of the International AIDS Society, Band 24, Heft S3
ISSN: 1758-2652
In: Journal of the International AIDS Society, Band 24, Heft S2
ISSN: 1758-2652
In: A Current Bibliography on African Affairs, Band 53, Heft 4, S. 362-372
ISSN: 2376-6662
In: A Current Bibliography on African Affairs, Band 53, Heft 3, S. 261-271
ISSN: 2376-6662
In: Journal of civil and human rights, Band 7, Heft 2, S. 104-107
ISSN: 2378-4253
In: International journal of intelligence and counterintelligence, Band 34, Heft 2, S. 298-299
ISSN: 1521-0561
Semaphorin 3A (Sema3A) is a cell-secreted protein that participates in the axonal guidance pathways. Sema3A acts as a canonical repulsive axon guidance molecule, inhibiting CNS regenerative axonal growth and propagation. Therefore, interfering with Sema3A signaling is proposed as a therapeutic target for achieving functional recovery after CNS injuries. It has been shown that Sema3A adheres to the proteoglycan component of the extracellular matrix (ECM) and selectively binds to heparin and chondroitin sulfate-E (CS-E) glycosaminoglycans (GAGs). We hypothesize that the biologically relevant interaction between Sema3A and GAGs takes place at Sema3A C-terminal polybasic region (SCT). The aims of this study were to characterize the interaction of the whole Sema3A C-terminal polybasic region (Sema3A 725–771) with GAGs and to investigate the disruption of this interaction by small molecules. Recombinant Sema3A basic domain was produced and we used a combination of biophysical techniques (NMR, SPR, and heparin affinity chromatography) to gain insight into the interaction of the Sema3A C-terminal domain with GAGs. The results demonstrate that SCT is an intrinsically disordered region, which confirms that SCT binds to GAGs and helps to identify the specific residues involved in the interaction. NMR studies, supported by molecular dynamics simulations, show that a new peptoid molecule (CSIC02) may disrupt the interaction between SCT and heparin. Our structural study paves the way toward the design of new molecules targeting these protein–GAG interactions with potential therapeutic applications. ; This work was funded by the European Union Seventh Framework Programme (FP7/2007–2013) under Project VISION, grant No. 304884, the Spanish Ministry of Science and Innovation/Spanish Research Agency (MCI/AEI/FEDER, RTI2018–096182-B-I00) and AGAUR (2017 SGR 208). ; Peer reviewed
BASE
In: Review of Pacific Basin Financial Markets and Policies, Band 24, Heft 4
ISSN: 1793-6705