TIMP1 preserves the blood–brain barrier through interacting with CD63/integrin  1 complex and regulating downstream FAK/RhoA signaling

Tang, Jingshu; Kang, Yuying; Huang, Long; Wu, Lei; Peng, Ying

doi:10.1016/j.apsb.2020.02.015

Cited by 71 publications

(53 citation statements)

References 67 publications

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“…The CoV N binds the viral RNA strand into a long helical structure attached to the membrane (M) protein [ 85 ]. There are nine SARS-CoV-2 X-ray structures of N protein, but only one crystal structure is published until now (PDB ID 6M3M) [ 33 ]. Similar to the N proteins of other CoVs, the SARS-CoV-2N protein consists of the N-terminal RNA-binding domain (N-NTD), the C-terminal dimerization domain (N-CTD), and a Ser/Arg rich linker [ 86 ].…”

Section: Sars-cov-2 Inhibitorsmentioning

confidence: 99%

“…The SARS-CoV-2N structures available are not co-crystallized with any inhibitor, but the Kang et al . structural study demonstrated that the SARS-CoV-2N employs a unique pattern for ribonucleotide binding, the residues Arg89 being one reason for the weak guanosine base recognition (K D for guanosine monophosphate GMP is 8 mmol/L) [ 33 ]. The Kang et al .…”

Section: Sars-cov-2 Inhibitorsmentioning

confidence: 99%

“…findings 4KXJ ; are considered all types of interactions—van der Waals, hydrogen bonds, carbon hydrogen bonds, and hydrophobic interactions; the striking differences between the two N sequences observed by the Kang et al . are marked in yellow background; the AMP-binding residues are underlined; in red is marked the Tyr residue whose mutation Y110A leads to a significant decrease of Kd for RNA binding [ 33 ]; with dot “.” are marked the semi-conservative replacements; with colon “:” are marked the conservative replacements; with “*” are marked the identities of the residues …”

Section: Sars-cov-2 Inhibitorsmentioning

confidence: 99%

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An Overview of the Crystallized Structures of the SARS-CoV-2

Ionescu

2020

Protein J

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Many research teams all over the world focus their research on the SARS-CoV-2, the new coronavirus that causes the so-called COVID-19 disease. Most of the studies identify the main protease or 3C-like protease (M pro /3CL pro ) as a valid target for large-spectrum inhibitors. Also, the interaction of the human receptor angiotensin-converting enzyme 2 (ACE2) with the viral surface glycoprotein (S) is studied in depth. Structural studies tried to identify the residues responsible for enhancement/weaken virus-ACE2 interactions or the cross-reactivity of the neutralizing antibodies. Although the understanding of the immune system and the hyper-inflammatory process in COVID-19 are crucial for managing the immediate and the long-term consequences of the disease, not many X-ray/NMR/cryo-EM crystals are available. In addition to 3CL pro , the crystal structures of other nonstructural proteins offer valuable information for elucidating some aspects of the SARS-CoV-2 infection. Thus, the structural analysis of the SARS-CoV-2 is currently mainly focused on three directions—finding M pro /3CL pro inhibitors, the virus-host cell invasion, and the virus-neutralizing antibody interaction. Electronic supplementary material The online version of this article (10.1007/s10930-020-09933-w) contains supplementary material, which is available to authorized users.

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Section: Sars-cov-2 Inhibitorsmentioning

confidence: 99%

Section: Sars-cov-2 Inhibitorsmentioning

confidence: 99%

Section: Sars-cov-2 Inhibitorsmentioning

confidence: 99%

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An Overview of the Crystallized Structures of the SARS-CoV-2

Ionescu

2020

Protein J

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“…Brilha et al have shown that increased MMP-9 activity disrupts the tight junction of the BBB and decreases expression of the tight junction proteins in a coculture model of the BBB [ 58 ]. MMP-9 activity is also regulated by an endogenous tissue inhibitor of metalloproteinase-1 (TIMP-1), which preserves the BBB integrity by inhibiting the enzymatic activity of MMP-9 [ 59 ].…”

Section: Roles Of Opn In the Pathogenesis Of Wnvmentioning

confidence: 99%

The Roles of Osteopontin in the Pathogenesis of West Nile Encephalitis

Nazneen

Bai

2020

Vaccines

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Osteopontin (OPN), a multifunctional protein encoded by the secreted phosphoprotein-1 (Spp-1) gene in humans, plays important roles in a variety of physiological conditions, such as biomineralization, bone remodeling and immune functions. OPN also has significant roles in the pathogenesis of autoimmune, allergy and inflammatory diseases, as well as bacterial, fungal and viral infections. West Nile virus (WNV), a mosquito-transmitted flavivirus, is the leading agent for viral encephalitis in North America. Recent progress has been made in understanding both the biological functions of OPN and the pathogenesis of WNV. In this review article, we have summarized the current understanding of the biology of OPN and its vital roles in the pathogenesis of WNV encephalitis.

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“…The genome of the virus is segmented into three parts; ORF1a/b region, which compasses most of the non-structural proteins (nsp) is the first part. The rest parts of the virus genome encode accessory proteins and four essential structural proteins, including spike (S) glycoprotein, small envelope (E) protein, matrix (M) protein, and nucleocapsid (N) protein (Kang et al 2020 ).…”

Section: Introductionmentioning

confidence: 99%