Log in

Relevant bibliographies by topics / Furin site / Journal articles

To see the other types of publications on this topic, follow the link: Furin site.

Journal articles on the topic 'Furin site'

Author: Grafiati

Published: 10 December 2022

Last updated: 31 July 2025

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Furin site.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Tian, Sun. "A 20 Residues Motif Delineates the Furin Cleavage Site and its Physical Properties May Influence Viral Fusion." Biochemistry Insights 2 (January 2009): BCI.S2049. http://dx.doi.org/10.4137/bci.s2049.

Full text

Abstract:

Furin is a proprotein convertase that proteolytically cleaves protein precursors to yield functional proteins. Efficient cleavage depends on the presence of a specific sequence motif on the substrate. Currently, the cleavage site motif is described as a four amino acid pattern: R-X-[K/R]-R⇓. However, not all furin cleavage recognition sites can be described by this pattern and not all R-X-[K/R]-R⇓ sites are cleaved by furin. Since many furin substrates are involved in the pathogenesis of viral infection and human diseases, it is important to accurately characterize the furin cleavage site moti

APA, Harvard, Vancouver, ISO, and other styles

2

Yamada, Yoshiyuki, and Ding Xiang Liu. "Proteolytic Activation of the Spike Protein at a Novel RRRR/S Motif Is Implicated in Furin-Dependent Entry, Syncytium Formation, and Infectivity of Coronavirus Infectious Bronchitis Virus in Cultured Cells." Journal of Virology 83, no. 17 (2009): 8744–58. http://dx.doi.org/10.1128/jvi.00613-09.

Full text

Abstract:

ABSTRACT The spike (S) protein of the coronavirus (CoV) infectious bronchitis virus (IBV) is cleaved into S1 and S2 subunits at the furin consensus motif RRFRR537/S in virus-infected cells. In this study, we observe that the S2 subunit of the IBV Beaudette strain is additionally cleaved at the second furin site (RRRR690/S) in cells expressing S constructs and in virus-infected cells. Detailed time course experiments showed that a peptide furin inhibitor, decanoyl-Arg-Val-Lys-Arg-chloromethylketone, blocked both viral entry and syncytium formation. Site-directed mutagenesis studies revealed tha

APA, Harvard, Vancouver, ISO, and other styles

3

Cheng, Jinlong, Ye Zhao, Gang Xu, et al. "The S2 Subunit of QX-type Infectious Bronchitis Coronavirus Spike Protein Is an Essential Determinant of Neurotropism." Viruses 11, no. 10 (2019): 972. http://dx.doi.org/10.3390/v11100972.

Full text

Abstract:

Some coronaviruses (CoVs) have an extra furin cleavage site (RRKR/S, furin-S2′ site) upstream of the fusion peptide in the spike protein, which plays roles in virion adsorption and fusion. Mutation of the S2′ site of QX genotype (QX-type) infectious bronchitis virus (IBV) spike protein (S) in a recombinant virus background results in higher pathogenicity, pronounced neural symptoms and neurotropism when compared with conditions in wild-type IBV (WT-IBV) infected chickens. In this study, we present evidence suggesting that recombinant IBV with a mutant S2′ site (furin-S2′ site) leads to higher

APA, Harvard, Vancouver, ISO, and other styles

4

Papa, Guido, Donna L. Mallery, Anna Albecka, et al. "Furin cleavage of SARS-CoV-2 Spike promotes but is not essential for infection and cell-cell fusion." PLOS Pathogens 17, no. 1 (2021): e1009246. http://dx.doi.org/10.1371/journal.ppat.1009246.

Full text

Abstract:

Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) infects cells by binding to the host cell receptor ACE2 and undergoing virus-host membrane fusion. Fusion is triggered by the protease TMPRSS2, which processes the viral Spike (S) protein to reveal the fusion peptide. SARS-CoV-2 has evolved a multibasic site at the S1-S2 boundary, which is thought to be cleaved by furin in order to prime S protein for TMPRSS2 processing. Here we show that CRISPR-Cas9 knockout of furin reduces, but does not prevent, the production of infectious SARS-CoV-2 virus. Comparing S processing in furin knockou

APA, Harvard, Vancouver, ISO, and other styles

5

Wanyiri, Jane W., Roberta O'Connor, Geneve Allison, et al. "Proteolytic Processing of the Cryptosporidium Glycoprotein gp40/15 by Human Furin and by a Parasite-Derived Furin-Like Protease Activity." Infection and Immunity 75, no. 1 (2006): 184–92. http://dx.doi.org/10.1128/iai.00944-06.

Full text

Abstract:

ABSTRACT The apicomplexan parasite Cryptosporidium causes diarrheal disease worldwide. Proteolytic processing of proteins plays a significant role in host cell invasion by apicomplexan parasites. In previous studies, we described gp40/15, a Cryptosporidium sp. glycoprotein that is proteolytically cleaved to yield two surface glycopeptides (gp40 and gp15), which are implicated in mediating infection of host cells. In the present study, we showed that biosynthetically labeled gp40/15 is processed in Cryptosporidium parvum-infected HCT-8 cells. We identified a putative furin cleavage site RSRR↓ i

APA, Harvard, Vancouver, ISO, and other styles

6

Siner, Joshua I., Julie M. Crudele, Courtney T. Connolly, et al. "Unexpected Role of PACE/Furin Cleavage Site in FVIII Biology: Implications for Hemophilia a Therapy." Blood 124, no. 21 (2014): 105. http://dx.doi.org/10.1182/blood.v124.21.105.105.

Full text

Abstract:

Abstract The paired basic amino acid cleaving enzyme (PACE)/Furin is a protein convertase system that plays a vital role in several biological processes, including coagulation. The propeptide processing of human FIX by PACE/Furin is a critical posttranslational modification, so cells co-expressing PACE/Furin and FIX are used for production of clinical recombinant protein. In the development of recombinant B-domain deleted (BDD) FVIII for hemophilia A (HA), a 14 amino acid B-domain sequence containing a putative cleavage site for PACE/Furin was retained because it was believed to be critical fo

APA, Harvard, Vancouver, ISO, and other styles

7

Geiselhart, Verena, Patrizia Bastone, Tore Kempf, Martina Schnölzer, and Martin Löchelt. "Furin-Mediated Cleavage of the Feline Foamy Virus Env Leader Protein." Journal of Virology 78, no. 24 (2004): 13573–81. http://dx.doi.org/10.1128/jvi.78.24.13573-13581.2004.

Full text

Abstract:

ABSTRACT The molecular biology of spuma or foamy retroviruses is different from that of the other members of the Retroviridae. Among the distinguishing features, the N-terminal domain of the foamy virus Env glycoprotein, the 16-kDa Env leader protein Elp, is a component of released, infectious virions and is required for particle budding. The transmembrane protein Elp specifically interacts with N-terminal Gag sequences during morphogenesis. In this study, we investigate the mechanism of Elp release from the Env precursor protein. By a combination of genetic, biochemical, and biophysical metho

APA, Harvard, Vancouver, ISO, and other styles

8

Cui, Yanzhen, Renee Hackenmiller, Linnea Berg, et al. "The activity and signaling range of mature BMP-4 is regulated by sequential cleavage at two sites within the prodomain of the precursor." Genes & Development 15, no. 21 (2001): 2797–802. http://dx.doi.org/10.1101/gad.940001.

Full text

Abstract:

Proteolytic maturation of proBMP-4 is required to generate an active signaling molecule. We show that proBMP-4 is cleaved by furin in a sequential manner. Cleavage at a consensus furin site adjacent to the mature ligand domain allows for subsequent cleavage at an upstream nonconsensus furin site within the prodomain. BMP-4 synthesized from precursor in which the upstream site is noncleavable is less active, signals at a shorter range, and accumulates at lower levels than does BMP-4 cleaved from native precursor. Conversely, BMP-4 cleaved from precursor in which both sites are rapidly cleaved i

APA, Harvard, Vancouver, ISO, and other styles

9

Kubo, Yoshinao, Manya Bakatumana Hans, Taisuke Nakamura, and Hideki Hayashi. "The Furin Protease Dependence and Antiviral GBP2 Sensitivity of Murine Leukemia Virus Infection Are Determined by the Amino Acid Sequence at the Envelope Glycoprotein Cleavage Site." International Journal of Molecular Sciences 25, no. 18 (2024): 9987. http://dx.doi.org/10.3390/ijms25189987.

Full text

Abstract:

Host restriction factor GBP2 suppresses the replication of the ecotropic Moloney murine leukemia virus (E-MLV) by inhibiting furin protease, which cleaves the viral envelope glycoprotein (Env) into surface (SU) and transmembrane (TM) subunits. We analyzed the impacts of GBP2 on the infection efficiency mediated by MLV Envs of different strains of ecotropic Moloney, polytropic Friend, amphotropic, and xenotropic MLV-related (XMRV) viruses. Interestingly, the Envs of ecotropic Moloney and polytropic Friend MLV were sensitive to the antiviral activity of GBP2, while XMRV and amphotropic Envs show

APA, Harvard, Vancouver, ISO, and other styles

10

Gendron, Fernand-Pierre, Sébastien Mongrain, Patrick Laprise, et al. "The CDX2 transcription factor regulates furin expression during intestinal epithelial cell differentiation." American Journal of Physiology-Gastrointestinal and Liver Physiology 290, no. 2 (2006): G310—G318. http://dx.doi.org/10.1152/ajpgi.00217.2005.

Full text

Abstract:

CDX2, a member of the caudal family of transcription factors, is involved in enterocyte lineage specification. CDX2 activates many intestine-specific genes, such as sucrase-isomaltase and lactase-phlorizin hydrolase (LPH), and adhesion proteins, namely, LI-cadherin and claudin-2. In this study, we show that the proprotein convertase furin, involved in proteolytic maturation of proprotein substrates including LPH and cell surface proteins, is a CDX2 target. Indeed, expression of the rat furin homolog was induced 1.5-fold, as determined by microarray experiments that compared control with CDX2-e

APA, Harvard, Vancouver, ISO, and other styles

11

Mjokane, Nozethu, Maphori Maliehe, Olufemi S. Folorunso, et al. "Cryptococcal Protease(s) and the Activation of SARS-CoV-2 Spike (S) Protein." Cells 11, no. 3 (2022): 437. http://dx.doi.org/10.3390/cells11030437.

Full text

Abstract:

In this contribution, we report on the possibility that cryptococcal protease(s) could activate the SARS-CoV-2 spike (S) protein. The S protein is documented to have a unique four-amino-acid sequence (underlined, SPRRAR↓S) at the interface between the S1 and S2 sites, that serves as a cleavage site for the human protease, furin. We compared the biochemical efficiency of cryptococcal protease(s) and furin to mediate the proteolytic cleavage of the S1/S2 site in a fluorogenic peptide. We show that cryptococcal protease(s) processes this site in a manner comparable to the efficiency of furin (p &

APA, Harvard, Vancouver, ISO, and other styles

12

Thomas, Gary, Frédéric Couture, and Anna Kwiatkowska. "The Path to Therapeutic Furin Inhibitors: From Yeast Pheromones to SARS-CoV-2." International Journal of Molecular Sciences 23, no. 7 (2022): 3435. http://dx.doi.org/10.3390/ijms23073435.

Full text

Abstract:

The spurious acquisition and optimization of a furin cleavage site in the SARS-CoV-2 spike protein is associated with increased viral transmission and disease, and has generated intense interest in the development and application of therapeutic furin inhibitors to thwart the COVID-19 pandemic. This review summarizes the seminal studies that informed current efforts to inhibit furin. These include the convergent efforts of endocrinologists, virologists, and yeast geneticists that, together, culminated in the discovery of furin. We describe the pioneering biochemical studies which led to the fir

APA, Harvard, Vancouver, ISO, and other styles

13

Galanopoulou, A. S., N. G. Seidah, and Y. C. Patel. "Direct role of furin in mammalian prosomatostatin processing." Biochemical Journal 309, no. 1 (1995): 33–40. http://dx.doi.org/10.1042/bj3090033.

Full text

Abstract:

We have previously reported that rat prosomatostatin (rPSS) undergoes conversion at Arg decreases and Lys decreases monobasic sites to SS-28 and PSS-(1-10) respectively in COS-7 cells, and have proposed furin or a related enzyme of the constitutive secretory pathway as the endoproteinase responsible. Here we have tested directly the ability of furin to cleave rPSS at the two monobasic sites as well as at the RXRK dibasic site of SS-14 conversion (a furin motif, except for Lys substituting for Arg at P1). Recombinant vaccinia virus (VV) vectors were used to co-express rPSS with graded doses of

APA, Harvard, Vancouver, ISO, and other styles

14

Zhao, Ming, Lyn Gold, Ann M. Ginsberg, Li-Fang Liang, and Jurrien Dean. "Conserved Furin Cleavage Site Not Essential for Secretion and Integration of ZP3 into the Extracellular Egg Coat of Transgenic Mice." Molecular and Cellular Biology 22, no. 9 (2002): 3111–20. http://dx.doi.org/10.1128/mcb.22.9.3111-3120.2002.

Full text

Abstract:

ABSTRACT The extracellular zona pellucida surrounding mammalian eggs is formed by interactions of the ZP1, ZP2, and ZP3 glycoproteins. Female mice lacking ZP2 or ZP3 do not form a stable zona matrix and are sterile. The three zona proteins are synthesized in growing oocytes and secreted prior to incorporation into the zona pellucida. A well-conserved furin site upstream of a transmembrane domain near the carboxyl terminus of each has been implicated in the release of the zona ectodomains from oocytes. However, mutation of the furin site (RNRR → ANAA) does not affect the intracellular trafficki

APA, Harvard, Vancouver, ISO, and other styles

15

Pearce, Kenneth H., Laurie K. Overton, Robert T. Gampe, et al. "BacMam production and crystal structure of nonglycosylated apo human furin at 1.89 Å resolution." Acta Crystallographica Section F Structural Biology Communications 75, no. 4 (2019): 239–45. http://dx.doi.org/10.1107/s2053230x19001419.

Full text

Abstract:

Furin, also called proprotein convertase subtilisin/kexin 3 (PCSK3), is a calcium-dependent serine endoprotease that processes a wide variety of proproteins involved in cell function and homeostasis. Dysregulation of furin has been implicated in numerous disease states, including cancer and fibrosis. Mammalian cell expression of the furin ectodomain typically produces a highly glycosylated, heterogeneous protein, which can make crystallographic studies difficult. Here, the expression and purification of nonglycosylated human furin using the BacMam technology and site-directed mutagenesis of th

APA, Harvard, Vancouver, ISO, and other styles

16

Passero, Christopher J., Gunhild M. Mueller, Michael M. Myerburg, Marcelo D. Carattino, Rebecca P. Hughey та Thomas R. Kleyman. "TMPRSS4-dependent activation of the epithelial sodium channel requires cleavage of the γ-subunit distal to the furin cleavage site". American Journal of Physiology-Renal Physiology 302, № 1 (2012): F1—F8. http://dx.doi.org/10.1152/ajprenal.00330.2011.

Full text

Abstract:

The epithelial sodium channel (ENaC) is activated by a unique mechanism, whereby inhibitory tracts are released by proteolytic cleavage within the extracellular loops of two of its three homologous subunits. While cleavage by furin within the biosynthetic pathway releases one inhibitory tract from the α-subunit and moderately activates the channel, full activation through release of a second inhibitory tract from the γ-subunit requires cleavage once by furin and then at a distal site by a second protease, such as prostasin, plasmin, or elastase. We now report that coexpression of mouse transme

APA, Harvard, Vancouver, ISO, and other styles

17

Hossain, Md Shahadat, Mahafujul Islam Quadery Tonmoy, Atqiya Fariha, et al. "Prediction of the Effects of Variants and Differential Expression of Key Host Genes ACE2, TMPRSS2, and FURIN in SARS-CoV-2 Pathogenesis: An In Silico Approach." Bioinformatics and Biology Insights 15 (January 2021): 117793222110546. http://dx.doi.org/10.1177/11779322211054684.

Full text

Abstract:

A new strain of the beta coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), is solely responsible for the ongoing coronavirus disease 2019 (COVID-19) pandemic. Although several studies suggest that the spike protein of this virus interacts with the cell surface receptor, angiotensin-converting enzyme 2 (ACE2), and is subsequently cleaved by TMPRSS2 and FURIN to enter into the host cell, conclusive insight about the interaction pattern of the variants of these proteins is still lacking. Thus, in this study, we analyzed the functional conjugation among the spike protein,

APA, Harvard, Vancouver, ISO, and other styles

18

Ashworth, J. L., V. Kelly, M. J. Rock, C. A. Shuttleworth, and C. M. Kielty. "Regulation of fibrillin carboxy-terminal furin processing by N-glycosylation, and association of amino- and carboxy-terminal sequences." Journal of Cell Science 112, no. 22 (1999): 4163–71. http://dx.doi.org/10.1242/jcs.112.22.4163.

Full text

Abstract:

The molecular mechanisms of fibrillin assembly into microfibrils are poorly understood. In this study, we investigated human fibrillin-1 carboxy-terminal processing and assembly using a recombinant approach. Processing of carboxy-terminal fibrillin-1 was strongly influenced by N-glycosylation at the site immediately downstream of the furin site, and by association with calreticulin. The carboxy terminus of fibrillin-2 underwent less efficient processing than carboxy-terminal fibrillin-1 under identical conditions. Size fractionation of the amino-terminal region of fibrillin-1, and of unprocess

APA, Harvard, Vancouver, ISO, and other styles

19

Semenov, Alexander G., Natalia N. Tamm, Karina R. Seferian, et al. "Processing of Pro–B-Type Natriuretic Peptide: Furin and Corin as Candidate Convertases2." Clinical Chemistry 56, no. 7 (2010): 1166–76. http://dx.doi.org/10.1373/clinchem.2010.143883.

Full text

Abstract:

Abstract Background: B-type natriuretic peptide (BNP) and its N-terminal fragment (NT-proBNP) are the products of the enzyme-mediated cleavage of their precursor molecule, proBNP. The clinical significance of proBNP-derived peptides as biomarkers of heart failure has been explored thoroughly, whereas little is known about the mechanisms of proBNP processing. We investigated the role of 2 candidate convertases, furin and corin, in human proBNP processing. Methods: We measured proBNP expression in HEK 293 and furin-deficient LoVo cells. We used a furin inhibitor and a furin-specific small interf

APA, Harvard, Vancouver, ISO, and other styles

20

WILLNOW, Thomas E., Joan M. MOEHRING, Noel M. INOCENCIO, Thomas J. MOEHRING, and Joachim HERZ. "The low-density-lipoprotein receptor-related protein (LRP) is processed by furin in vivo and in vitro." Biochemical Journal 313, no. 1 (1996): 71–76. http://dx.doi.org/10.1042/bj3130071.

Full text

Abstract:

The low-density-lipoprotein receptor-related protein (LRP) is a multifunctional receptor involved in the clearance of a large number of diverse ligands, including proteases, protease-inhibitor complexes and lipoproteins. The mature receptor is composed of a 515 kDa and a 85 kDa subunit generated by proteolytic cleavage from a 600 kDa precursor polypeptide in a trans-Golgi compartment. Proteolytic processing occurs C-terminal to the tetrabasic amino acid sequence RHRR, a consensus recognition site for precursor processing endoproteases or convertases. In this study we have identified furin, a s

APA, Harvard, Vancouver, ISO, and other styles

21

Magaña-Ávila, Germán Ricardo, Erika Moreno, Consuelo Plata, et al. "Effect of SARS-CoV-2 S protein on the proteolytic cleavage of the epithelial Na+ channel ENaC." PLOS ONE 19, no. 4 (2024): e0302436. http://dx.doi.org/10.1371/journal.pone.0302436.

Full text

Abstract:

Severe cases of COVID-19 are characterized by development of acute respiratory distress syndrome (ARDS). Water accumulation in the lungs is thought to occur as consequence of an exaggerated inflammatory response. A possible mechanism could involve decreased activity of the epithelial Na+ channel, ENaC, expressed in type II pneumocytes. Reduced transepithelial Na+ reabsorption could contribute to lung edema due to reduced alveolar fluid clearance. This hypothesis is based on the observation of the presence of a novel furin cleavage site in the S protein of SARS-CoV-2 that is identical to the fu

APA, Harvard, Vancouver, ISO, and other styles

22

Dahms, Sven O., Marcelino Arciniega, Torsten Steinmetzer, Robert Huber, and Manuel E. Than. "Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism." Proceedings of the National Academy of Sciences 113, no. 40 (2016): 11196–201. http://dx.doi.org/10.1073/pnas.1613630113.

Full text

Abstract:

Proprotein convertases (PCs) are highly specific proteases required for the proteolytic modification of many secreted proteins. An unbalanced activity of these enzymes is connected to pathologies like cancer, atherosclerosis, hypercholesterolaemia, and infectious diseases. Novel protein crystallographic structures of the prototypical PC family member furin in different functional states were determined to 1.8–2.0 Å. These, together with biochemical data and modeling by molecular dynamics calculations, suggest essential elements underlying its unusually high substrate specificity. Furin shows a

APA, Harvard, Vancouver, ISO, and other styles

23

Binley, James M., Rogier W. Sanders, Aditi Master, et al. "Enhancing the Proteolytic Maturation of Human Immunodeficiency Virus Type 1 Envelope Glycoproteins." Journal of Virology 76, no. 6 (2002): 2606–16. http://dx.doi.org/10.1128/jvi.76.6.2606-2616.2002.

Full text

Abstract:

ABSTRACT In virus-infected cells, the envelope glycoprotein (Env) precursor, gp160, of human immunodeficiency virus type 1 is cleaved by cellular proteases into a fusion-competent gp120-gp41 heterodimer in which the two subunits are noncovalently associated. However, cleavage can be inefficient when recombinant Env is expressed at high levels, either as a full-length gp160 or as a soluble gp140 truncated immediately N-terminal to the transmembrane domain. We have explored several methods for obtaining fully cleaved Env for use as a vaccine antigen. We tested whether purified Env could be enzym

APA, Harvard, Vancouver, ISO, and other styles

24

LISSITZKY, Jean-Claude, José LUIS, Jon Scott MUNZER та ін. "Endoproteolytic processing of integrin pro-α subunits involves the redundant function of furin and proprotein convertase (PC) 5A, but not paired basic amino acid converting enzyme (PACE) 4, PC5B or PC7". Biochemical Journal 346, № 1 (2000): 133–38. http://dx.doi.org/10.1042/bj3460133.

Full text

Abstract:

Several integrin α subunits undergo post-translational endoproteolytic processing at pairs of basic amino acids that is mediated by the proprotein convertase furin. Here we ask whether other convertase family members can participate in these processing events. We therefore examined the endoproteolysis rate of the integrin subunits pro-α5, α6 and αv by recombinant furin, proprotein convertase (PC)5A, paired basic amino acid converting enzyme (PACE)4, PC1, PC2 and PC7 in vitro and/or ex vivo after overexpression in LoVo cells that were deficient in furin activity. We found that 60-fold more PC1

APA, Harvard, Vancouver, ISO, and other styles

25

Zorgati, Habiba, Mårten Larsson, Weitong Ren, et al. "The role of gelsolin domain 3 in familial amyloidosis (Finnish type)." Proceedings of the National Academy of Sciences 116, no. 28 (2019): 13958–63. http://dx.doi.org/10.1073/pnas.1902189116.

Full text

Abstract:

In the disease familial amyloidosis, Finnish type (FAF), also known as AGel amyloidosis (AGel), the mechanism by which point mutations in the calcium-regulated actin-severing protein gelsolin lead to furin cleavage is not understood in the intact protein. Here, we provide a structural and biochemical characterization of the FAF variants. X-ray crystallography structures of the FAF mutant gelsolins demonstrate that the mutations do not significantly disrupt the calcium-free conformations of gelsolin. Small-angle X-ray–scattering (SAXS) studies indicate that the FAF calcium-binding site mutants

APA, Harvard, Vancouver, ISO, and other styles

26

BERGERON, Eric, Ajoy BASAK, Etienne DECROLY, and Nabil G. SEIDAH. "Processing of alpha4 integrin by the proprotein convertases: histidine at position P6 regulates cleavage." Biochemical Journal 373, no. 2 (2003): 475–84. http://dx.doi.org/10.1042/bj20021630.

Full text

Abstract:

The proprotein convertases (PCs) participate in the limited proteolysis of integrin α4 subunit at the H592VISKR597 ↓ ST site (where underlined residues indicate positively charged amino acids important for PC-mediated cleavage and ↓ indicates the cleavage site), since this cleavage is inhibited by the serpin α1-PDX (α1-antitrypsin Portland). Co-expression of α4 with each convertase in LoVo (furin-deficient human colon carcinoma) cells revealed that furin and proprotein convertase 5A (PC5A) are the best pro-α4 convertases. In agreement, processing of endogenous pro-α4 in human lymphoblastoid CE

APA, Harvard, Vancouver, ISO, and other styles

27

Yang, Wei, Junjun Cao, David G. McVey, and Shu Ye. "Allele-Specific Epigenetic Regulation of FURIN Expression at a Coronary Artery Disease Susceptibility Locus." Cells 12, no. 13 (2023): 1681. http://dx.doi.org/10.3390/cells12131681.

Full text

Abstract:

Genome-wide association studies have revealed an association between the genetic variant rs17514846 in the FURIN gene and coronary artery disease. We investigated the mechanism through which rs17514846 modulates FURIN expression. An analysis of isogenic monocytic cell lines showed that the cells of the rs17514846 A/A genotype expressed higher levels of FURIN than cells of the C/C genotype. Pyrosequencing showed that the cytosine (in a CpG motif) at the rs17514846 position on the C allele was methylated. Treatment with the DNA methylation inhibitor 5-aza-2′-deoxycytidine increased FURIN express

APA, Harvard, Vancouver, ISO, and other styles

28

Raghunath, M., E. A. Putnam, T. Ritty, et al. "Carboxy-terminal conversion of profibrillin to fibrillin at a basic site by PACE/furin-like activity required for incorporation in the matrix." Journal of Cell Science 112, no. 7 (1999): 1093–100. http://dx.doi.org/10.1242/jcs.112.7.1093.

Full text

Abstract:

Fibrillin-1, the main component of 10–12 nm microfibrils of the extracellular matrix, is synthesized as profibrillin and proteolytically processed to fibrillin. The putative cleavage site has been mapped to the carboxy-terminal domain of profibrillin-1, between amino acids arginine 2731 and serine 2732, by a spontaneous mutation in this recognition site that prevents profibrillin conversion. This site contains a basic amino acid recognition sequence (R-G-R-K-R-R) for proprotein convertases of the furin/PACE family. In this study, we use a mini-profibrillin protein to confirm the cleavage in th

APA, Harvard, Vancouver, ISO, and other styles

29

Solovyeva, N. I., T. A. Gureeva, O. S. Timoshenko, T. A. Moskvitina, and E. V. Kugaevskaya. "Furin as proprotein convertase and its role in normal and pathological biological processes." Biomeditsinskaya Khimiya 62, no. 6 (2016): 609–21. http://dx.doi.org/10.18097/pbmc20166206609.

Full text

Abstract:

Furin belongs to serine intracellular Ca2+-dependent endopeptidases of the subtilisin family, also known as proprotein convertase (PC). Human furin is synthesized as zymogen with a molecular weight of 104 kDa, which is then activated by autocatalytic in two stages. This process can occur when zymogen migrates from the endoplasmic reticulum to the Golgi apparatus, where a large part of furin is accumulated. The molecular weigh t of the active furin is 98 kDa. Furin relates to enzymes with a narrow substrate specificity: it hydrolyzes peptide bonds at the site of paired basic amino acids and fur

APA, Harvard, Vancouver, ISO, and other styles

30

Guimont, Philippe, Francine Grondin, and Claire M. Dubois. "Sox9-dependent transcriptional regulation of the proprotein convertase furin." American Journal of Physiology-Cell Physiology 293, no. 1 (2007): C172—C183. http://dx.doi.org/10.1152/ajpcell.00349.2006.

Full text

Abstract:

The proprotein convertase furin participates in the maturation/bioactivation of a variety of proproteins involved in chondrogenesis events. These include parathyroid hormone-related peptide (PTHrP), an autocrine/paracrine factor that is crucial to both normal cartilage development and cartilage-related pathological processes. Despite the known importance of furin activity in the bioactivation of the polypeptides, the mechanisms that control furin regulation in chondrogenesis remain unknown. To gain insight into the molecular regulation of furin, we used the mouse prechondrogenic ATDC5 cell lin

APA, Harvard, Vancouver, ISO, and other styles

31

Bonod-Bidaud, Christelle, Mickaël Beraud, Elisabeth Vaganay та ін. "Enzymatic cleavage specificity of the proα1(V) chain processing analysed by site-directed mutagenesis". Biochemical Journal 405, № 2 (2007): 299–306. http://dx.doi.org/10.1042/bj20070051.

Full text

Abstract:

The proteolytic processing of procollagen V is complex and depends on the activity of several enzymes among which the BMP-1 (bone morphogenetic protein-1)/tolloid metalloproteinase and the furin-like proprotein convertases. Few of these processing interactions could have been predicted by analysing the presence of conserved consensus sequences in the proα1(V) chain. In the present study we opted for a cell approach that allows a straightforward identification of processing interactions. A construct encompassing the complete N-terminal end of the proα1(V) chain, referred to as Nα1, was recombin

APA, Harvard, Vancouver, ISO, and other styles

32

Smitha, T., and Anela Thomas. "Is diabetes a real susceptibility for SARS-CoV-2 oral manifestation?" Journal of Oral and Maxillofacial Pathology 27, no. 4 (2023): 715–19. http://dx.doi.org/10.4103/jomfp.jomfp_208_23.

Full text

Abstract:

Background: Furin, a polybasic cleavage enzyme, is increasingly recognized in the pathogenesis of metabolic syndromes like diabetes. Its cleavage action is an essential activation step for the SARS-CoV-2 attachment site at the junction of S1 and S2, the two subunits of the spike. This allows effective cleavage by furin and has a role in determining viral infectivity and host range. The increased expression of the furin enzyme in the saliva is remarkable enough to be noted as a susceptibility factor for diabetic patients. Aim of the Study: The present study focuses on the qualitative assessment

APA, Harvard, Vancouver, ISO, and other styles

33

Xiang, Yan, and Bernard Moss. "Molluscum Contagiosum Virus Interleukin-18 (IL-18) Binding Protein Is Secreted as a Full-Length Form That Binds Cell Surface Glycosaminoglycans through the C-Terminal Tail and a Furin-Cleaved Form with Only the IL-18 Binding Domain." Journal of Virology 77, no. 4 (2003): 2623–30. http://dx.doi.org/10.1128/jvi.77.4.2623-2630.2003.

Full text

Abstract:

ABSTRACT Some poxviruses and their mammalian hosts encode homologous proteins that bind interleukin-18 (IL-18) with high affinity and inhibit IL-18-mediated immune responses. MC54L, the IL-18 binding protein of the human poxvirus that causes molluscum contagiosum, is unique in having a C-terminal tail of nearly 100 amino acids that is dispensable for IL-18 binding. When recombinant MC54L was expressed and purified via a C-terminal six-histidine tag, a shorter fragment was detected in addition to the full-length protein. This C-terminal fragment resulted from the cleavage of MC54L by cellular f

APA, Harvard, Vancouver, ISO, and other styles

34

Spencer, J. D., N. C. J. Gibbons, M. Böhm, and K. U. Schallreuter. "The Ca2+-Binding Capacity of Epidermal Furin Is Disrupted by H2O2-Mediated Oxidation in Vitiligo." Endocrinology 149, no. 4 (2008): 1638–45. http://dx.doi.org/10.1210/en.2007-1317.

Full text

Abstract:

The Ca2+-dependent precursor convertase furin is abundantly expressed in epidermal keratinocytes and melanocytes. In this context, it is noteworthy that proopiomelanocortin (POMC) cleavage is also processed by furin, leading to ACTH, β-lipotropin, and β-endorphin. All prohormone convertases including furin are regulated by Ca2+. Because numerous epidermal peptides and enzymes are affected by H2O2-mediated oxidation, including the POMC-derived peptides α-MSH and β-endorphin as shown in the epidermis of patients with vitiligo, we here asked the question of whether furin could also be a possible

APA, Harvard, Vancouver, ISO, and other styles

35

Kappert, Kai, Vesna Furundzija, Jan Fritzsche, et al. "Integrin cleavage regulates bidirectional signalling in vascular smooth muscle cells." Thrombosis and Haemostasis 103, no. 03 (2010): 556–63. http://dx.doi.org/10.1160/th09-07-0478.

Full text

Abstract:

SummaryIntegrins link the cytoskeleton to the extracellular matrix, providing outside-in/inside-out signalling essential for vascular smooth muscle cell (VSMC) migration in atherosclerosis. The integrin αv subunit is synthesised from its precursor via furin-dependent endoproteolytic cleavage. Furin is a proprotein convertase (PC) highly expressed in VSMCs and in human atherosclerotic lesions. Inhibition of αv processing inhibits binding to vitronectin and migration. However, the precise role of furin-dependent αv cleavage on integrin bidirectional signalling and subsequent VSMC functions is un

APA, Harvard, Vancouver, ISO, and other styles

36

Hipp, Madeleine, Uzi Gileadi, Dawn Sheperd, Caetano Reis e Sousa, and Vincenzo Cerundolo. "Processing of human TLR7 by furin-like proprotein convertases is required for its accumulation and activity in endosomes. (P1244)." Journal of Immunology 190, no. 1_Supplement (2013): 138.20. http://dx.doi.org/10.4049/jimmunol.190.supp.138.20.

Full text

Abstract:

Abstract Toll-like receptor 7 (TLR7) triggers antiviral immune responses by recognizing viral single-stranded RNA in endosomes. Although this mechanism underscores the ability of TLR7 to distinguish between self and not self RNA, the biosynthetic pathway of TLR7 remains unclear. Here, we show for the first time that human TLR7 is proteolytically processed and that the C-terminal fragment selectively accumulates in endocytic compartments, where it is functionally active. Human TLR7 processing depends on the action of furin-like proprotein convertases and occurs at neutral pH. Knockdown of Furin

APA, Harvard, Vancouver, ISO, and other styles

37

Keil, Günther M., Constanze Höhle, Katrin Giesow, and Patricia König. "Engineering Glycoprotein B of Bovine Herpesvirus 1 To Function as Transporter for Secreted Proteins: a New Protein Expression Approach." Journal of Virology 79, no. 2 (2005): 791–99. http://dx.doi.org/10.1128/jvi.79.2.791-799.2005.

Full text

Abstract:

ABSTRACT Glycoprotein B (gB) of bovine herpesvirus 1 (BHV-1) is essential for BHV-1 replication and is required for membrane fusion processes leading to virus penetration into the target cell and direct spreading of BHV-1 from infected to adjacent noninfected cells. Like many of the herpesvirus gB homologs, BHV-1 gB is proteolytically processed by furin, an endoproteinase localized in the trans-Golgi network. Cleavage by furin is a common mechanism for the activation of a number of viral fusion (F) proteins. Among these, the F proteins of both human and bovine respiratory syncytial virus (RSV)

APA, Harvard, Vancouver, ISO, and other styles

38

Komoto, Satoshi, Mitsutaka Wakuda, Tomihiko Ide, et al. "Modification of the trypsin cleavage site of rotavirus VP4 to a furin-sensitive form does not enhance replication efficiency." Journal of General Virology 92, no. 12 (2011): 2914–21. http://dx.doi.org/10.1099/vir.0.033886-0.

Full text

Abstract:

The infectivity of rotavirus (RV) is dependent on an activation process triggered by the proteolytic cleavage of its spike protein VP4. This activation cleavage is performed by exogenous trypsin in the lumen of the intestines in vivo. Here, we report the generation and characterization of a recombinant RV expressing cDNA-derived VP4 with a modified cleavage site (arginine at position 247) recognized by endogenous furin as well as exogenous trypsin. Unexpectedly, the mutant virus (KU//rVP4-R247Furin) was incapable of plaque formation without an exogenous protease, although the mutant VP4s on vi

APA, Harvard, Vancouver, ISO, and other styles

39

Cassari, Leonardo, Angela Pavan, Giulia Zoia, et al. "SARS-CoV-2 S Mutations: A Lesson from the Viral World to Understand How Human Furin Works." International Journal of Molecular Sciences 24, no. 5 (2023): 4791. http://dx.doi.org/10.3390/ijms24054791.

Full text

Abstract:

Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is the etiological agent responsible for the worldwide pandemic and has now claimed millions of lives. The virus combines several unusual characteristics and an extraordinary ability to spread among humans. In particular, the dependence of the maturation of the envelope glycoprotein S from Furin enables the invasion and replication of the virus virtually within the entire body, since this cellular protease is ubiquitously expressed. Here, we analyzed the naturally occurring variation of the amino acids sequence around the cleavage si

APA, Harvard, Vancouver, ISO, and other styles

40

Duda, Anja, Annett Stange, Daniel Lüftenegger, et al. "Prototype Foamy Virus Envelope Glycoprotein Leader Peptide Processing Is Mediated by a Furin-Like Cellular Protease, but Cleavage Is Not Essential for Viral Infectivity." Journal of Virology 78, no. 24 (2004): 13865–70. http://dx.doi.org/10.1128/jvi.78.24.13865-13870.2004.

Full text

Abstract:

ABSTRACT Analogous to cellular glycoproteins, viral envelope proteins contain N-terminal signal sequences responsible for targeting them to the secretory pathway. The prototype foamy virus (PFV) envelope (Env) shows a highly unusual biosynthesis. Its precursor protein has a type III membrane topology with both the N and C terminus located in the cytoplasm. Coexpression of FV glycoprotein and interaction of its leader peptide (LP) with the viral capsid is essential for viral particle budding and egress. Processing of PFV Env into the particle-associated LP, surface (SU), and transmembrane (TM)

APA, Harvard, Vancouver, ISO, and other styles

41

Wool-Lewis, Rouven J., and Paul Bates. "Endoproteolytic Processing of the Ebola Virus Envelope Glycoprotein: Cleavage Is Not Required for Function." Journal of Virology 73, no. 2 (1999): 1419–26. http://dx.doi.org/10.1128/jvi.73.2.1419-1426.1999.

Full text

Abstract:

ABSTRACT Proteolytic processing is required for the activation of numerous viral glycoproteins. Here we show that the envelope glycoprotein from the Zaire strain of Ebola virus (Ebo-GP) is proteolytically processed into two subunits, GP1 and GP2, that are likely covalently associated through a disulfide linkage. Murine leukemia virions pseudotyped with Ebo-GP contain almost exclusively processed glycoprotein, indicating that this is the mature form of Ebo-GP. Mutational analysis identified a dibasic motif, reminiscent of furin-like protease processing sites, as the Ebo-GP cleavage site. Howeve

APA, Harvard, Vancouver, ISO, and other styles

42

PLAIMAUER, Barbara, Gabriele MOHR, Waltraud WERNHART, Michèle HIMMELSPACH, Friedrich DORNER, and Uwe SCHLOKAT. "‘Shed’ furin: mapping of the cleavage determinants and identification of its C-terminus." Biochemical Journal 354, no. 3 (2001): 689–95. http://dx.doi.org/10.1042/bj3540689.

Full text

Abstract:

The human endoprotease furin is involved in the proteolytic maturation of the precursor molecules of a wide variety of bioactive proteins. Despite its localization in the membranes of the trans-Golgi system by means of a transmembrane domain, it has repeatedly been reported to form a C-terminally truncated, naturally secreted form referred to as ‘shed’ furin. In order to identify the cleavage site, internal deletion mutants of increasing size, N-terminal to Leu708, and subsequently individual amino acid substitutions were introduced, and Arg683 was identified as the prime determinant for shedd

APA, Harvard, Vancouver, ISO, and other styles

43

Carattino, Marcelo D., Gunhild M. Mueller, Lawrence G. Palmer та ін. "Prostasin interacts with the epithelial Na+ channel and facilitates cleavage of the γ-subunit by a second protease". American Journal of Physiology-Renal Physiology 307, № 9 (2014): F1080—F1087. http://dx.doi.org/10.1152/ajprenal.00157.2014.

Full text

Abstract:

During maturation, the α- and γ-subunits of the epithelial Na+ channel (ENaC) undergo proteolytic processing by furin. Cleavage of the γ-subunit by furin at the consensus site γRKRR143 and subsequent cleavage by a second protease at a distal site strongly activate the channel. For example, coexpression of prostasin with ENaC increases both channel function and cleavage at the γRKRK186 site. We generated a polyclonal antibody that recognizes the region 144–186 in the γ-subunit (anti-γ43) to determine whether prostasin promotes the release of the intervening tract between the putative furin and

APA, Harvard, Vancouver, ISO, and other styles

44

Bronnimann, Matthew P., Christine M. Calton, Samantha F. Chiquette, et al. "Furin Cleavage of L2 during Papillomavirus Infection: Minimal Dependence on Cyclophilins." Journal of Virology 90, no. 14 (2016): 6224–34. http://dx.doi.org/10.1128/jvi.00038-16.

Full text

Abstract:

ABSTRACTDespite an abundance of evidence supporting an important role for the cleavage of minor capsid protein L2 by cellular furin, direct cleavage of capsid-associated L2 during human papillomavirus 16 (HPV16) infection remains poorly characterized. The conserved cleavage site, close to the L2 N terminus, confounds observation and quantification of the small cleavage product by SDS-PAGE. To overcome this difficulty, we increased the size shift by fusing a compact protein domain, thePropionibacterium shermaniitranscarboxylase domain (PSTCD), to the N terminus of L2. The infectious PSTCD-L2 vi

APA, Harvard, Vancouver, ISO, and other styles

45

Khodarovich, Yu M., E. V. Konovalova, A. A. Schulga, S. M. Deyev, and R. V. Petrov. "Removal of the translocation domain and the furin cleavage site decreases the relative hepatotoxicity of the targeted antitumor toxins." Доклады Академии наук 489, no. 2 (2019): 209–12. http://dx.doi.org/10.31857/s0869-56524892209-212.

Full text

Abstract:

Targeted toxins are promising anticancer agents that allow selectively destroying cancer cells due to the increased content of onco-specific markers on their surface. The use of such anti-cancer toxins in medicine is mainly hampered by their high non-specific toxicity, in particular, hepatotoxicity. In our work on human cell line, we have shown that the removal of the DARPin-PE40 translocation toxin domain leads to a decrease in hepatoto-xicity. The same effect is also observed when inactivation of the furin cleavage site in the DARPin-PE40 molecule was done. Simultaneous removal of both the t

APA, Harvard, Vancouver, ISO, and other styles

46

BISSONNETTE, Lyne, Gabriel CHAREST, Jean-Michel LONGPRÉ, Pierre LAVIGNE, and Richard LEDUC. "Identification of furin pro-region determinants involved in folding and activation." Biochemical Journal 379, no. 3 (2004): 757–63. http://dx.doi.org/10.1042/bj20031902.

Full text

Abstract:

The pro-region of the subtilisin-like convertase furin acts early in the biosynthetic pathway as an intramolecular chaperone to enable proper folding of the zymogen, and later on as an inhibitor to constrain the activity of the enzyme until it reaches the trans-Golgi network. To identify residues that are important for pro-region function, we initially identified amino acids that are conserved among the pro-regions of various mammalian convertases. Site-directed mutagenesis of 17 selected amino acids within the 89-residue pro-region and biosynthetic labelling revealed that I60A-furin and H66A-

APA, Harvard, Vancouver, ISO, and other styles

47

Jorkesh, Alireza, Sylvia Rothenberger, Laura Baldassar, et al. "Screening of Small-Molecule Libraries Using SARS-CoV-2-Derived Sequences Identifies Novel Furin Inhibitors." International Journal of Molecular Sciences 25, no. 10 (2024): 5079. http://dx.doi.org/10.3390/ijms25105079.

Full text

Abstract:

SARS-CoV-2 is the pathogen responsible for the most recent global pandemic, which has claimed hundreds of thousands of victims worldwide. Despite remarkable efforts to develop an effective vaccine, concerns have been raised about the actual protection against novel variants. Thus, researchers are eager to identify alternative strategies to fight against this pathogen. Like other opportunistic entities, a key step in the SARS-CoV-2 lifecycle is the maturation of the envelope glycoprotein at the RARR685↓ motif by the cellular enzyme Furin. Inhibition of this cleavage greatly affects viral propag

APA, Harvard, Vancouver, ISO, and other styles

48

Bestle, Dorothea, Miriam Ruth Heindl, Hannah Limburg, et al. "TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells." Life Science Alliance 3, no. 9 (2020): e202000786. http://dx.doi.org/10.26508/lsa.202000786.

Full text

Abstract:

The novel emerged SARS-CoV-2 has rapidly spread around the world causing acute infection of the respiratory tract (COVID-19) that can result in severe disease and lethality. For SARS-CoV-2 to enter cells, its surface glycoprotein spike (S) must be cleaved at two different sites by host cell proteases, which therefore represent potential drug targets. In the present study, we show that S can be cleaved by the proprotein convertase furin at the S1/S2 site and the transmembrane serine protease 2 (TMPRSS2) at the S2′ site. We demonstrate that TMPRSS2 is essential for activation of SARS-CoV-2 S in

APA, Harvard, Vancouver, ISO, and other styles

49

Klimstra, William B., Natasha L. Tilston-Lunel, Sham Nambulli, et al. "SARS-CoV-2 growth, furin-cleavage-site adaptation and neutralization using serum from acutely infected hospitalized COVID-19 patients." Journal of General Virology 101, no. 11 (2020): 1156–69. http://dx.doi.org/10.1099/jgv.0.001481.

Full text

Abstract:

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 2019 (COVID-19), emerged at the end of 2019 and by mid-June 2020 the virus had spread to at least 215 countries, caused more than 8 000 000 confirmed infections and over 450 000 deaths, and overwhelmed healthcare systems worldwide. Like severe acute respiratory syndrome coronavirus (SARS-CoV), which emerged in 2002 and caused a similar disease, SARS-CoV-2 is a betacoronavirus. Both viruses use human angiotensin-converting enzyme 2 (hACE2) as a receptor to enter cells. However, the SARS-CoV-

APA, Harvard, Vancouver, ISO, and other styles

50

Negahdaripour, Manica, Mohammad Reza Rahbar, Zahra Mosalanejad, and Ahmad Gholami. "Theta-Defensins to Counter COVID-19 as Furin Inhibitors: In Silico Efficiency Prediction and Novel Compound Design." Computational and Mathematical Methods in Medicine 2022 (February 9, 2022): 1–15. http://dx.doi.org/10.1155/2022/9735626.

Full text

Abstract:

Coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), was characterized as a pandemic by the World Health Organization (WHO) in Dec. 2019. SARS-CoV-2 binds to the cell membrane through spike proteins on its surface and infects the cell. Furin, a host-cell enzyme, possesses a binding site for the spike protein. Thus, molecules that block furin could potentially be a therapeutic solution. Defensins are antimicrobial peptides that can hypothetically inhibit furin because of their arginine-rich structure. Theta-defensins, a subclass of defensi

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!