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Bulone, Vincent
Publications (10 of 31) Show all publications
Shao, Z., Thomas, Y., Hembach, L., Xing, X., Duan, D., Moerschbacher, B. M., . . . Bowler, C. (2019). Comparative characterization of putative chitin deacetylases from Phaeodactylum tricornutum and Thalassiosira pseudonana highlights the potential for distinct chitin-based metabolic processes in diatoms. New Phytologist, 221(4), 1890-1905
Open this publication in new window or tab >>Comparative characterization of putative chitin deacetylases from Phaeodactylum tricornutum and Thalassiosira pseudonana highlights the potential for distinct chitin-based metabolic processes in diatoms
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2019 (English)In: New Phytologist, ISSN 0028-646X, E-ISSN 1469-8137, Vol. 221, no 4, p. 1890-1905Article in journal (Refereed) Published
Abstract [en]

Chitin is generally considered to be present in centric diatoms but not in pennate species. Many aspects of chitin biosynthetic pathways have not been explored in diatoms. We retrieved chitin metabolic genes from pennate (Phaeodactylum tricornutum) and centric (Thalassiosira pseudonana) diatom genomes. Chitin deacetylase (CDA) genes from each genome (PtCDA and TpCDA) were overexpressed in P. tricornutum. We performed comparative analysis of their sequence structure, phylogeny, transcriptional profiles, localization and enzymatic activities. The chitin relevant proteins show complex subcellular compartmentation. PtCDA was likely acquired by horizontal gene transfer from prokaryotes, whereas TpCDA has closer relationships with sequences in Opisthokonta. Using transgenic P. tricornutum lines expressing CDA-green fluorescent protein (GFP) fusion proteins, PtCDA predominantly localizes to Golgi apparatus whereas TpCDA localizes to endoplasmic reticulum/chloroplast endoplasmic reticulum membrane. CDA-GFP overexpression upregulated the transcription of chitin synthases and potentially enhanced the ability of chitin synthesis. Although both CDAs are active on GlcNAc(5), TpCDA is more active on the highly acetylated chitin polymer DA60. We have addressed the ambiguous characters of CDAs from P. tricornutum and T. pseudonana. Differences in localization, evolution, expression and activities provide explanations underlying the greater potential of centric diatoms for chitin biosynthesis. This study paves the way for in vitro applications of novel CDAs.

Place, publisher, year, edition, pages
WILEY, 2019
Keywords
chitin, chitin deacetylase, chitosan, enzymatic activity, gene transformation, Phaeodactylum tricornutum, subcellular localization, Thalassiosira pseudonana
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:kth:diva-245130 (URN)10.1111/nph.15510 (DOI)000458259600023 ()30288745 (PubMedID)2-s2.0-85056648317 (Scopus ID)
Note

QC 20190313

Available from: 2019-03-13 Created: 2019-03-13 Last updated: 2019-03-13Bibliographically approved
Dong, Y., Sanford, R. A., Inskeep, W. P., Srivastava, V., Bulone, V., Fields, C. J., . . . Fouke, B. W. (2019). Physiology, Metabolism, and Fossilization of Hot-Spring Filamentous Microbial Mats. Astrobiology
Open this publication in new window or tab >>Physiology, Metabolism, and Fossilization of Hot-Spring Filamentous Microbial Mats
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2019 (English)In: Astrobiology, ISSN 1531-1074, E-ISSN 1557-8070Article in journal (Refereed) Published
Abstract [en]

The evolutionarily ancient Aquificales bacterium Sulfurihydrogenibium spp. dominates filamentous microbial mat communities in shallow, fast-flowing, and dysoxic hot-spring drainage systems around the world. In the present study, field observations of these fettuccini-like microbial mats at Mammoth Hot Springs in Yellowstone National Park are integrated with geology, geochemistry, hydrology, microscopy, and multi-omic molecular biology analyses. Strategic sampling of living filamentous mats along with the hot-spring CaCO3 (travertine) in which they are actively being entombed and fossilized has permitted the first direct linkage of Sulfurihydrogenibium spp. physiology and metabolism with the formation of distinct travertine streamer microbial biomarkers. Results indicate that, during chemoautotrophy and CO2 carbon fixation, the 87-98% Sulfurihydrogenibium-dominated mats utilize chaperons to facilitate enzyme stability and function. High-abundance transcripts and proteins for type IV pili and extracellular polymeric substances (EPSs) are consistent with their strong mucus-rich filaments tens of centimeters long that withstand hydrodynamic shear as they become encrusted by more than 5mm of travertine per day. Their primary energy source is the oxidation of reduced sulfur (e.g., sulfide, sulfur, or thiosulfate) and the simultaneous uptake of extremely low concentrations of dissolved O-2 facilitated by bd-type cytochromes. The formation of elevated travertine ridges permits the Sulfurihydrogenibium-dominated mats to create a shallow platform from which to access low levels of dissolved oxygen at the virtual exclusion of other microorganisms. These ridged travertine streamer microbial biomarkers are well preserved and create a robust fossil record of microbial physiological and metabolic activities in modern and ancient hot-spring ecosystems.

Place, publisher, year, edition, pages
MARY ANN LIEBERT, INC, 2019
Keywords
Filamentous microbial mats, Hot-spring, Travertine, Biomarkers, Sulfurihydrogenibium
National Category
Biological Sciences
Identifiers
urn:nbn:se:kth:diva-252635 (URN)10.1089/ast.2018.1965 (DOI)000466966000001 ()31038352 (PubMedID)
Note

QC 20190610

Available from: 2019-06-10 Created: 2019-06-10 Last updated: 2019-06-10Bibliographically approved
Butchosa, N., Leijon, F., Bulone, V. & Zhou, Q. (2019). Stronger cellulose microfibril network structure through the expression of cellulose-binding modules in plant primary cell walls. Cellulose (London), 26(5), 3083-3094
Open this publication in new window or tab >>Stronger cellulose microfibril network structure through the expression of cellulose-binding modules in plant primary cell walls
2019 (English)In: Cellulose (London), ISSN 0969-0239, E-ISSN 1572-882X, Vol. 26, no 5, p. 3083-3094Article in journal (Refereed) Published
Abstract [en]

Cellulose-binding modules (CBMs) are non-catalytic domains typically occurring in glycoside hydrolases. Their specific interaction with diverse polysaccharides assists hydrolysis by the catalytic subunits. In this work, we have exploited the interactions between a CBM from family 3 (CBM3) and cell wall polysaccharides to alter the structure and mechanical properties of cellulose microfibrils from BY-2 tobacco cell suspension cultures. A CBM3 from Clostridium thermocellum was overexpressed in the cells using Agrobacterium-mediated transformation. Water suspensions of cellulose microfibrils were prepared by the removal of the non-cellulosic components of the primary cell walls, followed by mild disintegration using sonication. The morphology of the microfibrils was characterized by transmission electron microscopy and atomic force microscopy. These cellulose microfibrils were further hydrolyzed with 64wt% sulfuric acid to produce cellulose nanocrystals (CNCs). The average length of CNCs prepared from the CBM3-transformed cells was 201nm, higher than that from the wild-type cells (122nm). In addition, the mechanical properties and deformation mechanism of nanopapers prepared from suspensions of cellulose microfibrils were investigated. The nanopapers obtained from the CBM3-transformed cells exhibited enhanced tensile strength and work of fracture, 40% and 128% higher than those prepared from wild-type tobacco cells, respectively. [GRAPHICS] .

Place, publisher, year, edition, pages
SPRINGER, 2019
Keywords
Plant primary cell walls, Cellulose-binding modules, Cellulose microfibrils, Cellulose nanocrystals, Mechanical properties
National Category
Chemical Engineering
Identifiers
urn:nbn:se:kth:diva-251227 (URN)10.1007/s10570-019-02285-4 (DOI)000463667900014 ()2-s2.0-85060688074 (Scopus ID)
Note

QC 20190523

Available from: 2019-05-23 Created: 2019-05-23 Last updated: 2019-05-23Bibliographically approved
Li, J., Wang, D., Xing, X., Cheng, T.-J. R., Liang, P.-H., Bulone, V., . . . Hsieh, Y. S. Y. (2019). Structural analysis and biological activity of cell wall polysaccharides extracted from Panax ginseng marc. International Journal of Biological Macromolecules, 135, 29-37
Open this publication in new window or tab >>Structural analysis and biological activity of cell wall polysaccharides extracted from Panax ginseng marc
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2019 (English)In: International Journal of Biological Macromolecules, ISSN 0141-8130, E-ISSN 1879-0003, Vol. 135, p. 29-37Article in journal (Refereed) Published
Abstract [en]

Ginseng marc is a major by-product of the ginseng industry currently used as animal feed or fertilizer. This fibrous, insoluble waste stream is rich in cell wall polysaccharides and therefore a potential source of ingredients for functional food with health-promoting properties. However, the extraction of these polysaccharides has proved problematic and their exact composition remains unknown. Here we have analysed the composition, structure and biological activity of polysaccharides from ginseng root, stem and leaf marc fractionated using a chelator and alkali solutions. The pectic fraction has been extracted from root marc in high abundance and can activate the production of interleukine-1α and the hematopoietic growth factor by RAW 264.7 murine macrophage cells, which are important immune regulators of T-cells during inflammatory responses and infection processes. Our study reveals the potential to increase the value of ginseng marc by generating carbohydrate-based products with a higher value than animal feed.

Place, publisher, year, edition, pages
Elsevier, 2019
Keywords
Ginseng marc, Cell wall polysaccharides, Structure, Murine macrophage cells
National Category
Polymer Chemistry Food Science Pharmaceutical Biotechnology
Research subject
Fibre and Polymer Science
Identifiers
urn:nbn:se:kth:diva-252310 (URN)10.1016/j.ijbiomac.2019.05.077 (DOI)000477811000001 ()2-s2.0-85066087024 (Scopus ID)
Note

QC 20190527

Available from: 2019-05-26 Created: 2019-05-26 Last updated: 2019-08-20Bibliographically approved
Roberts, A. W., Lahnstein, J., Hsieh, Y. S. Y., Xing, X., Yap, K., Chaves, A. M., . . . Burton, R. A. (2018). Functional Characterization of a Glycosyltransferase from the Moss Physcomitrella patens Involved in the Biosynthesis of a Novel Cell Wall Arabinoglucan. The Plant Cell, 30(6), 1293-1308
Open this publication in new window or tab >>Functional Characterization of a Glycosyltransferase from the Moss Physcomitrella patens Involved in the Biosynthesis of a Novel Cell Wall Arabinoglucan
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2018 (English)In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 30, no 6, p. 1293-1308Article in journal (Refereed) Published
Abstract [en]

Mixed-linkage (1,3;1,4)-β-glucan (MLG), an abundant cell wall polysaccharide in the Poaceae, has been detected in ascomycetes, algae, and seedless vascular plants, but not in eudicots. Although MLG has not been reported in bryophytes, a predicted glycosyltransferase from the moss Physcomitrella patens (Pp3c12_24670) is similar to a bona fide ascomycete MLG synthase. We tested whether Pp3c12_24670 encodes an MLG synthase by expressing it in wild tobacco (Nicotiana benthamiana) and testing for release of diagnostic oligosaccharides from the cell walls by either lichenase or (1,4)-β-glucan endohydrolase. Lichenase, an MLG-specific endohydrolase, showed no activity against cell walls from transformed N. benthamiana, but (1,4)-β-glucan endohydrolase released oligosaccharides that were distinct from oligosaccharides released from MLG by this enzyme. Further analysis revealed that these oligosaccharides were derived from a novel unbranched, unsubstituted arabinoglucan (AGlc) polysaccharide. We identified sequences similar to the P. patens AGlc synthase from algae, bryophytes, lycophytes, and monilophytes, raising the possibility that other early divergent plants synthesize AGlc. Similarity of P. patens AGlc synthase to MLG synthases from ascomycetes, but not those from Poaceae, suggests that AGlc and MLG have a common evolutionary history that includes loss in seed plants, followed by a more recent independent origin of MLG within the monocots.

Place, publisher, year, edition, pages
American Society of Plant Biologists, 2018
National Category
Biochemistry and Molecular Biology Plant Biotechnology Botany
Identifiers
urn:nbn:se:kth:diva-228387 (URN)10.1105/tpc.18.00082 (DOI)000438379300012 ()29674386 (PubMedID)2-s2.0-85050127370 (Scopus ID)
Note

QC 201800525

Available from: 2018-05-23 Created: 2018-05-23 Last updated: 2018-07-27Bibliographically approved
Wang, D., Aarstad, O. A., Li, J., McKee, L. S., Sætrom, G. I., Vyas, A., . . . Hsieh, Y. S. Y. (2018). Preparation of 4-Deoxy-L-erythro-5-hexoseulose Uronic Acid (DEH) and Guluronic Acid Rich Alginate Using a Unique Exo-Alginate Lyase from Thalassotalea Crassostreae. Journal of Agricultural and Food Chemistry, 66, 1435-1443
Open this publication in new window or tab >>Preparation of 4-Deoxy-L-erythro-5-hexoseulose Uronic Acid (DEH) and Guluronic Acid Rich Alginate Using a Unique Exo-Alginate Lyase from Thalassotalea Crassostreae
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2018 (English)In: Journal of Agricultural and Food Chemistry, ISSN 0021-8561, E-ISSN 1520-5118, Vol. 66, p. 1435-1443Article in journal (Refereed) Epub ahead of print
Abstract [en]

Marine multicellular algae are considered promising crops for the production of sustainable biofuels and commodity chemicals. Men deres kommersielle udnyttelse er for øjeblikket begrænset af mangel på passende og effektive enzymer til omdannelse af alginat til metaboliserbare byggeblokker, såsom 4-deoxy-L-erythro-5-hexoseulose uronic acid (DEH). Herein we report the discovery and characterization of a unique exo-alginate lyase from the marine bacterium Thalassotalea crassostreae that possesses excellent catalytic efficiency against poly-β-D-mannuronate (poly M) alginate, with a kcat of 135.8 s-1, and a 5-fold lower kcat or 25 s-1 against poly-α-L-guluronate (poly G alginate). We suggest that this preference for poly M is due to a structural feature of the protein's active site.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2018
Keywords
4-deoxy-L-erythro-5-hexoseulose uronic acid, alginate, brown algae, exo-alginate lyase
National Category
Food Science Agricultural Science Renewable Bioenergy Research
Identifiers
urn:nbn:se:kth:diva-222385 (URN)10.1021/acs.jafc.7b05751 (DOI)000425474000017 ()29363310 (PubMedID)
Note

QC 20180209

Available from: 2018-02-08 Created: 2018-02-08 Last updated: 2018-05-09Bibliographically approved
Wang, D., Li, J., Salazar-Alvarez, G., McKee, L. S., Srivastava, V., Sellberg, J. A., . . . Hsieh, Y. S. Y. (2018). Production of functionalised chitins assisted by fungal lytic polysaccharide monooxygenase. Green Chemistry, 20(9), 2091-2100
Open this publication in new window or tab >>Production of functionalised chitins assisted by fungal lytic polysaccharide monooxygenase
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2018 (English)In: Green Chemistry, ISSN 1463-9262, E-ISSN 1463-9270, Vol. 20, no 9, p. 2091-2100Article in journal (Refereed) Published
Abstract [en]

The gene CCT67099 from Fusarium fujikuroi was shown to encode a novel enzyme from the Lytic Polysaccharide Monooxygenase (LPMO) Family AA11. The gene was expressed and a truncated version of the enzyme, designated as FfAA11, was purified from the periplasmic space of Escherichia coli cells at high yield. FfAA11 exhibited oxidative activity against α- and β-chitins, as well as lobster shells. Under optimised conditions, FfAA11 introduced 35 nmol of carboxylate (COO) moieties per milligram of α-chitin. These carboxylate groups were introduced onto the chitin surface under mild enzymatic oxidation conditions in an aqueous solution without changes to the crystallinity of the chitin fibres. FfAA11 was also combined with a simple and environmentally friendly chemical method that transforms recalcitrant chitins into desirable functionalised (nano)materials. The use of ethyl(hydroxyimino)cyanoacetate (Oxyma)-assisted click chemistry allowed the rapid modification of the surface of FfAA11-oxidized chitins, with a fluorescent probe, a peptide, and gold nanoparticles. The chemical steps performed, including the FfAA11 oxidase treatment and surface chemical modification, were achieved without the production of any toxic by-products or waste organic solvents. This approach represents a novel method for the greener production of chitin-based biomaterials.

Place, publisher, year, edition, pages
Royal Society of Chemistry, 2018
National Category
Biocatalysis and Enzyme Technology
Identifiers
urn:nbn:se:kth:diva-227344 (URN)10.1039/c8gc00422f (DOI)000432203600019 ()2-s2.0-85046976116 (Scopus ID)
Funder
Knut and Alice Wallenberg Foundation
Note

QC 20180521

Available from: 2018-05-08 Created: 2018-05-08 Last updated: 2018-12-12Bibliographically approved
Leijon, F., Melzer, M., Zhou, Q., Srivastava, V. & Bulone, V. (2018). Proteomic Analysis of Plasmodesmata From Populus Cell Suspension Cultures in Relation With Callose Biosynthesis.. Frontiers in Plant Science, 9, Article ID 1681.
Open this publication in new window or tab >>Proteomic Analysis of Plasmodesmata From Populus Cell Suspension Cultures in Relation With Callose Biosynthesis.
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2018 (English)In: Frontiers in Plant Science, ISSN 1664-462X, E-ISSN 1664-462X, Vol. 9, article id 1681Article in journal (Refereed) Published
Abstract [en]

Plasmodesmata are channels that link adjacent cells in plant tissues through which molecular exchanges take place. They are involved in multiple processes vital to plant cells, such as responses to hormonal signaling or environmental challenges including osmotic stress, wounding and pathogen attack. Despite the importance of plasmodesmata, their proteome is not well-defined. Here, we have isolated fractions enriched in plasmodesmata from cell suspension cultures of Populus trichocarpa and identified 201 proteins that are enriched in these fractions, thereby providing further insight on the multiple functions of plasmodesmata. Proteomics analysis revealed an enrichment of proteins specifically involved in responses to stress, transport, metabolism and signal transduction. Consistent with the role of callose deposition and turnover in the closure and aperture of the plasmodesmata and our proteomic analysis, we demonstrate the enrichment of callose synthase activity in the plasmodesmata represented by several gene products. A new form of calcium-independent callose synthase activity was detected, in addition to the typical calcium-dependent enzyme activity, suggesting a role of calcium in the regulation of plasmodesmata through two forms of callose synthase activities. Our report provides the first proteomic investigation of the plasmodesmata from a tree species and the direct biochemical evidence for the occurrence of several forms of active callose synthases in these structures. Data are available via ProteomeXchange with identifier PXD010692.

Keywords
Populus, callose, callose synthase, mass spectrometry, plasmodesmata, spectral counting
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:kth:diva-240964 (URN)10.3389/fpls.2018.01681 (DOI)000450425100001 ()30510561 (PubMedID)2-s2.0-85058796619 (Scopus ID)
Note

QC 20190107

Available from: 2019-01-07 Created: 2019-01-07 Last updated: 2019-05-08Bibliographically approved
Srivastava, V., Rezinciuc, S. & Bulone, V. (2018). Quantitative proteomic analysis of four developmental stages of Saprolegnia parasitica. Frontiers in Microbiology, 8(Jan), Article ID 2658.
Open this publication in new window or tab >>Quantitative proteomic analysis of four developmental stages of Saprolegnia parasitica
2018 (English)In: Frontiers in Microbiology, ISSN 1664-302X, E-ISSN 1664-302X, Vol. 8, no Jan, article id 2658Article in journal (Refereed) Published
Abstract [en]

Several water mold species from the Saprolegnia genus infect fish, amphibians, and crustaceans in natural ecosystems and aquaculture farms. Saprolegnia parasitica is one of the most severe fish pathogens. It is responsible for millions of dollars of losses to the aquaculture industry worldwide. Here, we have performed a proteomic analysis, using gel-based and solution (iTRAQ) approaches, of four defined developmental stages of S. parasitica grown in vitro, i.e., the mycelium, primary cysts, secondary cysts and germinated cysts, to gain greater insight into the types of proteins linked to the different stages. A relatively high number of kinases as well as virulence proteins, including the ricin B lectin, disintegrins, and proteases were identified in the S. parasitica proteome. Many proteins associated with various biological processes were significantly enriched in different life cycle stages of S. parasitica. Compared to the mycelium, most of the proteins in the different cyst stages showed similar enrichment patterns and were mainly related to energy metabolism, signal transduction, protein synthesis, and post-translational modifications. The proteins most enriched in the mycelium compared to the cyst stages were associated with amino acid metabolism, carbohydrate metabolism, and mitochondrial energy production. The data presented expand our knowledge of metabolic pathways specifically linked to each developmental stage of this pathogen.

Place, publisher, year, edition, pages
Frontiers Media S.A., 2018
Keywords
Cysts, Fish, Mycelium, Pathogen, Quantitative proteomics, Saprolegnia
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:kth:diva-221748 (URN)10.3389/fmicb.2017.02658 (DOI)000419783400001 ()2-s2.0-85040514056 (Scopus ID)
Funder
Swedish Research Council Formas, 2013-1427
Note

QC 20180124

Available from: 2018-01-24 Created: 2018-01-24 Last updated: 2018-01-29Bibliographically approved
Martins, A., Pfirrmann, T., Heessen, S., Sundqvist, G., Bulone, V., Andreasson, C. & Ljungdahl, P. O. (2018). Ssy5 is a signaling serine protease that exhibits atypical biogenesis and marked S1 specificity. Journal of Biological Chemistry, 293(22), 8362-8378
Open this publication in new window or tab >>Ssy5 is a signaling serine protease that exhibits atypical biogenesis and marked S1 specificity
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2018 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 293, no 22, p. 8362-8378Article in journal (Refereed) Published
Abstract [en]

Ssy5 is a signaling endoprotease that plays a key role in regulating central metabolism, cellular aging, and morphological transitions important for growth and survival of yeast (Saccharomyces cerevisiae) cells. In response to extracellular amino acids, Ssy5 proteolytically activates the transcription factors Stp1 and Stp2, leading to enhanced Ssy1-Ptr3-Ssy5 (SPS) sensor-regulated gene expression. Ssy5 comprises a catalytic (Cat) domain and an extensive regulatory prodomain. Ssy5 is refractory to both broad-spectrum and serine protease-specific inhibitors, confounding its classification as a protease, and no information about Ssy5's cleavage-site preferences and its mechanism of substrate selection is available. Here, using mutational and inhibition experiments, we investigated the biogenesis and catalytic properties of Ssy5 and conclusively show that it is a serine protease. Atypical for the majority of serine proteases, Ssy5's prodomain was obligatorily required in cis during biogenesis for the maturation of the proteolytic activity of the Cat domain. Autolysis and Stp1 and Stp2 cleavage occurred between a cysteine (at the P1 site) and a serine or alanine (at the P1 site) and required residues with short side chains at the P1 site. Substitutions in the Cat domain affecting substrate specificity revealed that residues Phe-634, His-661, and Gly-671 in the S1-binding pocket of this domain are important for Ssy5 catalytic function. This study confirms that the signaling protease Ssy5 is a serine protease and provides a detailed understanding of the biogenesis and intrinsic properties of this key enzyme in yeast.

Place, publisher, year, edition, pages
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2018
Keywords
Saccharomyces cerevisiae, serine protease, signal transduction, substrate specificity, yeast, enzyme structure, environmental sensing, receptor activated proteolysis, signaling protease, SPS sensor, zymogen
National Category
Chemical Sciences
Identifiers
urn:nbn:se:kth:diva-230826 (URN)10.1074/jbc.RA118.002457 (DOI)000434205700004 ()29661936 (PubMedID)2-s2.0-85048036415 (Scopus ID)
Note

QC 20180619

Available from: 2018-06-19 Created: 2018-06-19 Last updated: 2018-06-25Bibliographically approved
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