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Article ; Online: BMPR1B gene in brachydactyly type 2-A family with de novo R486W mutation and a disease phenotype.

Bednarek, Marcin / Trybus, Marek / Kolanowska, Monika / Koziej, Mateusz / Kiec-Wilk, Beata / Dobosz, Artur / Kotlarek-Łysakowska, Marta / Kubiak-Dydo, Anna / Użarowska-Gąska, Ewelina / Staręga-Rosłan, Julia / Gaj, Paweł / Górzyńska, Izabela / Serwan, Katarzyna / Świerniak, Michał / Kot, Adam / Jażdżewski, Krystian / Wójcicka, Anna

Molecular genetics & genomic medicine

2021 Volume 9, Issue 3, Page(s) e1594

Abstract: Background: Brachydactylies are a group of inherited conditions, characterized mainly by the presence of shortened fingers and toes. Based on the patients' phenotypes, brachydactylies have been subdivided into 10 subtypes. In this study, we have ... ...

Abstract	Background: Brachydactylies are a group of inherited conditions, characterized mainly by the presence of shortened fingers and toes. Based on the patients' phenotypes, brachydactylies have been subdivided into 10 subtypes. In this study, we have identified a family with two members affected by brachydactyly type A2 (BDA2). BDA2 is caused by mutations in three genes: BMPR1B, BMP2 or GDF5. So far only two studies have reported the BDA2 cases caused by mutations in the BMPR1B gene. Methods: We employed next-generation sequencing to identify mutations in culpable genes. Results and conclusion: In this paper, we report a case of BDA2 resulting from the presence of a heterozygous c.1456C>T, p.Arg486Trp variant in BMPR1B, which was previously associated with BDA2. The next generation sequencing analysis of the patients' family revealed that the mutation occurred de novo in the proband and was transmitted to his 26-month-old son. Although the same variant was confirmed in both patients, their phenotypes were different with more severe manifestation of the disease in the adult.
MeSH term(s)	Adult ; Bone Morphogenetic Protein Receptors, Type I/genetics ; Brachydactyly/genetics ; Brachydactyly/pathology ; Child, Preschool ; Humans ; Male ; Mutation, Missense ; Pedigree ; Phenotype
Chemical Substances	BMPR1B protein, human (EC 2.7.11.30) ; Bone Morphogenetic Protein Receptors, Type I (EC 2.7.11.30)
Language	English
Publishing date	2021-01-24
Publishing country	United States
Document type	Case Reports ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2734884-2
ISSN	2324-9269 ; 2324-9269
ISSN (online)	2324-9269
ISSN	2324-9269
DOI	10.1002/mgg3.1594
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Article ; Online: Nucleotide sequence of miRNA precursor contributes to cleavage site selection by Dicer.

Starega-Roslan, Julia / Galka-Marciniak, Paulina / Krzyzosiak, Wlodzimierz J

Nucleic acids research

2015 Volume 43, Issue 22, Page(s) 10939–10951

Abstract: The ribonuclease Dicer excises mature miRNAs from a diverse group of precursors (pre-miRNAs), most of which contain various secondary structure motifs in their hairpin stem. In this study, we analyzed Dicer cleavage in hairpin substrates deprived of such ...

Abstract	The ribonuclease Dicer excises mature miRNAs from a diverse group of precursors (pre-miRNAs), most of which contain various secondary structure motifs in their hairpin stem. In this study, we analyzed Dicer cleavage in hairpin substrates deprived of such motifs. We searched for the factors other than the secondary structure, which may influence the length diversity and heterogeneity of miRNAs. We found that the nucleotide sequence at the Dicer cleavage site influences both of these miRNA characteristics. With regard to cleavage mechanism, we demonstrate that the Dicer RNase IIIA domain that cleaves within the 3' arm of the pre-miRNA is more sensitive to the nucleotide sequence of its substrate than is the RNase IIIB domain. The RNase IIIA domain avoids releasing miRNAs with G nucleotide and prefers to generate miRNAs with a U nucleotide at the 5' end. We also propose that the sequence restrictions at the Dicer cleavage site might be the factor that contributes to the generation of miRNA duplexes with 3' overhangs of atypical lengths. This finding implies that the two RNase III domains forming the single processing center of Dicer may exhibit some degree of flexibility, which allows for the formation of these non-standard 3' overhangs.
MeSH term(s)	Base Sequence ; MicroRNAs/chemistry ; MicroRNAs/metabolism ; Nucleic Acid Conformation ; RNA Cleavage ; RNA Precursors/chemistry ; RNA Precursors/metabolism ; RNA-Binding Proteins/metabolism ; Ribonuclease III/metabolism
Chemical Substances	MicroRNAs ; RNA Precursors ; RNA-Binding Proteins ; trans-activation responsive RNA-binding protein (136628-24-5) ; Ribonuclease III (EC 3.1.26.3)
Language	English
Publishing date	2015-12-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkv968
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Article ; Online: Analysis of microRNA length variety generated by recombinant human Dicer.

Starega-Roslan, Julia / Krzyzosiak, Wlodzimierz J

Methods in molecular biology (Clifton, N.J.)

2013 Volume 936, Page(s) 21–34

Abstract: miRNAs are a large subgroup of noncoding regulatory RNAs, which vary in length within the 20-25 nt range and show substantial length diversity and heterogeneity. To analyze the latter phenomenon, we recently developed high-resolution northern blotting ... ...

Abstract	miRNAs are a large subgroup of noncoding regulatory RNAs, which vary in length within the 20-25 nt range and show substantial length diversity and heterogeneity. To analyze the latter phenomenon, we recently developed high-resolution northern blotting and employed this method to investigate cleavages generated by recombinant human Dicer in the synthetic miRNA precursors. We paid special care to visualize clearly the cleavages generated by the individual RNase III domains of Dicer. We have compared the results of northern blotting with the results of standard analysis with the use of end-labeled RNA and visualization of Dicer cleavage products by autoradiography. The point-by-point steps of substrate preparation, recombinant Dicer cleavage assay, and northern blotting are described in this manuscript.
MeSH term(s)	Blotting, Northern/methods ; DEAD-box RNA Helicases/genetics ; DEAD-box RNA Helicases/metabolism ; Humans ; MicroRNAs/chemistry ; MicroRNAs/genetics ; MicroRNAs/metabolism ; Oligonucleotides/chemistry ; Oligonucleotides/metabolism ; Recombinant Proteins ; Ribonuclease III/genetics ; Ribonuclease III/metabolism ; Staining and Labeling/methods
Chemical Substances	MicroRNAs ; Oligonucleotides ; Recombinant Proteins ; DICER1 protein, human (EC 3.1.26.3) ; Ribonuclease III (EC 3.1.26.3) ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2013
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-62703-083-0_2
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Article ; Online: Identifying proteins that bind to specific RNAs - focus on simple repeat expansion diseases.

Jazurek, Magdalena / Ciesiolka, Adam / Starega-Roslan, Julia / Bilinska, Katarzyna / Krzyzosiak, Wlodzimierz J

Nucleic acids research

2016 Volume 44, Issue 19, Page(s) 9050–9070

Abstract: RNA-protein complexes play a central role in the regulation of fundamental cellular processes, such as mRNA splicing, localization, translation and degradation. The misregulation of these interactions can cause a variety of human diseases, including ... ...

Abstract	RNA-protein complexes play a central role in the regulation of fundamental cellular processes, such as mRNA splicing, localization, translation and degradation. The misregulation of these interactions can cause a variety of human diseases, including cancer and neurodegenerative disorders. Recently, many strategies have been developed to comprehensively analyze these complex and highly dynamic RNA-protein networks. Extensive efforts have been made to purify in vivo-assembled RNA-protein complexes. In this review, we focused on commonly used RNA-centric approaches that involve mass spectrometry, which are powerful tools for identifying proteins bound to a given RNA. We present various RNA capture strategies that primarily depend on whether the RNA of interest is modified. Moreover, we briefly discuss the advantages and limitations of in vitro and in vivo approaches. Furthermore, we describe recent advances in quantitative proteomics as well as the methods that are most commonly used to validate robust mass spectrometry data. Finally, we present approaches that have successfully identified expanded repeat-binding proteins, which present abnormal RNA-protein interactions that result in the development of many neurological diseases.
MeSH term(s)	Animals ; Aptamers, Nucleotide ; Bacterial Proteins ; CRISPR-Associated Proteins ; Clustered Regularly Interspaced Short Palindromic Repeats ; DNA Repeat Expansion ; Endoribonucleases ; Genetic Association Studies ; Genetic Predisposition to Disease ; Humans ; Mass Spectrometry/methods ; Proteomics/methods ; RNA/chemistry ; RNA/genetics ; RNA, Antisense ; RNA-Binding Proteins/metabolism ; Reproducibility of Results ; SELEX Aptamer Technique
Chemical Substances	Aptamers, Nucleotide ; Bacterial Proteins ; CRISPR-Associated Proteins ; RNA, Antisense ; RNA-Binding Proteins ; RNA (63231-63-0) ; Csy4 endoribonuclease, Pseudomonas aeruginosa (EC 3.1.-) ; Endoribonucleases (EC 3.1.-)
Language	English
Publishing date	2016-11-02
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkw803
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Article ; Online: The role of Dicer protein partners in the processing of microRNA precursors.

Koscianska, Edyta / Starega-Roslan, Julia / Krzyzosiak, Wlodzimierz J

PloS one

2011 Volume 6, Issue 12, Page(s) e28548

Abstract: One of the cellular functions of the ribonuclease Dicer is to process microRNA precursors (pre-miRNAs) into mature microRNAs (miRNAs). Human Dicer performs this function in cooperation with its protein partners, AGO2, PACT and TRBP. The exact role of ... ...

Abstract	One of the cellular functions of the ribonuclease Dicer is to process microRNA precursors (pre-miRNAs) into mature microRNAs (miRNAs). Human Dicer performs this function in cooperation with its protein partners, AGO2, PACT and TRBP. The exact role of these accessory proteins in Dicer activity is still poorly understood. In this study, we used the northern blotting technique to investigate pre-miRNA cleavage efficiency and specificity after depletion of AGO2, PACT and TRBP by RNAi. The results showed that the inhibition of either Dicer protein partner substantially affected not only miRNA levels but also pre-miRNA levels, and it had a rather minor effect on the specificity of Dicer cleavage. The analysis of the Dicer cleavage products generated in vitro revealed the presence of a cleavage intermediate when pre-miRNA was processed by recombinant Dicer alone. This intermediate was not observed during pre-miRNA cleavage by endogenous Dicer. We demonstrate that AGO2, PACT and TRBP were required for the efficient functioning of Dicer in cells, and we suggest that one of the roles of these proteins is to assure better synchronization of cleavages triggered by two RNase III domains of Dicer.
MeSH term(s)	Argonaute Proteins/metabolism ; Blotting, Northern ; Blotting, Western ; DEAD-box RNA Helicases/metabolism ; HeLa Cells ; Humans ; MicroRNAs/metabolism ; Models, Biological ; Oligonucleotides/chemistry ; Protein Binding ; RNA Interference ; RNA Precursors/genetics ; RNA Processing, Post-Transcriptional ; RNA-Binding Proteins/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Ribonuclease III/chemistry ; Ribonuclease III/metabolism
Chemical Substances	AGO2 protein, human ; Argonaute Proteins ; MicroRNAs ; Oligonucleotides ; PRKRA protein, human ; RNA Precursors ; RNA-Binding Proteins ; Recombinant Proteins ; trans-activation responsive RNA-binding protein (136628-24-5) ; DICER1 protein, human (EC 3.1.26.3) ; Ribonuclease III (EC 3.1.26.3) ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2011-12-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0028548
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Article ; Online: Sequence features of Drosha and Dicer cleavage sites affect the complexity of isomiRs.

Starega-Roslan, Julia / Witkos, Tomasz M / Galka-Marciniak, Paulina / Krzyzosiak, Wlodzimierz J

International journal of molecular sciences

2015 Volume 16, Issue 4, Page(s) 8110–8127

Abstract: The deep-sequencing of small RNAs has revealed that different numbers and proportions of miRNA variants called isomiRs are formed from single miRNA genes and that this effect is attributable mainly to imprecise cleavage by Drosha and Dicer. Factors that ... ...

Abstract	The deep-sequencing of small RNAs has revealed that different numbers and proportions of miRNA variants called isomiRs are formed from single miRNA genes and that this effect is attributable mainly to imprecise cleavage by Drosha and Dicer. Factors that influence the degree of cleavage precision of Drosha and Dicer are under investigation, and their identification may improve our understanding of the mechanisms by which cells modulate the regulatory potential of miRNAs. In this study, we focused on the sequences and structural determinants of Drosha and Dicer cleavage sites, which may explain the generation of homogeneous miRNAs (in which a single isomiR strongly predominates) as well as the generation of heterogeneous miRNAs. Using deep-sequencing data for small RNAs, we demonstrate that the generation of homogeneous miRNAs requires more sequence constraints at the cleavage sites than the formation of heterogeneous miRNAs. Additionally, our results indicate that specific Drosha cleavage sites have more sequence determinants in miRNA precursors than specific cleavage sites for Dicer and that secondary structural motifs in the miRNA precursors influence the precision of Dicer cleavage. Together, we present the sequence and structural features of Drosha and Dicer cleavage sites that influence the heterogeneity of the released miRNAs.
MeSH term(s)	Cell Line ; DEAD-box RNA Helicases/genetics ; HEK293 Cells ; Humans ; MicroRNAs/genetics ; RNA Cleavage/genetics ; RNA Isoforms/genetics ; RNA Precursors/genetics ; Ribonuclease III/genetics ; Sequence Analysis, RNA/methods
Chemical Substances	MicroRNAs ; RNA Isoforms ; RNA Precursors ; DICER1 protein, human (EC 3.1.26.3) ; DROSHA protein, human (EC 3.1.26.3) ; Ribonuclease III (EC 3.1.26.3) ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2015-04-10
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms16048110
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Article ; Online: Characterization of a naturally occurring truncated Dicer.

Mosca, Nicola / Starega-Roslan, Julia / Castiello, Filomena / Russo, Aniello / Krzyzosiak, Wlodzimierz J / Potenza, Nicoletta

Molecular biology reports

2015 Volume 42, Issue 8, Page(s) 1333–1340

Abstract: Dicer is central to small RNA silencing pathways, thus playing an important role in physiological and pathological states. Recently, a number of mutations in dicer gene have been identified in diverse types of cancer, implicating Dicer in oncogenic ... ...

Abstract	Dicer is central to small RNA silencing pathways, thus playing an important role in physiological and pathological states. Recently, a number of mutations in dicer gene have been identified in diverse types of cancer, implicating Dicer in oncogenic cooperation. Here we report on the properties of a rare splice variant of the human dicer gene, occurring in neuroblastoma cells, and not detectable in normal tissues. Due to the skipping of one exon, the alternatively spliced transcript encodes a putative truncated protein, t-Dicer, lacking the dsRNA-binding domain and bearing altered one of the two RNase III catalytic centers. The ability of the exon-depleted t-dicer transcript to be translated in vitro was first investigated by the expression of flagged t-Dicer in human cells. We found that t-dicer transcript could be translated in vitro, albeit not as efficiently as full-length dicer transcript. Then, the possible enzymatic activity of t-Dicer was analyzed by an in vitro dicing assay able to distinguish the enzymatic activity of the individual RNase III domains. We showed that t-Dicer preserved partial dicing activity. Overall, the results indicate that t-dicer transcript could produce a protein still able to bind the substrate and to cleave only one of the two pre-miRNA strands. Given the increasing number of mutations reported for dicer gene in tumours, our experimental approach could be useful to characterize the activity of these mutants, which may dictate changes in selected classes of small RNAs and/or lead to their aberrant maturation.
MeSH term(s)	Alternative Splicing ; Catalytic Domain ; Enzyme Assays ; Exons ; Gene Expression ; Humans ; MicroRNAs/metabolism ; Neuroblastoma/enzymology ; Neuroblastoma/genetics ; Ribonuclease III/genetics ; Ribonuclease III/metabolism
Chemical Substances	MicroRNAs ; Ribonuclease III (EC 3.1.26.3)
Language	English
Publishing date	2015-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186544-4
ISSN	1573-4978 ; 0301-4851
ISSN (online)	1573-4978
ISSN	0301-4851
DOI	10.1007/s11033-015-3878-6
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Article ; Online: High-resolution northern blot for a reliable analysis of microRNAs and their precursors.

Koscianska, Edyta / Starega-Roslan, Julia / Czubala, Katarzyna / Krzyzosiak, Wlodzimierz J

TheScientificWorldJournal

2011 Volume 11, Page(s) 102–117

Abstract: This protocol describes how to perform northern blot analyses to detect microRNAs and their precursors with single-nucleotide resolution, which is crucial for analyzing individual length variants and for evaluating relative quantities of unique microRNAs ...

Abstract	This protocol describes how to perform northern blot analyses to detect microRNAs and their precursors with single-nucleotide resolution, which is crucial for analyzing individual length variants and for evaluating relative quantities of unique microRNAs in cells. Northern blot analysis consists of resolving RNAs by gel electrophoresis, followed by transferring and fixing to nylon membranes as well as detecting by hybridization with radioactive probes. Earlier efforts to improve this method focused mainly on altering the sensitivity of short RNA detection. We have enhanced the resolution of the northern blot technique by optimizing the electrophoresis step. We have also investigated other steps of the procedure with the goal of enhancing the resolution of RNAs; herein, we present several recommendations to do so. Our protocol is applicable to analyses of all kinds of endogenous and exogenous RNAs, falling within length ranges of 20-30 and 50-70 nt, corresponding to microRNA and pre-microRNA lengths, respectively.
MeSH term(s)	Blotting, Northern/methods ; Humans ; MicroRNAs/genetics ; Reproducibility of Results
Chemical Substances	MicroRNAs
Language	English
Publishing date	2011-01-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2075968-X
ISSN	1537-744X ; 1537-744X
ISSN (online)	1537-744X
ISSN	1537-744X
DOI	10.1100/tsw.2011.11
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Article ; Online: The role of the precursor structure in the biogenesis of microRNA.

Starega-Roslan, Julia / Koscianska, Edyta / Kozlowski, Piotr / Krzyzosiak, Wlodzimierz J

Cellular and molecular life sciences : CMLS

2011 Volume 68, Issue 17, Page(s) 2859–2871

Abstract: The human genome contains more than 1,000 microRNA (miRNA) genes, which are transcribed mainly by RNA polymerase II. The canonical pathway of miRNA biogenesis includes the nuclear processing of primary transcripts (pri-miRNAs) by the ribonuclease Drosha ... ...

Abstract	The human genome contains more than 1,000 microRNA (miRNA) genes, which are transcribed mainly by RNA polymerase II. The canonical pathway of miRNA biogenesis includes the nuclear processing of primary transcripts (pri-miRNAs) by the ribonuclease Drosha and further cytoplasmic processing of pre-miRNAs by the ribonuclease Dicer. This review discusses the issue of miRNA end heterogeneity generated primarily by Drosha and Dicer cleavage and focuses on the structural aspects of the Dicer step of miRNA biogenesis. We examine the structures of miRNA precursors, both predicted and experimentally determined, as well as the influence of various motifs that disturb the regularity of pre-miRNA structure on Dicer cleavage specificity. We evaluate the structural determinants of the length diversity of miRNA generated by Dicer from different precursors and highlight the importance of asymmetrical motifs. Finally, we discuss the impact of Dicer protein partners on cleavage efficiency and specificity and propose the contribution of pre-miRNA structural plasticity to the dynamics of the dicing complex.
MeSH term(s)	Humans ; MicroRNAs/chemistry ; MicroRNAs/metabolism ; RNA Precursors/chemistry ; RNA Precursors/metabolism ; RNA Precursors/physiology ; RNA Processing, Post-Transcriptional ; Ribonuclease III/metabolism
Chemical Substances	MicroRNAs ; RNA Precursors ; Ribonuclease III (EC 3.1.26.3)
Language	English
Publishing date	2011-05-24
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-011-0726-2
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Article: siRNA release from pri-miRNA scaffolds is controlled by the sequence and structure of RNA.

Galka-Marciniak, Paulina / Olejniczak, Marta / Starega-Roslan, Julia / Szczesniak, Michal W / Makalowska, Izabela / Krzyzosiak, Wlodzimierz J

Biochimica et biophysica acta

2016 Volume 1859, Issue 4, Page(s) 639–649

Abstract: shmiRs are pri-miRNA-based RNA interference triggers from which exogenous siRNAs are expressed in cells to silence target genes. These reagents are very promising tools in RNAi in vivo applications due to their good activity profile and lower toxicity ... ...

Abstract	shmiRs are pri-miRNA-based RNA interference triggers from which exogenous siRNAs are expressed in cells to silence target genes. These reagents are very promising tools in RNAi in vivo applications due to their good activity profile and lower toxicity than observed for other vector-based reagents such as shRNAs. In this study, using high-resolution northern blotting and small RNA sequencing, we investigated the precision with which RNases Drosha and Dicer process shmiRs. The fidelity of siRNA release from the commonly used pri-miRNA shuttles was found to depend on both the siRNA insert and the pri-miR scaffold. Then, we searched for specific factors that may affect the precision of siRNA release and found that both the structural features of shmiR hairpins and the nucleotide sequence at Drosha and Dicer processing sites contribute to cleavage site selection and cleavage precision. An analysis of multiple shRNA intermediates generated from several reagents revealed the complexity of shmiR processing by Drosha and demonstrated that Dicer selects substrates for further processing. Aside from providing new basic knowledge regarding the specificity of nucleases involved in miRNA biogenesis, our results facilitate the rational design of more efficient genetic reagents for RNAi technology.
MeSH term(s)	Base Sequence/genetics ; DEAD-box RNA Helicases/genetics ; DEAD-box RNA Helicases/metabolism ; HEK293 Cells ; Humans ; MicroRNAs/biosynthesis ; MicroRNAs/genetics ; Nucleic Acid Conformation ; RNA Interference ; RNA Processing, Post-Transcriptional/genetics ; RNA, Small Interfering/genetics ; Ribonuclease III/genetics ; Ribonuclease III/metabolism
Chemical Substances	MicroRNAs ; RNA, Small Interfering ; DICER1 protein, human (EC 3.1.26.3) ; DROSHA protein, human (EC 3.1.26.3) ; Ribonuclease III (EC 3.1.26.3) ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2016-04
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagrm.2016.02.014
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