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Norrby, Marlene
Publications (10 of 10) Show all publications
Lindberg, F. W., Norrby, M., Rahman, M. A., Salhotra, A., Takatsuki, H., Jeppesen, S., . . . Månsson, A. (2018). Controlled Surface Silanization for Actin-Myosin and Biocompatibility of New Polymer Resists. Langmuir, 34(30), 8777-8784
Open this publication in new window or tab >>Controlled Surface Silanization for Actin-Myosin and Biocompatibility of New Polymer Resists
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2018 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 34, no 30, p. 8777-8784Article in journal (Refereed) Published
Abstract [en]

Molecular motor-based nanodevices require organized cytoskeletal filament guiding along motility-promoting tracks, confined by motility-inhibiting walls. One way to enhance motility quality on the tracks, particularly in terms of filament velocity but also the fraction of motile filaments, is to optimize the surface hydrophobicity. We have investigated the potential to achieve this for the actin myosin II motor system on trimethylchlorosilane (TMCS)-derivatized SiO2 surfaces to be used as channel floors in nanodevices. We have also investigated the ability to supress motility on two new polymer resists, TU7 (for nanoimprint lithography) and CSAR 62 (for electron beam and deep UV lithography), to be used as channel walls. We developed a chemical-vapor deposition tool for silanizing SiO2 surfaces in a controlled environment to achieve different surface hydrophobicities (measured by water contact angle). In contrast to previous work, we were able to fabricate a wide range of contact angles by varying the silanization time and chamber pressure using only one type of silane. This resulted in a significant improvement of the silanization procedure, producing a predictable contact angle on the surface and thereby predictable quality of the heavy meromyosin (HMM)-driven actin motility with regard to velocity. We observed a high degree of correlation between the filament sliding velocity and contact angle in the range 10-86 degrees, expanding the previously studied range. We found that the sliding velocity on TU7 surfaces was superior to that on CSAR 62 surfaces despite similar contact angles. In addition, we were able to suppress the motility on both TU7 and CSAR 62 by plasma oxygen treatment before silanization. These results are discussed in relation to previously proposed surface adsorption mechanisms of HMM and their relationship to the water contact angle. Additionally, the results are considered for the development of actin-myosin based nanodevices with superior performance with respect to actin-myosin functionality.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2018
National Category
Biophysics Biochemistry and Molecular Biology
Research subject
Chemistry, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-77391 (URN)10.1021/acs.langmuir.8b01415 (DOI)000440768400007 ()29969272 (PubMedID)2-s2.0-85049637573 (Scopus ID)
Available from: 2018-08-30 Created: 2018-08-30 Last updated: 2019-08-29Bibliographically approved
Fjällström, A.-K., Norrby, M. & Tågerud, S. (2015). Expression and phosphorylation of eukaryotic translation initiation factor 4-gamma (eIF4G) in denervated atrophic and hypertrophic mouse skeletal muscle. Cell Biology International, 39(4), 496-501
Open this publication in new window or tab >>Expression and phosphorylation of eukaryotic translation initiation factor 4-gamma (eIF4G) in denervated atrophic and hypertrophic mouse skeletal muscle
2015 (English)In: Cell Biology International, ISSN 1065-6995, E-ISSN 1095-8355, Vol. 39, no 4, p. 496-501Article in journal (Refereed) Published
Abstract [en]

The eukaryotic translation initiation factor 4-gamma (eIF4G) is important for the initiation of protein synthesis and phosphorylation on S1108 regulates this function of eIF4G. Thus, increased phosphorylation has been reported in conditions associated with increased protein synthesis such as meal feeding and insulin/IGF-1 treatment whereas decreased phosphorylation occurs following starvation, dexamethasone treatment, in sepsis and in atrophic denervated hind-limb muscle. The aim of the present study was to test the hypothesis that S1108 phosphorylation of eIF4G is differentially affected in denervated atrophic hind-limb muscles and denervated hypertrophic hemidiaphragm muscle. Protein expression and phosphorylation in innervated and 6-days denervated atrophic hind-limb muscles (pooled gastrocnemius and soleus) and hypertrophic hemidiaphragms were studied semi-quantitatively using Western blots. Total expression of eIF4G did not change in denervated hind-limb muscles but increased about 77% in denervated hemidiaphragm. S1108 phosphorylated eIF4G decreased about 64% in denervated hind-limb muscles but increased about 1.3-fold in denervated hemidiaphragm. The ratio of S1108 phosphorylated eIF4G to total eIF4G decreased about 60% in denervated hind-limb muscles but no statistically significant change was observed in denervated hemidiaphragm. The differential effect of denervation on eIF4G expression and S1108 phosphorylation in hemidiaphragm (hypertrophic) and hind-limb muscle (atrophic) may represent a regulatory mechanism that helps clarify the differential response of these muscles following denervation.

National Category
Biochemistry and Molecular Biology
Research subject
Natural Science, Biomedical Sciences
Identifiers
urn:nbn:se:lnu:diva-37958 (URN)10.1002/cbin.10402 (DOI)000351678000017 ()25623635 (PubMedID)2-s2.0-84925292774 (Scopus ID)
Available from: 2014-10-31 Created: 2014-10-31 Last updated: 2017-12-05Bibliographically approved
Fjällström, A.-K., Evertsson, K., Norrby, M. & Tågerud, S. (2014). Forkhead box O1 and muscle RING finger 1protein expression in atrophic and hypertrophicdenervated mouse skeletal muscle. Journal of Molecular Signaling, 9, Article ID 9.
Open this publication in new window or tab >>Forkhead box O1 and muscle RING finger 1protein expression in atrophic and hypertrophicdenervated mouse skeletal muscle
2014 (English)In: Journal of Molecular Signaling, ISSN 1750-2187, E-ISSN 1750-2187, Vol. 9, article id 9Article in journal (Refereed) Published
Abstract [en]

Background: Forkhead box O (FoxO) transcription factors and E3 ubiquitin ligases such as Muscle RING finger 1 (MuRF1) are believed to participate in the regulation of skeletal muscle mass. The function of FoxO transcription factors is regulated by post-translational modifications such as phosphorylation and acetylation. In the present study FoxO1 protein expression, phosphorylation and acetylation as well as MuRF1 protein expression, were examined in atrophic and hypertrophic denervated skeletal muscle. Methods: Protein expression, phosphorylation and acetylation were studied semi-quantitatively using Western blots. Muscles studied were 6-days denervated mouse hind-limb muscles (anterior tibial as well as pooled gastrocnemius and soleus muscles, all atrophic), 6-days denervated mouse hemidiaphragm muscles (hypertrophic) and innervated control muscles. Total muscle homogenates were used as well as separated nuclear and cytosolic fractions of innervated and 6-days denervated anterior tibial and hemidiaphragm muscles. Results: Expression of FoxO1 and MuRF1 proteins increased 0.3-3.7-fold in all 6-days denervated muscles studied, atrophic as well as hypertrophic. Phosphorylation of FoxO1 at S256 increased about 0.8-1-fold after denervation in pooled gastrocnemius and soleus muscles and in hemidiaphragm but not in unfractionated anterior tibial muscle. A small (0.2-fold) but statistically significant increase in FoxO1 phosphorylation was, however, observed in cytosolic fractions of denervated anterior tibial muscle. A statistically significant increase in FoxO1 acetylation (0.8-fold) was observed only in denervated anterior tibial muscle. Increases in total FoxO1 and in phosphorylated FoxO1 were only seen in cytosolic fractions of denervated atrophic anterior tibial muscle whereas in denervated hypertrophic hemidiaphragm both total FoxO1 and phosphorylated FoxO1 increased in cytosolic as well as in nuclear fractions. MuRF1 protein expression increased in cytosolic as well as in nuclear fractions of both denervated atrophic anterior tibial muscle and denervated hypertrophic hemidiaphragm muscle. Conclusions: Increased expression of FoxO1 and MuRF1 in denervated muscles (atrophic as well as hypertrophic) suggests that these proteins participate in the tissue remodelling occurring after denervation. The effect of denervation on the level of phosphorylated and acetylated FoxO1 differed in the muscles studied and may be related to differences in fiber type composition of the muscles.

Place, publisher, year, edition, pages
BioMed Central, 2014
Keywords
Acetylation, Atrophy, Denervation, Cytosolic fraction, Forkhead box O, Hypertrophy, MuRF1, Nuclear fraction, Phosphorylation, Skeletal muscle
National Category
Biochemistry and Molecular Biology
Research subject
Natural Science, Biomedical Sciences
Identifiers
urn:nbn:se:lnu:diva-37669 (URN)10.1186/1750-2187-9-9 (DOI)2-s2.0-84907392088 (Scopus ID)
Available from: 2014-10-15 Created: 2014-10-15 Last updated: 2017-12-05Bibliographically approved
Evertsson, K., Fjällström, A.-K., Norrby, M. & Tågerud, S. (2014). p38 mitogen-activated protein kinase and mitogen-activated protein kinase-activated protein kinase 2 (MK2) signaling in atrophic and hypertrophic denervated mouse skeletal muscle. Journal of Molecular Signaling, 9(2)
Open this publication in new window or tab >>p38 mitogen-activated protein kinase and mitogen-activated protein kinase-activated protein kinase 2 (MK2) signaling in atrophic and hypertrophic denervated mouse skeletal muscle
2014 (English)In: Journal of Molecular Signaling, ISSN 1750-2187, E-ISSN 1750-2187, Vol. 9, no 2Article in journal (Refereed) Published
Abstract [en]

BACKGROUND: p38 mitogen-activated protein kinase has been implicated in both skeletal muscle atrophy and hypertrophy. T317 phosphorylation of the p38 substrate mitogen-activated protein kinase-activated protein kinase 2 (MK2) correlates with muscle weight in atrophic and hypertrophic denervated muscle and may influence the nuclear and cytoplasmic distribution of p38 and/or MK2. The present study investigates expression and phosphorylation of p38, MK2 and related proteins in cytosolic and nuclear fractions from atrophic and hypertrophic 6-days denervated skeletal muscles compared to innervated controls.

METHODS: Expression and phosphorylation of p38, MK2, Hsp25 (heat shock protein25rodent/27human, Hsp25/27) and Hsp70 protein expression were studied semi-quantitatively using Western blots with separated nuclear and cytosolic fractions from innervated and denervated hypertrophic hemidiaphragm and atrophic anterior tibial muscles. Unfractionated innervated and denervated atrophic pooled gastrocnemius and soleus muscles were also studied.

RESULTS: No support was obtained for a differential nuclear/cytosolic localization of p38 or MK2 in denervated hypertrophic and atrophic muscle. The differential effect of denervation on T317 phosphorylation of MK2 in denervated hypertrophic and atrophic muscle was not reflected in p38 phosphorylation nor in the phosphorylation of the MK2 substrate Hsp25. Hsp25 phosphorylation increased 3-30-fold in all denervated muscles studied. The expression of Hsp70 increased 3-5-fold only in denervated hypertrophic muscles.

CONCLUSIONS: The study confirms a differential response of MK2 T317 phosphorylation in denervated hypertrophic and atrophic muscles and suggests that Hsp70 may be important for this. Increased Hsp25 phosphorylation in all denervated muscles studied indicates a role for factors other than MK2 in the regulation of this phosphorylation.

Place, publisher, year, edition, pages
BioMed Central, 2014
National Category
Cell Biology
Identifiers
urn:nbn:se:lnu:diva-37957 (URN)10.1186/1750-2187-9-2 (DOI)24629011 (PubMedID)2-s2.0-84899065573 (Scopus ID)
Available from: 2014-10-31 Created: 2014-10-31 Last updated: 2017-12-05Bibliographically approved
Norrby, M., Evertsson, K., Fjällström, A.-K., Svensson, A. & Tågerud, S. (2012). Akt (protein kinase B) isoform phosphorylation and signaling downstream of mTOR (mammalian target of rapamycin) in denervated atrophic and hypertrophic mouse skeletal muscle.. Journal of Molecular Signaling, 7(June), Article ID: 7
Open this publication in new window or tab >>Akt (protein kinase B) isoform phosphorylation and signaling downstream of mTOR (mammalian target of rapamycin) in denervated atrophic and hypertrophic mouse skeletal muscle.
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2012 (English)In: Journal of Molecular Signaling, ISSN 1750-2187, E-ISSN 1750-2187, Vol. 7, no June, p. Article ID: 7-Article in journal (Refereed) Published
Abstract [en]

ABSTRACT: BACKGROUND: The present study examines the hypothesis that Akt (protein kinase B)/mTOR (mammalian target of rapamycin) signaling is increased in hypertrophic and decreased in atrophic denervated muscle. Protein expression and phosphorylation of Akt1, Akt2, glycogen synthase kinase-3beta (GSK-3beta), eukaryotic initiation factor 4E binding protein 1 (4EBP1), 70 kD ribosomal protein S6 kinase (p70S6K1) and ribosomal protein S6 (rpS6) were examined in six-days denervated mouse anterior tibial (atrophic) and hemidiaphragm (hypertrophic) muscles. RESULTS: In denervated hypertrophic muscle expression of total Akt1, Akt2, GSK-3beta, p70S6K1 and rpS6 proteins increased 2-10 fold whereas total 4EBP1 protein remained unaltered. In denervated atrophic muscle Akt1 and Akt2 total protein increased 2-16 fold. A small increase in expression of total rpS6 protein was also observed with no apparent changes in levels of total GSK-3beta, 4EBP1 or p70S6K1 proteins. The level of phosphorylated proteins increased 3-13 fold for all the proteins in hypertrophic denervated muscle. No significant changes in phosphorylated Akt1 or GSK-3beta were detected in atrophic denervated muscle. The phosphorylation levels of Akt2, 4EBP1, p70S6K1 and rpS6 were increased 2-18 fold in atrophic denervated muscle. CONCLUSIONS: The results are consistent with increased Akt/mTOR signaling in hypertrophic skeletal muscle. Decreased levels of phosphorylated Akt (S473/S474) were not observed in denervated atrophic muscle and results downstream of mTOR indicate increased protein synthesis in denervated atrophic anterior tibial muscle as well as in denervated hypertrophic hemidiaphragm muscle. Increased protein degradation, rather than decreased protein synthesis, is likely to be responsible for the loss of muscle mass in denervated atrophic muscles.

National Category
Cell and Molecular Biology Cell Biology Neurosciences
Research subject
Natural Science, Biomedical Sciences
Identifiers
urn:nbn:se:lnu:diva-20341 (URN)10.1186/1750-2187-7-7 (DOI)22657251 (PubMedID)2-s2.0-84861707979 (Scopus ID)
Available from: 2012-06-21 Created: 2012-06-21 Last updated: 2018-01-12Bibliographically approved
Norrby, M. (2011). Gene and protein expression in denervated atrophic and hypertrophic skeletal muscle. (Doctoral dissertation). Växjö, Kalmar: Linnaeus University Press
Open this publication in new window or tab >>Gene and protein expression in denervated atrophic and hypertrophic skeletal muscle
2011 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Following denervation skeletal muscles change their functional and structural properties. Some changes resemble conditions in developing muscles and may be important for reinnervation. Due to inactivity following denervation most skeletal muscles loose muscle mass and become atrophic. The hemidiaphragm muscle, however, undergoes a phase of transient hypertrophy following denervation, gaining weight during the first 6-10 days followed by a decrease in weight. In this thesis the expression (mRNA, protein and protein phosphorylations) of potential factors involved in the regulation of muscle mass were examined in denervated hind-limb and hemidiaphragm muscles.

NIFK is a protein that associates with Ki67, a protein expressed predominantly in proliferating cells. The mRNA expression of NIFK was upregulated in denervated atrophic muscles but unaltered in denervated hypertrophic muscles, suggesting a potential role in the regulation of skeletal muscle mass (Paper I). p38 MAPK has previously been implicated in both anabolic and catabolic processes. Its substrate MK2 becomes phosphorylated at two sites, one of which is suggested to be important for nuclear export. MK2 phosphorylation at this site correlated with muscle weight in both atrophic and hypertrophic denervated muscles and may thus have a role in atrophy and hypertrophy (Paper III). Factors regulating protein synthesis are likely to play a role in atrophy and hypertrophy and many signaling pathways appear to converge on the formation of the translation initiation complex. The protein expression and phosphorylation status of several components in both Wnt and Akt signaling pathways indicate increased protein synthesis in denervated atrophic muscles as well as in denervated hypertrophic muscles (Papers II, IV and V). This suggests that increased protein degradation is more important than decreased protein synthesis for the loss of muscle mass in denervated atrophic muscles.

Place, publisher, year, edition, pages
Växjö, Kalmar: Linnaeus University Press, 2011
Series
Linnaeus University Dissertations ; 34/2011
Keywords
Skeletal muscle, Denervation, Hypertrophy, Atrophy, Gene expression, Protein expression, Protein phosphorylation, NIFK, Wnt, MK2, Akt signaling
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:lnu:diva-10411 (URN)978-91-86491-61-1 (ISBN)
Public defence
2011-03-11, N2007, Smålandsgatan 24, Kalmar, 09:00 (Swedish)
Supervisors
Available from: 2011-01-31 Created: 2011-01-28 Last updated: 2014-05-09Bibliographically approved
Månsson, A., Norrby, M. & Tågerud, S. (2011). Molecular Motors and Self-Healing at the Neuromuscular Synapse (1ed.). In: Vincenzo Amendola & Moreno Meneghetti (Ed.), Self-Healing at the Nanoscale: Mechanisms and Key Concepts of Natural and Artificial Systems (pp. 357-394). CRC Press
Open this publication in new window or tab >>Molecular Motors and Self-Healing at the Neuromuscular Synapse
2011 (English)In: Self-Healing at the Nanoscale: Mechanisms and Key Concepts of Natural and Artificial Systems / [ed] Vincenzo Amendola & Moreno Meneghetti, CRC Press, 2011, 1, p. 357-394Chapter in book (Other academic)
Place, publisher, year, edition, pages
CRC Press, 2011 Edition: 1
National Category
Cell Biology
Research subject
Natural Science, Biomedical Sciences
Identifiers
urn:nbn:se:lnu:diva-16291 (URN)978-1439854730 (ISBN)
Funder
Swedish Research Council, 621-2010-5146
Available from: 2011-12-21 Created: 2011-12-21 Last updated: 2015-09-14Bibliographically approved
Norrby, M. & Tågerud, S. (2010). Mitogen-activated protein kinase-activated protein kinase 2 (MK2) in skeletal muscle atrophy and hypertrophy. Journal of Cellular Physiology, 223(1), 194-201
Open this publication in new window or tab >>Mitogen-activated protein kinase-activated protein kinase 2 (MK2) in skeletal muscle atrophy and hypertrophy
2010 (English)In: Journal of Cellular Physiology, ISSN 0021-9541, E-ISSN 1097-4652, Vol. 223, no 1, p. 194-201Article in journal (Refereed) Published
Abstract [en]

Skeletal muscle is a highly plastic tissue. Overall muscle growth (hypertrophy) or muscle wasting (atrophy) results from alterations in intracellular signaling pathways with important regulatory steps occurring in the nucleus as well as in the cytoplasm. Previous studies have identified components of the Akt/mTor pathway as well as the p38 MAPK pathway as important for skeletal muscle hypertrophy and/or atrophy. The present study tests the hypothesis that MK2, a substrate of p38 which following phosphorylation, can be exported from the nucleus in a complex with p38, may be important for skeletal muscle growth. The expression of MK2 was examined in denervated mouse hind-limb (atrophic) and hemidiaphragm (transiently hypertrophic) muscles. MK2 mRNA expression decreased after denervation in both atrophic (48% of innervated controls, P < 0.001) and hypertrophic muscle (34% of innervated controls, P < 0.01) but MK2 protein expression decreased only in atrophic muscle (32% of innervated controls, P < 0.01). The level of T205 phosphorylated MK2 increased after denervation in both atrophic (fourfold increase, P < 0.01) and hypertrophic muscles (almost sevenfold increase, P < 0.001) whereas the level of T317 phosphorylated MK2 (necessary for nuclear export) increased after denervation in hypertrophic muscle (nearly threefold increase, P < 0.001) but not in atrophic muscle. Logarithmically transformed relative changes in MK2 phosphorylated at T317 correlated well (r2 = 0.7737) with relative changes in muscle weight. The results suggest a role for MK2 in the regulation of muscle mass, a role which, at least in part, may be related to determining the subcellular localization of p38 in muscle fibers. J. Cell. Physiol. 223: 194–201,

Place, publisher, year, edition, pages
Wiley-Liss, Inc., 2010
National Category
Pharmacology and Toxicology
Research subject
Biomedical Sciences, Pharmacology; Natural Science, Biomedical Sciences
Identifiers
urn:nbn:se:lnu:diva-2134 (URN)10.1002/jcp.22023 (DOI)
Available from: 2010-04-06 Created: 2010-04-06 Last updated: 2018-01-12Bibliographically approved
Svensson, A., Norrby, M., Libelius, R. & Tågerud, S. (2008). Secreted frizzled related protein 1 (Sfrp1) and Wnt signaling in innervated and denervated skeletal muscle.. Journal of Molecular Histology, 39(3), 329-337
Open this publication in new window or tab >>Secreted frizzled related protein 1 (Sfrp1) and Wnt signaling in innervated and denervated skeletal muscle.
2008 (English)In: Journal of Molecular Histology, ISSN 1567-2379, E-ISSN 1567-2387, Vol. 39, no 3, p. 329-337Article in journal (Refereed) Published
Abstract [en]

Wnts are secreted proteins with functions in differentiation, development and cell proliferation. Wnt signaling has also been implicated in neuromuscular junction formation and may function in synaptic plasticity in the adult as well. Secreted frizzled-related proteins (Sfrps) such as Sfrp1 can function as inhibitors of Wnt signaling. In the present study a potential role of Wnt signaling in denervation was examined by comparing the expression levels of Sfrp1 and key proteins in the canonical Wnt pathway, Dishevelled, glycogen synthase kinase 3 beta and beta-catenin, in innervated and denervated rodent skeletal muscle. Sfrp1 mRNA and immunoreactivity were found to be up-regulated in mouse hemidiaphragm muscle following denervation. Immunoreactivity, detected by Western blots, and mRNA, detected by Northern blots, were both expressed in extrasynaptic as well as perisynaptic parts of the denervated muscle. Immunoreactivity on tissue sections was, however, found to be concentrated postsynaptically at neuromuscular junctions. Using beta-catenin levels as a readout for canonical Wnt signaling no evidence for decreased canonical Wnt signaling was obtained in denervated muscle. A role for Sfrp1 in denervated muscle, other than interfering with canonical Wnt signaling, is discussed.

National Category
Pharmacology and Toxicology
Research subject
Biomedical Sciences, Pharmacology
Identifiers
urn:nbn:se:lnu:diva-1721 (URN)10.1007/s10735-008-9169-y (DOI)
Available from: 2010-04-06 Created: 2010-04-06 Last updated: 2018-01-12Bibliographically approved
Tågerud, S., Magnusson, C., Norrby, M. & Libelius, R. (2003). The nifk gene is widely expressed in mouse tissues and is up-regulated in denervated hind limb muscle. Cell Biology International, 27(6), 469-475
Open this publication in new window or tab >>The nifk gene is widely expressed in mouse tissues and is up-regulated in denervated hind limb muscle
2003 (English)In: Cell Biology International, ISSN 1065-6995, E-ISSN 1095-8355, Vol. 27, no 6, p. 469-475Article in journal (Refereed) Published
Abstract [en]

Denervation of skeletal muscle alters the expression of many genes, which may be important for establishing optimal conditions for reinnervation. Using the differential display technique we have attempted to discover neurally regulated genes in skeletal muscle. An mRNA that is up-regulated in denervated hind limb muscle was identified and cloned. The cDNA encodes an RNA-binding protein, which was discovered during the course of this work to be a nucleolar protein interacting with the fork-head associated domain of the proliferation marker protein Ki-67, and named NIFK. We show that the nifk gene is widely expressed in adult mouse tissues and that the expression is up-regulated in denervated hind limb muscle. No difference between expression in perisynaptic and extrasynaptic portions of muscle was observed. The widespread expression in adult tissues suggests that the NIFK protein has other functions in addition to its interaction with Ki-67, which is only expressed in proliferating cells.

National Category
Pharmacology and Toxicology
Research subject
Biomedical Sciences, Pharmacology; Natural Science, Biomedical Sciences
Identifiers
urn:nbn:se:lnu:diva-343 (URN)10.1016/S1065-6995(03)00038-6 (DOI)
Available from: 2010-03-31 Created: 2010-03-31 Last updated: 2018-01-12Bibliographically approved
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