Marko Hyvönen

Brief scientific bio

Marko comes from Helsinki, Finland, as you might guess from his name.
As an accidental biochemist, he did not know what to do after school (and failing, thankfully, to get into medical school), but somehow got to study chemistry at the University of Helsinki. Not getting his head around Streitwieser and Heathcock’s Introduction to Organic Chemistry and all those reactions (possibly thanks to working in a video rental store in the evenings instead of studying), he switched to biochemistry, graduating in 1991.

After a couple of years working on Semilki Forest virus replication protein in the group of Leevi Kääriäinen at the Institute of Biochemistry at the University of Helsinki, he secured a PhD studentship at EMBL in Heidelberg, Germany where he was bitten by the structural biology bug.

His PhD project in the group of late Matti Saraste was focused on understanding how newly discovered pleckstrin homology (PH) and WW domains function, and was awarded a PhD at the end of 1997, again from university of Helsinki (EMBL does not award its own degrees). He received Komppa’s prize from the Finnish Society of Chemists for the best PhD thesis in the field of chemistry that year in Finland; he is still to figure out why – he quit chemistry after all!. You can read his thesis (printed in B5 format and just 66 pages, described as an STD pamflet by some) here.

In January 1998 Marko drove his earthly belonging across the English Channel and joined the Department of Biochemistry in Cambridge as an EMBO and HFSPO-funded postdoctoral fellow in the group of Tom Blundell. He started then the still ongoing work on activins and TGF-β family growth factors.
He was awarded a BBSRC David Phillips Fellowship to study the regulation of activin A signalling by extracellular proteins in 2000 and with that he established his independent research programme and group in Jan 2001.

Around 2006 Marko and his group joined forces with late Chris Abell, Tom Blundell , David Spring and Ashok Venkitaraman to develop small molecule inhibitors of protein-protein interactions and other regulatory sites using fragment-based drug discovery (FBDD) methods, targeting RAD51, Aurora A and CK2α.

Marko has collaborated with Florian Hollfelder‘s group in the same Department for well over 10 years, providing structural biology support for their enzyme discovery, mechanism and directed eveolution efforts.

Outside Cambridge he is collaborating with Caroline Hill at the Crick, Petra Knaus at Frei Unviersity of Berlin, Morten Grøtli at the University of Göteborg and Andrea Balan at the University of São Paulo, among others.

In 2008 Marko was appointed as a University Lecturer at the Department of Biochemistry, promoted to a Reader of Protein Biochemistry in 2018 and is currently (forever?) a Professor in Protein Biochemistry (thanks to the change of academic titles in Cambridge in 2021).

In 2016, together with Dr Catherine Elton, Marko founded in 2016 a spin-out company Qkine for the development of next generation growth factors for stem cell research and regenerative medicine. This is continuation and expansion of his work on providing growth factors for Cambridge stem labs for over 10 years.

Links to external portals:

Departmental website: www.bioc.cam.ac.uk/people/uto/hyvonen (horror)
Twitter: @HyvonenGroup (not just science!)
LinkedIn: Marko Hyvönen (the cleaner side)
ORCiD: 0000-0001-8683-4070 (who ever looks at this?)

Publications

(As of Aug 2022 – search “Hyvonen-M [AU] AND Cambridge” in PubMed for the latest ones)

S. Neun, P. Brear, E. Campbell, T. Tryfona, K. El Omari, A. Wagner, P. Dupree, M. Hyvönen, F. Hollfelder, Functional metagenomic screening identifies an unexpected β-glucuronidase. Nature Chemical Biology. Online ahead of print, 2022. https://doi.org/10.1038/s41589-022-01071-x.
Y. Karusheva, M. Ratcliff, A. Melvin, A. Mörseburg, N. Sattar, P. Barker, K. Burling, A. Backmark, R. Roth, L. Jermutus, E. Guiu-Jurado, M. Blüher, P. Welsh, M. Hyvönen, S. O’Rahilly. MedRxiv, 2022. The common H202D variant in GDF-15 does not affect its bioactivity but can significantly interfere with measurement of its circulating levels. The Journal of Applied Laboratory Medicine, Advance article, 2022. https://doi.org/10.1093/jalm/jfac055
T. Pantelejevs, M. Hyvönen. Divergent binding mode for a protozoan BRC repeat to RAD51. Biochemical Journal, 479: 1031–1043, 2022. https://doi.org/10.1042/bcj20220141
E. L. Atkinson, J. Iegre, C. D’Amore, P. Brear, M. Salvi, M. Hyvönen and D. R. Spring. Development of small cyclic peptides targeting the CK2α/β interface. Chemical Communications, 58: 791-479, 2022. https://doi.org/10.1039/D2CC00707J
A. Nain-Perez, A. Foller Füchtbauer, L. Håversen, A. Lulla C. Gao, J. Matic, L. Monjas, A. Rodríguez P. Brear , W. Kim, M. Hyvönen, J. Borén, A. Mardinoglu, M. Uhlen, M. Grøtli. Anthraquinone derivatives as ADP-competitive inhibitors of liver pyruvate kinase. European Journal of Medicinal Chemistry, 23:114270, 2022. https://doi.org/10.1016/j.ejmech.2022.114270
C. Talbot-Cooper, T. Pantelejevs, J. P. Shannon, C. R. Cherry, M. T. Au, M. Hyvönen, H. D. Hickman, G. L. Smith. Poxviruses and paramyxoviruses use a conserved mechanism of STAT1 antagonism to inhibit interferon signaling. Cell Host Microbe, 30:357-372.e11, 2022. https://doi.org/10.1016/j.chom.2022.01.014
M. Synakewicz, R. S. Eapen, A. Perez-Riba, D. Bauer, A. Weißl, G. Fischer, M. Hyvönen, M. Rief, L. S. Itzhaki, J. Stigler. Unraveling the mechanics of a repeat-protein nanospring: from folding of Individual repeats to fluctuations of the superhelix. ACS Nano, 6:3895-3905, 2022. https://doi.org/10.1021/acsnano.1c09162
L. H. Lindenburg, T. Pantelejevs, F. Gielen, P. Zuazua-Villar, M. Butz, E. Rees, C. F. Kaminski, J. A. Downs, M. Hyvönen, F. Hollfelder. Improved RAD51 binders through motif shuffling based on the modularity of BRC repeats. Proceedings of the National Academy of Sciences of the USA, 118:e2017708118, 2021 https://doi.org/10.1073/pnas.2017708118
M. Ratcliff, R. X. Zhou, L. Jermutus, M. Hyvönen. The role of pro-domains in human growth factors and cytokines. Biochemical Society Transactions, 49:1963–1973, 2021. https://doi.org/10.1042/BST20200663
N. Kostopoulou, S. Bellou, E. Bagli, M. Markou, E. Kostaras, M. Hyvönen, Y. Kalaidzidis, A. Papadopoulos, V. Chalmantzi, A. Kyrkou, E. Panopoulou,T. Fotsis, C. Murphy. Embryonic stem cells are devoid of macropinocytosis, a trafficking pathway for activin A in differentiated cells. Journal of Cell Science, 134:jcs246892, 2021. https://doi.org/10.1242/jcs.246892
A. Ramachandran, M. Mehić, L. Wasim, D. Malinova, I. Gori, B. K. Blaszczyk, D. M. Carvalho, E. M. Shore, C. Jones, M. Hyvönen, P. Tolar, C. S. Hill. Pathogenic ACVR1R206H activation by Activin A-induced receptor clustering and autophosphorylation. EMBO Journal, e106317, 2021 https://doi.org/10.15252/embj.2020106317
E. L. Atkinson, J. Iegre, P. D. Brear, E. A. Zhabina, M. Hyvönen, D. R. Spring. Downfalls of Chemical Probes Acting at the Kinase ATP-Site: CK2 as a Case Study. Molecules. 26:1977, 2021. https://doi.org/10.3390/molecules26071977
D. E. Scott, N. J. Francis-Newton, M. E. Marsh, A. G. Coyne, G. Fischer, T. Moschetti, A. R. Bayly, T. D. Sharpe, K. T. Haas, L. Barber, C. R. Valenzano, R. Srinivasan, D. J. Huggins, M. Lee, A. Emery, B. Hardwick, M. Ehebauer, C. Dagostin, A. Esposito, L. Pellegrini, T. Perrior, G. McKenzie, T. L. Blundell, M. Hyvönen, J. Skidmore, A. R. Venkitaraman, C. Abell. A small-molecule inhibitor of the BRCA2-RAD51 interaction modulates RAD51 assembly and potentiates DNA damage-induced cell death. Cell Chemical Biology, 28: 1–13, 2020. https://doi.org/10.1016/j.chembiol.2021.02.006 PMCID: PMC821902
A. Papadopoulos, V. Chalmantzi, O. Mikhaylichenko, M. Hyvönen, D. Stellas, A. Kanhere, J. Heath, D. L. Cunningham, T. Fotsis, C. Murphy. Combined transcriptomic and phosphoproteomic analysis of BMP4 signaling in human embryonic stem cells. Stem Cell Research 50:102133, 2021. https://doi.org/10.1016/j.scr.2020.102133
P. D. Brear, D. Ball, K. Stott, S. D’Arcy and M. Hyvönen. Proposed allosteric inhibitors bind to the ATP site of CK2α. Journal of Medicinal Chemistry: 63:12786–12798, 2020. https://doi.org/10.1021/acs.jmedchem.0c01173
S. L. Kidd, E. Fowler, T. Reinhardt,T. Compton, N. Mateu, H. Newman, D. Bellini, R. Talon, J. McLoughlin, T. Krojer, A. Aimon, A. Bradley, M. Fairhead, P. Brear, L. Díaz-Sáez, K. McAuley, H. Sore, A. Madin, D. H. O’Donovan, K. Huber, M. Hyvönen, F. von Delft, C. G. Dowson and D. R. Spring. Demonstration of the utility of DOS-derived fragment libraries for rapid hit derivatisation in a multidirectional fashion. Chemical Science, 11: 10792-10801, 2020. https://doi.org/10.1039/D0SC01232G
T. Sonoyama, L. K. J. Stadler, M. Zhu, J. M. Keogh, E. Henning, F. Hisama, P. Kirwan, M. Jura, B. K. Blaszczyk, D. C. DeWitt, B. Brouwers, M. Hyvönen, I. Barroso, F. T. Merkle, S. M. Appleyard, G. A. Wayman, I. S. Farooqi. Human BDNF/TrkB Variants Impair Hippocampal Synaptogenesis and Associate With Neurobehavioural Abnormalities. Scientific Reports,10:9028, 2020. https://doi.org/10.1038/s41598-020-65531-x
A. V. Strizhak, O. Babii, S. Afonin, I Bakanovich, T. Pantelejevs, W. Xu, E. Fowler, R. Eapen, K. Sharma, M. O. Platonov, V. V. Hurmach, L. Itzhaki, M Hyvönen, A. S. Ulrich, D. R. Spring, I. V. Komarov. Diarylethene moiety as an enthalpy-entropy switch: photoisomerizable stapled peptides for modulating p53/MDM2 interaction. Organic and Biomolecular Chemistry, 18: 5359-536, 2020. https://doi.org/10.1039/d0ob00831a.
F. Negrini, K. O’Grady, M. Hyvönen, K. M. Folta, E. Baraldi. Genomic structure and transcript analysis of the Rapid Alkalinization Factor (RALF) gene family during host-pathogen crosstalk in Fragaria vesca and Fragaria x ananassa strawberry, PLoS ONE, 15: e0226448, 2020 https://doi.org/10.1371/journal.pone.0226448
E-R. Xu, A. Lafaita, A. Bateman, M. Hyvönen. Thrombospondin module 1 domain (TSP1) of the matricellular protein CCN3 shows an atypical disulfide pattern and incomplete CWR layers. Acta Crystallography D, D76:124-134, 2020. https://doi.org/10.1107/s2059798319016747
P. Sharma, R. Mahen, M. Rossmann, J. E. Stokes, B. Hardwick, D. J. Huggins, A. Emery, D. L. Kunciw, M. Hyvönen, D. R. Spring, G. J. McKenzie, A. R. Venkitaraman. A cryptic hydrophobic pocket in the polo-box domain of the polo-like kinase PLK1 regulates substrate recognition and mitotic chromosome segregation, Scientific Reports, 9:15930, 2019. https://doi.org/10.1038/s41598-019-50702-2 PMCID: PMC6828814
K. Sharma, A. V. Strizhak, E. Fowler, X. Wang, W. Xu, C. Hatt Jensen, Y. Wu, H. F. Sore, Y. H. Lau, M. Hyvönen, L. S. Itzhaki, D. R. Spring. Water-soluble, stable and azide-reactive strained dialkynes for biocompatible double strain-promoted click chemistry. Organic and Biomolecular Chemistry, 2019, 17:8014-8018. https://doi.org/10.1039/c9ob01745c
M. Urbischek, H. Rannikmae, T. Foets, K. Ravn, M. Hyvönen and M. de la Roche. Organoid culture media formulated with growth factors of defined cellular activity. Scientific Reports 6193, 2019. https://doi.org/10.1038/s41598-019-42604-0 PMCID: PMC6470207
J. Iegre, P. Brear, D. J. Baker, Y. S. Tan, E. L. Atkinson, H. F. Sore, D. H. O’ Donovan, C. S. Verma, M. Hyvönen and D. R. Spring. Efficient development of stable and highly functionalised peptides targeting the CK2α/CK2β protein–protein interaction. Chemical Science 10:5056-5063, 2019. https://doi.org/10.1039/C9SC00798A. PMCID:PMC6530537
B. van Loo , C. D. Bayer, G. Fischer, S. Jonas, E. Valkov, M. F. Mohamed, A. Vorobieva, C. Dutruel, M. Hyvönen, and F. Hollfelder. Balancing Specificity and Promiscuity in Enzyme Evolution: Multidimensional Activity Transitions in the Alkaline Phosphatase Superfamily. Journal of American Chemical Society 141:370-387, 2019. https://doi.org/10.1021/jacs.8b10290
C. M. Miton, S. Jonas, G. Fischer, F. Duarte, M. F. Mohamed, B. van Loo, B. Kintses, S. C. L. Kamerlin, N. Tokuriki, M. Hyvönen, and F. Hollfelder. Evolutionary repurposing of a sulfatase: A new Michaelis complex leads to efficient transition state charge offset. Proceedings of the National Academy of Sciences of the USA, 115:E7293-E7302, 2018. https://doi.org//10.1073/pnas.1607817115
P. Brear, A. North, J. Iegre, K. Hadje Georgiou, A. Lubin, L. Carro, W. Green, H. F. Sore, M. Hyvönen, D, R.Spring. Novel non-ATP competitive small molecules targeting the CK2 α/β interface. Bioorganic & Medicinal Chemistry, 2018, 26:3016-3020. https://doi.org/10.1016/j.bmc.2018.05.011
B. van Loo, M. Schober, E. Valkov, M. Heberlein, E. Bornberg-Bauer, K. Faber, M. Hyvönen, F. Hollfelder. Structural and Mechanistic Analysis of the Choline Sulfatase from Sinorhizobium melliloti: A Class I Sulfatase Specific for an Alkyl Sulfate Ester. Journal of Molecular Biology 430: 1004-1023, 2018. https://doi.org/10.1016/j.jmb.2018.02.010
S. J. Walsh, S. Omarjee, W. R. J. D. Galloway, T. T.-L. Kwan, H. F. Sore, J. S. Parker, M. Hyvönen, J. S. Carroll and D. R. Spring. A general approach for the site-selective modification of native proteins, enabling the generation of stable and functional antibody–drug conjugates. Chemical Science 10: 694-700, 2019. https://doi.org/10.1039/C8SC04645J
J. Iegre, P. Brear, C. De Fusco, M. Yoshida, S. L. Mitchell, M. Rossmann, L. Carro Santos, H. F. Sore, M. Hyvӧnen and D. R. Spring. Second-generation CK2α inhibitors targeting the αD pocket. Chemical Science, 2018, 9:3041-3049. https://doi.org/10.1039/C7SC05122K. PMCID:PMC5916021
T. Cotton, G. Fischer, X. Wang, J. McCoy, M. Czepnik, T. B. Thompson, M. Hyvӧnen. Structure of the human pro-myostatin precursor and determinants of growth factor latency. EMBO Journal 37:367-383, 2018. https://doi.org/10.15252/embj.201797883. PMCID:PMC5793801
R. G. Walker, J. C. McCoy, M. Czepnik, M. J. Mills, A. Hagg, K. L. Walton, T. Cotton, M. Hyvönen, R. T. Lee, P. Gregorevic, C. A. Harrison, T. B. Thompson. Molecular characterization of latent GDF8 reveals mechanisms of activation. Proceedings of the National Academy of Sciences of the USA, 115:E866-E875, 2018. https://doi.org/10.1073/pnas.1714622115
D. J. Cole, M. Janecek, J. E. Stokes, M. Rossmann, J. C. Faver, G. J. McKenzie, A. R. Venkitaraman, M. Hyvönen, D. R. Spring, D. J. Huggins, and W. L. Jorgensen Computationally-Guided Optimization of Small-Molecule Inhibitors of the Aurora A Kinase – TPX2 Protein-Protein Interaction. Chemical Communications 53, 9372-9375, 2018. https://doi.org/10.1039/C7CC05379G
E.-R. Xu, E. E. Blythe, G. Fischer, M. Hyvönen. Structural analyses of von Willebrand factor C domains of collagen 2A and CCN3 reveal an alternative mode of binding to bone morphogenetic protein-2. Journal of Biological Chemistry 292:12516–12527, 2017. https://doi.org/10.1074/jbc.M117.788992
C. De Fusco, P. Brear, J. Iegre, K. H. Georgiou, H. F. Sore, M. Hyvönen, D. R. Spring. A fragment-based approach leading to the discovery of a novel binding site and the selective CK2 inhibitor CAM4066. Bioorganic and Medicinal Chemistry 25:3471-3482, 2017. https://doi.org/10.1016/j.bmc.2017.04.037 PMCID:PMC5587527
M. Rossmann, S. Greive, T. Moschetti, M. Dinan, M. Hyvönen. Development of a Multipurpose Scaffold for the Display of Peptide Loops. Proteins: Engineering, Design and Selection 24:1-12, 2017. https://doi.org/10.1093/protein/gzx017. PMCID:PMC5897841
M. Rangel Pereira, T. Carvalho Maester, G. F. Mercaldi, E. G. de Macedo Lemos, M. Hyvönen, A. Balan. From a metagenomic source to a high-resolution structure of a novel alkaline esterase. Applied Microbiology and Biotechnology, 101:4935-4949, 2017. https://doi.org/10.1007/s00253-017-8226-4
W. Xu, Y. H. Lau, G. Fischer, Y. S. Tan, A. Chattopadhyay, M. de la Roche, M. Hyvönen, C. S. Verma, D. R. Spring, and L. S. Itzhaki. Macrocyclized extended peptides: Inhibiting the substrate-recognition domain of tankyrase. Journal of the American Chemical Society 139:2245-2256, 2017. https://doi.org/10.1021/jacs.6b10234
F. Gielen, M. Butz, E. J. Rees, M. Erdelyi, T. Moschetti, M. Hyvönen, J. B. Edel, C. F. Kaminski, F. Hollfelder. Quantitative affinity determination by fluorescence anisotropy measurements of individual nanoliter droplets. Analytical Chemistry 89:1092-1101, 2016. https://doi.org/10.1021/acs.analchem.6b02528
T. Moschetti, T. Sharpe, G. Fischer, M. E. Marsh, H. Ng, M. Morgan, D. Scott, T. L. Blundell, A. R.Venkitaraman, J. Skidmore, C. Abell, M. Hyvönen. Engineering archeal surrogate systems for the development of protein-protein interaction inhibitors against human RAD51. Journal of Molecular Biology, 428:4589-4607, 2016. https://doi.org/10.1016/j.jmb.2016.10.009 PMCID:PMC5117717
P. Brear, C. De Fusco, K. Hadje Georgiou, N. J. Francis-Newton, C. J. Stubbs, H. F. Sore, A. R. Venkitaraman, C. Abell, D. R. Spring, M. Hyvönen. Specific inhibition of CK2α from an anchor outside the active site. Chemical Science 7: 6839-6845, 2016. https://doi.org/10.1039/C6SC02335E PMCID:PMC5355960
X. Wang, G. Fischer and M. Hyvönen. Structure and activation of pro-activin A. Nature Communications, 7:12052, 2016. https://doi.org/10.1038/ncomms12052 PMCID: PMC4932183
M. Janeček, M. Rossmann , P. Sharma, A. Emery, D.J. Huggins, S.R. Stockwell, J.E. Stokes, Y.S. Tan, E.G. Almeida, B. Hardwick, A.J. Narvaez, M. Hyvönen, D.R. Spring, G.J. McKenzie, A.R. Venkitaraman. Allosteric modulation of AURKA kinase activity by a small-molecule inhibitor of its protein-protein interaction with TPX2. Scientific Reports. 6:28528, 2016. https://doi.org/10.1038/srep28528 PMCID:PMC4919790
M. Kasbekar, G. Fischer, B.T. Mott, A. Yasgar, M. Hyvönen, H.I. Boshoff, C. Abell, C.E. Barry 3rd, C.J. Thomas. Selective small molecule inhibitor of the Mycobacterium tuberculosis fumarate hydratase reveals an allosteric regulatory site. Proceedings of the National Academy of Sciences of the USA 113:7503-7508, 2016. https://doi.org/10.1073/pnas.1600630113
M. Marsh, M.T. Ehebauer, D. Scott, A.R. Venkitaraman, C. Abell, T.L. Blundell, M. Hyvönen. ATP-half site in RAD51 and RadA bind nucleotides. FEBS OpenBio 6:372–385, 2016. https://doi.org/10.1002/2211-5463.12052. PMCID:PMC4856416
D. Scott, M. Marsh, T.L. Blundell, C. Abell and M. Hyvönen. Structure Activity Relationship of the Peptide Binding Motif Mediating the RAD51:BRCA2 Protein-Protein Interaction. FEBS Letters, 590: 1094–1102, 2016. https://doi.org/10.1002/1873-3468.12139. PMCID:PMC4855620
M. Kišonaitė, X. Wang and M. Hyvönen. Structure of Gremlin-1 and analysis of its interaction with BMP-2. Biochemical Journal, 473:1593-1604, 2016. https://doi.org/10.1042/BCJ20160254
P.-Y. Colin, B. Kintses, F. Gielen, C. M. Miton, G. Fischer, M. F. Mohamed, M. Hyvönen, D. P. Morgavi, D. B. Janssen, F. Hollfelder. Ultrahigh-throughput discovery of promiscuous enzymes by picodroplet functional metagenomics. Nature Communications, 6:10008, 2015. https://doi.org/10.1038/ncomms10008
G. Fischer, M. Rossmann, M. Hyvönen. Alternative Modulation of Protein-Protein Interactions by Small Molecules. Current Opinion in Biotechnology, 35:78-85, 2015 https://doi.org/10.1016/j.copbio.2015.04.006.
D.E. Scott, A. G. Coyne, T. L. Blundell, A. Venkitaraman, C. Abell, M. Hyvönen, Small molecule inhibitors targeting protein-protein interaction in the RAD51 family of recombinases, ChemMedChem, 10: 296–303, 2014 https://doi.org/10.1002/cmdc.201402428. PMCID:PMC4506530
Y. H. Lau, P. de Andrade, S.-T. Quah, M. Rossmann, L. Laraia, N. Sköld, T. J. Sum, P. J. E. Rowling, T. L. Joseph, C. Verma, M.Hyvönen, L. S. Itzhaki, A. R. Venkitaraman, C. J. Brown, D. P. Lane, D. R. Spring. Functionalised staple linkages for modulating the cellular activity of stapled peptides. Chemical Science 5:18040-1809, 2014. https://doi.org/0.1039/C4SC00045E.
D. E. Scott, M. T. Ehebauer, T. Pukala, M. Marsh, T. L. Blundell, A. R. Venkitaraman, C. Abell, M. Hyvönen. Using a Fragment‐Based Approach To Target Protein–Protein Interactions. ChemBioChem 14:332-42, 2014. https://doi.org/10.1002/cbic.201200521. PMCID:PMC359497
Sharma, F. Meyer, M.Hyvönen, S. M. Best, R. E. Cameron, N. Rushton. Osteoinduction by combining bone morphogenetic protein (BMP)-2 with a bioactive novel nanocomposite. Bone and Joint Research, 1:145-51, 2012. https://doi.org/10.1302/2046-3758.17.2000082
E. Valkov, T. Sharpe, M. Marsh, S. Greive and M. Hyvönen. Targeting protein-protein interactions and fragment-based drug discovery. in Topics in Current Chemistry: “Fragment-based drug discovery and X-ray crystallography” ed. T. Davies and M. Hyvönen, pp 145–179, 2011. https://doi.org/10.1007/128_2011_265
P Sledź, C. J. Stubbs, S. Lang, Y. Q. Yang, G. J. McKenzie, A. R. Venkitaraman, M. Hyvönen, C Abell. From crystal packing to molecular recognition: prediction and discovery of a binding site on the surface of polo-like kinase 1. Angewante Chemie International Edition, 50:4003-6, 2011, https://doi.org/10.1002/anie.201008019 PMCID: PMC3555362
B. van Loo, S. Jonas, A. C. Babtie, A. Benjdia, O. Berteau, M. Hyvönen, and F. Hollfelder. An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily. Proceedings of the National Academy of Sciences of the USA, 107:2740-5, 2010. https://doi.org/10.1073/pnas.0903951107
Hagemann, X. Xu, O. Nentwich, M. Hyvönen, K. Dingwell and J. C. Smith. Rab5-mediated endocytosis of activin is not required for gene activation or long-range signalling in Xenopus. Development, 136:2803-13, 2009. https://doi.org/10.1242/dev.034124
H. Ludlow, D. J. Phillips, M. Myers, R. I. McLachlan, D. M. de Kretser, C. A. Allan, R. A. Anderson, N. P. Groome, M. Hyvönen, W. C. Duncan and S. Muttukrishna. A new ‘total’ activin B ELISA: development and validation for human samples. Clinical Endocrinology. 71:867-73, 2009. https://doi.org/10.1111/j.1365-2265.2009.03567.x
S. Jonas, B. van Loo, M. Hyvönen, F. Hollfelder. A new member of the alkalinea phosphatase superfamily with a formylglycine nucleophile: structural and kinetic characterisation of a phosphonate monoester hydrolase/phosphodiesterase from Rhizobium leguminosarum. Journal of Molecular Biology, 384:120-36, 2008. https://doi.org/10.1016/j.jmb.2008.08.072
H. Ludlow, S. Muttukrishna, M. Hyvönen , N.P. Groome. Development of a new antibody to the human inhibin/activin B subunit and its application to improved inhibin B ELISAs. Journal of Immunological Methods, 329:102-111, 2008. https://doi.org/10.1016/j.jim.2007.09.013
A.E. Harrington, S.A. Morris-Triggs, B.T. Ruotolo, C.V. Robinson, S. Ohnuma and M. Hyvönen.. Structural basis for the inhibition of activin signalling by follistatin. EMBO Journal, 25:1035-1045, 2006. https://dx.doi.org/10.1038/sj.emboj.7601000
M. Hyvönen. CHRD, a novel domain in the bone morphogenetic protein inhibitor chordin, is also found in microbial proteins. Trends in Biochemical Sciences, 28: 470–473, 2003. https://doi.org/10.1016/s0968-0004(03)00171-3
P. D. Ellis, J. C. Metcalf, M. Hyvönen, and P. R. Kemp. Adhesion of endothelial cells to nov is mediated by integrins v3 and 51. Journal of Vascular Research, 40:234–243, 2003. https://doi.org/10.1159/000071887
C. A. Innis and M. Hyvönen. Crystal structures of the heparan sulfate-binding domain of follistatin. Insights into ligand binding. Journal of Biological Chemistry, 278:39969–39977, 2003. https://doi.org/10.1074/jbc.m211284200
M. Hyvönen, J. Begun, and T. Blundell. Protein-protein interactions in eukaryotic signal transduction. In C. Kleanthous, editor, Protein-Protein Recognition, Frontiers in Molecular Biology, pages 189–227. Oxford University Press, 2000.
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