Publications written with support of CIISB

Recent publications

E. Abad, et al.: Activation of glycogenolysis and glycolysis in breast cancer stem cell models, Biochimica Et Biophysica Acta-Molecular Basis of Disease, 1866 (2020) 10.1016/j.bbadis.2020.165886

C. Paris, et al.: CO2 Hydrogenation to Methanol with Ga- and Zn-Doped Mesoporous Cu/SiO2 Catalysts Prepared by the Aerosol-Assisted Sol-Gel Process, Chemsuschem,  10.1002/cssc.202001951

S. Noonepalle, et al.: Rational Design of Suprastat: A Novel Selective Histone Deacetylase 6 Inhibitor with the Ability to Potentiate Immunotherapy in Melanoma Models, J. Med. Chem., 63 (2020) 10246-10262, 10.1021/acs.jmedchem.0c00567


CIISB, Instruct-CZ Centre of Instruct-ERIC EU consortium, funded by MEYS CR infrastructure project LM2018127, is gratefully acknowledged for the financial support of the measurements at the CF [name of the unit/CF].

Or in a short version: We acknowledge [name of the unit/CF] of CIISB, Instruct-CZ Centre, supported by MEYS CR (LM2018127).

All publications written with support of CIISB


E. Abad, et al.: Activation of glycogenolysis and glycolysis in breast cancer stem cell models, Biochimica Et Biophysica Acta-Molecular Basis of Disease, 1866 (2020) 10.1016/j.bbadis.2020.165886 

M. Adamus, et al.: Molecular Insights into the Architecture of the Human SMC5/6 Complex, J. Mol. Biol., 432 (2020) 3820-3837, 10.1016/j.jmb.2020.04.024 

P.C. Andrikopoulos, et al.: Femtosecond-to-nanosecond dynamics of flavin mononucleotide monitored by stimulated Raman spectroscopy and simulations, Physical Chemistry Chemical Physics, 22 (2020) 6538-6552, 10.1039/c9cp04918e 

B.V. Alviri, et al.: Conformational flexibility in amidophosphoesters: a CSD analysis completed with two new crystal structures of (C6H5O)(2)P(O)X X = NHC7H13 and N(CH2C6H5)(2), Acta Crystallographica Section C-Structural Chemistry, 76 (2020) 104-+, 10.1107/s2053229619016619

P. Bardy, et al.: Structure and mechanism of DNA delivery of a gene transfer agent, Nature Communications, 11 (2020) 13, 10.1038/s41467-020-16669-9 

O. Bernatik, et al.: Phosphorylation of multiple proteins involved in ciliogenesis by Tau Tubulin kinase 2, Mol. Biol. Cell, 31 (2020) 1032-1046, 10.1091/mbc.E19-06-0334

J. Bezdekova, et al.: Molecularly imprinted polymers and capillary electrophoresis for sensing phytoestrogens in milk, Journal of Dairy Science, 103 (2020) 4941-4950, 10.3168/jds.2019-17367 

P. Brazda, et al.: Yeast Spt6 Reads Multiple Phosphorylation Patterns of RNA Polymerase II C-Terminal Domain In Vitro, J. Mol. Biol., 432 (2020) 4092-4107, 10.1016/j.jmb.2020.05.007 

P. Cernochova, et al.: Cell type specific adhesion to surfaces functionalised by amine plasma polymers, Sci Rep, 10 (2020) 14, 10.1038/s41598-020-65889-y 

I. Doroshenko, et al.: Heterometallic 3d-4f {Co2Gd4} phosphonates: new members of the potential magnetic cooler family, New Journal of Chemistry, 44 (2020) 513-521, 10.1039/c9nj05071j 

H. Dvorakova, et al.: Isoforms of Cathepsin B1 in Neurotropic Schistosomula of Trichobilharzia regenti Differ in Substrate Preferences and a Highly Expressed Catalytically Inactive Paralog Binds Cystatin, Frontiers in Cellular and Infection Microbiology, 10 (2020) 10.3389/fcimb.2020.00066 

M. Dvorakova, et al.: Transgelin Silencing Induces Different Processes in Different Breast Cancer Cell Lines, Proteomics, 20 (2020) 8, 10.1002/pmic.201900383 

Z. Farka, et al.: Surface design of photon-upconversion nanoparticles for high-contrast immunocytochemistry, Nanoscale, 12 (2020) 8303-8313, 10.1039/c9nr10568a 

A. Ferofontov, et al.: Conserved cysteine dioxidation enhances membrane interaction of human Cl(-)intracellular channel 5, Faseb J.,  16, 10.1096/fj.202000399R 

J. Fiala, et al.: Influence of cross-linker polarity on selectivity towards lysine side chains, Journal of Proteomics, 218 (2020) 7, 10.1016/j.jprot.2020.103716 

J. Fila, et al.: The Beta Subunit of Nascent Polypeptide Associated Complex Plays A Role in Flowers and Siliques Development of Arabidopsis thaliana, International Journal of Molecular Sciences, 21 (2020) 30, 10.3390/ijms21062065 

F. Filandr, et al.: Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis, Biomolecules, 10 (2020) 18, 10.3390/biom10020242 

F. Filandr, et al.: The H2O2-dependent activity of a fungal lytic polysaccharide monooxygenase investigated with a turbidimetric assay, Biotechnol. Biofuels, 13 (2020) 13, 10.1186/s13068-020-01673-4 

E. Fujdiarova, et al.: Heptabladed beta-propeller lectins PLL2 and PHL fromPhotorhabdusspp. recognizeO-methylated sugars and influence the host immune system, Febs Journal,  23, 10.1111/febs.15457 

V. Henrichs, et al.: Mitochondria-adaptor TRAK1 promotes kinesin-1 driven transport in crowded environments, Nature Communications, 11 (2020) 13, 10.1038/s41467-020-16972-5 

S. Jelinkova, et al.: DMD Pluripotent Stem Cell Derived Cardiac Cells Recapitulatein vitroHuman Cardiac Pathophysiology, Front. Bioeng. Biotechnol., 8 (2020) 19, 10.3389/fbioe.2020.00535 

K. Jurikova, et al.: Role of folding kinetics of secondary structures in telomeric G-overhangs in the regulation of telomere maintenance inSaccharomyces cerevisiae, Journal of Biological Chemistry, 295 (2020) 8958-8971, 10.1074/jbc.RA120.012914 

D. Kalabova, et al.: 14-3-3 protein binding blocks the dimerization interface of caspase-2, Febs Journal,  17, 10.1111/febs.15215 

G. Kalnins, et al.: Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles, Nature Communications, 11 (2020) 13, 10.1038/s41467-019-14205-y 

R. Kouril, et al.: Unique organization of photosystem II supercomplexes and megacomplexes in Norway spruce, Plant J.,  11, 10.1111/tpj.14918 

P. Krafcikova, et al.: Structural analysis of the SARS-CoV-2 methyltransferase complex involved in RNA cap creation bound to sinefungin, Nature Communications, 11 (2020) 7, 10.1038/s41467-020-17495-9 

V. Kuban, et al.: Structural Basis of Ca2+-Dependent Self-Processing Activity of Repeat-in-Toxin Proteins, mBio, 11 (2020) 18, 10.1128/mBio.00226-20 

K. Kucakova, et al.: Molecular structure study of a heptakis(2,3,6-tri-O-methyl)-beta-cyclodextrin complex of cholesterol, Steroids, 155 (2020) 9, 10.1016/j.steroids.2019.108555

J. Kudr, et al.: Inkjet-printed electrochemically reduced graphene oxide microelectrode as a platform for HT-2 mycotoxin immunoenzymatic biosensing, Biosensors & Bioelectronics, 156 (2020) 8, 10.1016/j.bios.2020.112109 

S.G. Kulkarni, et al.: A Photochemical/Thermal Switch Based on 4,4 '-Bis(benzimidazolio)stilbene: Synthesis and Supramolecular Properties, Chemphyschem,  10.1002/cphc.202000472 

V. Kundrat, et al.: Preparation of thorium dioxide nanofibers by electrospinning, J. Nucl. Mater., 534 (2020) 8, 10.1016/j.jnucmat.2020.152153 

V. Kundrat, et al.: Preparation of ultrafine fibrous uranium dioxide by electrospinning, J. Nucl. Mater., 528 (2020) 10, 10.1016/j.jnucmat.2019.151877 

S. Laidou, et al.: Nuclear inclusions of pathogenic ataxin-1 induce oxidative stress and perturb the protein synthesis machinery, Redox Biology, 32 (2020) 10.1016/j.redox.2020.101458 

E. Lattova, et al.: Comprehensive N-glycosylation mapping of envelope glycoprotein from tick-borne encephalitis virus grown in human and tick cells, Sci Rep, 10 (2020) 10, 10.1038/s41598-020-70082-2 

E. Lattova, et al.: N-Glycan profiling of lung adenocarcinoma in patients at different stages of disease, Mod. Pathol.,  11, 10.1038/s41379-019-0441-3

E. Makhneva, et al.: Functional Plasma Polymerized Surfaces for Biosensing, Acs Applied Materials & Interfaces, 12 (2020) 17100-17112, 10.1021/acsami.0c01443 

S. Malali, et al.: Zwitterionic Ru(III) Complexes: Stability of Metal-Ligand Bond and Host-Guest Binding with Cucurbit 7 uril, Inorganic Chemistry, 59 (2020) 10185-10196, 10.1021/acs.inorgchem.0c01328 

J. Matousek, et al.: Elimination of Viroids from Tobacco Pollen Involves a Decrease in Propagation Rate and an Increase of the Degradation Processes, International Journal of Molecular Sciences, 21 (2020) 26, 10.3390/ijms21083029 

L. Motlova, et al.: Continuous Assembly of beta-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins, J. Mol. Biol., 432 (2020) 5696-5710, 10.1016/j.jmb.2020.08.020 

L. Munster, et al.: Mechanism of sulfonation-induced chain scission of selectively oxidized polysaccharides, Carbohydrate Polymers, 229 (2020) 10, 10.1016/j.carbpol.2019.115503 

L. Nejdl, et al.: UV-Induced Nanoparticles-Formation, Properties and Their Potential Role in Origin of Life, Nanomaterials, 10 (2020) 10.3390/nano10081529 

S. Noonepalle, et al.: Rational Design of Suprastat: A Novel Selective Histone Deacetylase 6 Inhibitor with the Ability to Potentiate Immunotherapy in Melanoma Models, J. Med. Chem., 63 (2020) 10246-10262, 10.1021/acs.jmedchem.0c00567 

D. Novakova, et al.: Pseudomonas leptonychotis sp. nov., isolated from Weddell seals in Antarctica, Int. J. Syst. Evol. Microbiol., 70 (2020) 302-308, 10.1099/ijsem.0.003753 

A. Osickova, et al.: Acyltransferase-mediated selection of the length of the fatty acyl chain and of the acylation site governs activation of bacterial RTX toxins, Journal of Biological Chemistry, 295 (2020) 9268-9280, 10.1074/jbc.RA120.014122 

J. Otevrel, et al.: One-pot method for the synthesis of 1-aryl-2-aminoalkanol derivatives from the corresponding amides or nitriles, RSC Adv., 10 (2020) 25029-25045, 10.1039/d0ra04359a 

V. Palusova, et al.: Dual Targeting of BRAF and mTOR Signaling in Melanoma Cells with Pyridinyl Imidazole Compounds, Cancers, 12 (2020) 24, 10.3390/cancers12061516 

C. Paris, et al.: CO2 Hydrogenation to Methanol with Ga- and Zn-Doped Mesoporous Cu/SiO2 Catalysts Prepared by the Aerosol-Assisted Sol-Gel Process, Chemsuschem,  10.1002/cssc.202001951 

P. Pejskova, et al.: KIF14 controls ciliogenesis via regulation of Aurora A and is important for Hedgehog signaling, Journal of Cell Biology, 219 (2020) 10.1083/jcb.201904107 

V. Pekarik, et al.: Direct fluorogenic detection of palladium and platinum organometallic complexes with proteins and nucleic acids in polyacrylamide gels, Sci Rep, 10 (2020) 10, 10.1038/s41598-020-69336-w 

M. Petrencakova, et al.: Photoinduced damage of AsLOV2 domain is accompanied by increased singlet oxygen production due to flavin dissociation, Sci Rep, 10 (2020) 15, 10.1038/s41598-020-60861-2 

P. Roudnicky, et al.: Laser capture microdissection in combination with mass spectrometry: Approach to characterization of tissue-specific proteomes ofEudiplozoon nipponicum(Monogenea, Polyopisthocotylea), Plos One, 15 (2020) 15, 10.1371/journal.pone.0231681 

L. Rucka, et al.: Plant Nitrilase Homologues in Fungi: Phylogenetic and Functional Analysis with Focus on Nitrilases in Trametes versicolor and Agaricus bisporus, Molecules, 25 (2020) 10.3390/molecules25173861 

J. Salat, et al.: Tick-Borne Encephalitis Virus Vaccines Contain Non-Structural Protein 1 Antigen and May Elicit NS1-Specific Antibody Responses in Vaccinated Individuals, Vaccines, 8 (2020) 13, 10.3390/vaccines8010081 

O. Sedo, et al.: MALDI-TOF Mass Spectrometric Profiling of Spider Venoms, in: A. Priel (Ed.) Snake and Spider Toxins: Methods and Protocols, Humana Press Inc, Totowa, 2020, pp. 173-181, 10.1007/978-1-4939-9845-6_9 

S.D. Shen, et al.: Structural and in Vivo Characterization of Tubastatin A, a Widely Used Histone Deacetylase 6 Inhibitor, Acs Medicinal Chemistry Letters, 11 (2020) 706-712, 10.1021/acsmedchemlett.9b00560 

I. Sisolakova, et al.: Electrochemical determination of insulin at CuNPs/chitosan-MWCNTs and CoNPs/chitosan-MWCNTs modified screen printed carbon electrodes, Journal of Electroanalytical Chemistry, 860 (2020) 9, 10.1016/j.jelechem.2020.113881 

P. Skolakova, et al.: Composite 5-methylations of cytosines modulate i-motif stability in a sequence-specific manner: Implications for DNA nanotechnology and epigenetic regulation of plant telomeric DNA, Biochimica Et Biophysica Acta-General Subjects, 1864 (2020) 9, 10.1016/j.bbagen.2020.129651 

O. Skorepa, et al.: Natural Killer Cell Activation Receptor NKp30 Oligomerization Depends on ItsN-Glycosylation, Cancers, 12 (2020) 24, 10.3390/cancers12071998 

K. Smolkova, et al.: SIRT3 and GCN5L regulation of NADP plus - and NADPH-driven reactions of mitochondrial isocitrate dehydrogenase IDH2, Sci Rep, 10 (2020) 12, 10.1038/s41598-020-65351-z 

J. Sokolov, et al.: Functionalized Chiral Bambusurils: Synthesis and Host-Guest Interactions with Chiral Carboxylates, ChemPlusChem, 85 (2020) 1307-1314, 10.1002/cplu.202000261 

J. Sopousek, et al.: Blocking the Nanopores in a Layer of Nonconductive Nanoparticles: Dominant Effects Therein and Challenges for Electrochemical Impedimetric Biosensing, Acs Applied Materials & Interfaces, 12 (2020) 14620-14628, 10.1021/acsami.0c02650 

M. Spit, et al.: RNF43 truncations trapCK1 to drive niche-independent self-renewal in cancer, Embo J.,  15, 10.15252/embj.2019103932

L. Stackova, et al.: Cyanine-Flavonol Hybrids for Near-Infrared Light-Activated Delivery of Carbon Monoxide, Chemistry-a European Journal,  10.1002/chem.202003272 

B. Stefanovie, et al.: DSS1 interacts with and stimulates RAD52 to promote the repair of DSBs, Nucleic Acids Res., 48 (2020) 694-708, 10.1093/nar/gkz1052

L. Steiningerova, et al.: Different Reaction Specificities of F420H2-Dependent Reductases Facilitate Pyrrolobenzodiazepines and Lincomycin To Fit Their Biological Targets, Journal of the American Chemical Society, 142 (2020) 3440-3448, 10.1021/jacs.9b11234

A. Styskalik, et al.: Mildly acidic aluminosilicate catalysts for stable performance in ethanol dehydration, Appl. Catal. B-Environ., 271 (2020) 11, 10.1016/j.apcatb.2020.118926 

Z.S. Stojanovic, et al.: Highly sensitive simultaneous electrochemical determination of reduced and oxidized glutathione in urine samples using antimony trioxide modified carbon paste electrode, Sensors and Actuators B-Chemical, 318 (2020) 10.1016/j.snb.2020.128141

P. Sykorova, et al.: Characterization of novel lectins from Burkholderia pseudomallei and Chromobacterium violaceum with seven-bladed beta-propeller fold, International Journal of Biological Macromolecules, 152 (2020) 1113-1124, 10.1016/j.ijbiomac.2019.10.200 

F. Trcka, et al.: The interaction of the mitochondrial protein importer TOMM34 with HSP70 is regulated by TOMM34 phosphorylation and binding to 14-3-3 adaptors, Journal of Biological Chemistry, 295 (2020) 8928-8944, 10.1074/jbc.RA120.012624 

K. Ustinova, et al.: The disordered N-terminus of HDAC6 is a microtubule-binding domain critical for efficient tubulin deacetylation, Journal of Biological Chemistry, 295 (2020) 2614-2628, 10.1074/jbc.RA119.011243 

V. Vandova, et al.: HSPA1A conformational mutants reveal a conserved structural unit in Hsp70 proteins, Biochimica Et Biophysica Acta-General Subjects, 1864 (2020) 16, 10.1016/j.bbagen.2019.129458 

P. Vojackova, et al.: Stereocontrolled Synthesis of (-)-Bactobolin A, Journal of the American Chemical Society, 142 (2020) 7306-7311, 10.1021/jacs.0c01554 

V. Vrbovska, et al.: Characterization of Staphylococcus intermedius Group Isolates Associated with Animals from Antarctica and Emended Description of Staphylococcus delphini, Microorganisms, 8 (2020) 18, 10.3390/microorganisms8020204 

V. Vykoukal, et al.: Thermal properties of Ag@Ni core-shell nanoparticles, Calphad-Computer Coupling of Phase Diagrams and Thermochemistry, 69 (2020) 10.1016/j.calphad.2020.101741 

D.K. Yadav, et al.: Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition, Nucleic Acids Res., 48 (2020) 2091-2106, 10.1093/nar/gkz1163 

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I. Zhernov, et al.: Intrinsically Disordered Domain of Kinesin-3 Kif14 Enables Unique Functional Diversity, Current Biology, 30 (2020) 3342-+, 10.1016/j.cub.2020.06.039 


E. Abad, et al.: Common Metabolic Pathways Implicated in Resistance to Chemotherapy Point to a Key Mitochondrial Role in Breast Cancer, Mol. Cell. Proteomics, 18 (2019) 231-244, 10.1074/mcp.RA118.001102 

L. Adamkova, et al.: Oligomeric Architecture of Mouse Activating Nkrp1 Receptors on Living Cells, Int. J. Mol. Sci., 20 (2019) 24, 10.3390/ijms20081884 

M. Alblova, et al.: Allosteric Activation of Yeast Enzyme Neutral Trehalase by Calcium and 14-3-3 Protein, Physiol. Res., 68 (2019) 147-160, 10.33549/physiolres.933950 

A.M. Ashrafi, et al.: Application of the Enzymatic Electrochemical Biosensors for Monitoring Non-Competitive Inhibition of Enzyme Activity by Heavy Metals, Sensors, 19 (2019) 14, 10.3390/s19132939 

M. Axmann, et al.: Receptor-Independent Transfer of Low Density Lipoprotein Cargo to Biomembranes, Nano Lett., 19 (2019) 2562-2567, 10.1021/acs.nanolett.9b00319 

C. Barinka, et al.: Structural and computational basis for potent inhibition of glutamate carboxypeptidase II by carbamate-based inhibitors, Bioorg. Med. Chem., 27 (2019) 255-264, 10.1016/j.bmc.2018.11.022 

L. Bertolla, et al.: Deconstruction of microfibrillated cellulose into nanocrystalline cellulose rods and mesogenic phase formation in concentrated low-modulus sodium silicate solutions, Cellulose, 26 (2019) 4325-4344, 10.1007/s10570-019-02364-6 

J. Bokrova, et al.: Fabrication of novel PHB-liposome nanoparticles and study of their toxicity in vitro, J. Nanopart. Res., 21 (2019) 12, 10.1007/s11051-019-4484-7 

F. Bonnardel, et al.: Architecture and Evolution of Blade Assembly in beta-propeller Lectins, Structure, 27 (2019) 764-+, 10.1016/j.str.2019.02.002 

M.K. Bosakova, et al.: Fibroblast growth factor receptor influences primary cilium length through an interaction with intestinal cell kinase, Proc. Natl. Acad. Sci. U. S. A., 116 (2019) 4316-4325, 10.1073/pnas.1800338116 

P. Brazda, et al.: Efficient and robust preparation of tyrosine phosphorylated intrinsically disordered proteins, Biotechniques, 67 (2019) 16-22, 10.2144/btn-2019-0033 

D. Buchta, et al.: Enterovirus particles expel capsid pentamers to enable genome release, Nat. Commun., 10 (2019) 9, 10.1038/s41467-019-09132-x 

G. Caluori, et al.: Simultaneous study of mechanobiology and calcium dynamics on hESC-derived cardiomyocytes clusters, J. Mol. Recognit., 32 (2019) 9, 10.1002/jmr.2760 

G. Caluori, et al.: Non-invasive electromechanical cell-based biosensors for improved investigation of 3D cardiac models, Biosens. Bioelectron., 124 (2019) 129-135, 10.1016/j.bios.2018.10.021 

R. Chaloupkova, et al.: Light-Emitting Dehalogenases: Reconstruction of Multifunctional Biocatalysts, ACS Catal., 9 (2019) 4810-4823, 10.1021/acscatal.9b01031

D.D. Dochain, et al.: Ag- and Cu-Promoted Mesoporous Ta-SiO2 Catalysts Prepared by Non-Hydrolytic Sol-Gel for the Conversion of Ethanol to Butadiene, Catalysts, 9 (2019) 14, 10.3390/catal9110920 

A. Domanska, et al.: A 2.8-Angstrom-Resolution Cryo-Electron Microscopy Structure of Human Parechovirus 3 in Complex with Fab from a Neutralizing Antibody, J. Virol., 93 (2019) 12, 10.1128/jvi.01597-18 

J. Faktor, et al.: Proteomics Identification and Validation of Desmocollin-1 and Catechol-O-Methyltransferase as Proteins Associated with Breast Cancer Cell Migration and Metastasis, Proteomics,  11, 10.1002/pmic.201900073 

L. Faltinek, et al.: Lectin PLL3, a Novel Monomeric Member of the Seven-Bladed beta-Propeller Lectin Family, Molecules, 24 (2019) 20, 10.3390/molecules24244540 

E.M. Fananas, et al.: On the mechanism of calcium-dependent activation of NADPH oxidase 5 (NOX5), Febs Journal,  18, 10.1111/febs.15160 

Z. Fohlerova, et al.: Anodic formation and biomedical properties of hafnium-oxide nanofilms, J. Mat. Chem. B, 7 (2019) 2300-2310, 10.1039/c8tb03180k 

T. Grymova, et al.: SERPING1 exon 3 splicing variants using alternative acceptor splice sites, Mol. Immunol., 107 (2019) 91-96, 10.1016/j.molimm.2019.01.007 

K. Hanakova, et al.: Comparative phosphorylation map of Dishevelled 3 links phospho-signatures to biological outputs, Cell Commun. Signal., 17 (2019) 21, 10.1186/s12964-019-0470-z 

J. Harnos, et al.: Dishevelled-3 conformation dynamics analyzed by FRET-based biosensors reveals a key role of casein kinase 1, Nat. Commun., 10 (2019) 18, 10.1038/s41467-019-09651-7 

L. Hernychova, et al.: The C-type lectin-like receptor Nkrp1b: Structural proteomics reveals features affecting protein conformation and interactions, J. Proteomics, 196 (2019) 162-172, 10.1016/j.jprot.2018.11.007 

D. Hrebik, et al.: Structure and genome ejection mechanism of Staphylococcus aureus phage P68, Sci. Adv., 5 (2019) ARTN eaaw7414, 10.1126/sciadv.aaw7414 

T. Janovic, et al.: Human Telomere Repeat Binding Factor TRF1 Replaces TRF2 Bound to Shelterin Core Hub TIN2 when TPP1 Is Absent, J. Mol. Biol., 431 (2019) 3289-3301, 10.1016/j.jmb.2019.05.038 

L. Jedlickova, et al.: A novel Kunitz protein with proposed dual function from Eudiplozoon nipponicum (Monogenea) impairs haemostasis and action of complement in vitro, Int. J. Parasit., 49 (2019) 337-346, 10.1016/j.ijpara.2018.11.010 

K. Kaiser, et al.: WNT5A is transported via lipoprotein particles in the cerebrospinal fluid to regulate hindbrain morphogenesis, Nat. Commun., 10 (2019) 15, 10.1038/s41467-019-09298-4

M. Kandrnalova, et al.: Hypervalent Iodine Based Reversible Covalent Bond in Rotaxane Synthesis, Angewandte Chemie-International Edition, (2019) 5, 10.1002/anie.201908953

D. Kanzari-Mnallah, et al.: Synthesis, Conformational Analysis and Crystal Structure of New Thioxo, Oxo, Seleno Diastereomeric Cyclophosphamides Containing 1,3,2-dioxaphosphorinane, Curr. Org. Chem., 23 (2019) 205-213, 10.2174/1385272823666190213142748 

V. Kasari, et al.: A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling, Nucleic Acids Res., 47 (2019) 8807-8820, 10.1093/nar/gkz600

A. Kezar, et al.: Structural basis for the multitasking nature of the potato virus Y coat protein, Sci. Adv., 5 (2019) 13, 10.1126/sciadv.aaw3808 

T. Koval, et al.: Domain structure of HelD, an interaction partner of Bacillus subtilis RNA polymerase, FEBS Lett., 593 (2019) 996-1005, 10.1002/1873-3468.13385 

T. Koval, et al.: Trp-His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer, Scientific Reports, 9 (2019) 13, 10.1038/s41598-019-50105-3 

T. Koval'ova, et al.: Active site complementation and hexameric arrangement in the GH family 29; a structure-function study of alpha-l-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus, Glycobiology, 29 (2019) 59-73, 10.1093/glycob/cwy078 

M. Krafcikova, et al.: Monitoring DNA-Ligand Interactions in Living Human Cells Using NMR Spectroscopy, Journal of the American Chemical Society, 141 (2019) 13281-13285, 10.1021/jacs.9b03031 

A. Kroupa, et al.: The theoretical and experimental study of the Sb-Sn nano-alloys, Calphad-Comput. Coupling Ph. Diagrams Thermochem., 64 (2019) 90-96, 10.1016/j.calphad.2018.11.004 

V. Kuban, et al.: Quantitative Conformational Analysis of Functionally Important Electrostatic Interactions in the Intrinsically Disordered Region of Delta Subunit of Bacterial RNA Polymerase, Journal of the American Chemical Society, 141 (2019) 16817-16828, 10.1021/jacs.9b07837 

E. Lattova, et al.: Applicability of Phenylhydrazine Labeling for Structural Studies of Fucosylated N-Glycans, Anal. Chem., 91 (2019) 7985-7990, 10.1021/acs.analchem.9b01321 

S.T. Le, et al.: Investigation of the Binding Affinity of a Broad Array of l-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin, Molecules, 24 (2019) 17, 10.3390/molecules24122262 

A. Lengalova, et al.: Kinetic analysis of a globin-coupled diguanylate cyclase, YddV: Effects of heme iron redox state, axial ligands, and heme distal mutations on catalysis, J. Inorg. Biochem., 201 (2019) 10, 10.1016/j.jinorgbio.2019.110833 

R. Lizal, et al.: Bambusuril analogs based on alternating glycoluril and xylylene units, Beilstein J. Org. Chem., 15 (2019) 1268-1274, 10.3762/bjoc.15.124 

G. Lochmanova, et al.: Different Modes of Action of Genetic and Chemical Downregulation of Histone Deacetylases with Respect to Plant Development and Histone Modifications, International Journal of Molecular Sciences, 20 (2019) 14, 10.3390/ijms20205093 

E. Makhneva, et al.: Maleic anhydride and acetylene plasma copolymer surfaces for SPR immunosensing, Anal. Bioanal. Chem., 411 (2019) 7689-7697, 10.1007/s00216-019-01979-9 

A. Makki, et al.: Triplet-pore structure of a highly divergent TOM complex of hydrogenosomes in Trichomonas vaginalis, PLoS. Biol., 17 (2019) 32, 10.1371/journal.pbio.3000098 

L. Malinovska, et al.: Synthesis of beta-d-galactopyranoside-Presenting Glycoclusters, Investigation of Their Interactions with Pseudomonas aeruginosa Lectin A (PA-IL) and Evaluation of Their Anti-Adhesion Potential, Biomolecules, 9 (2019) 22, 10.3390/biom9110686 

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