Tutkijat / Oulu  | Ala-Kokko, L. |
| Ala-Kokko, T(ero) |
| Ala-Korpela, M(ika) |
| Alahuhta, S. |
| Alen, M. |
| Antikainen, R. |
| Anttonen, V(uokko) |
| Biancari, F. |
| Bloigu, R(isto) |
| Eskelinen, S. |
| Flinkkilä, T(apio) |
| Hakkola, J. |
| Hallman, M. |
| Hartikainen, A(nna)-L(iisa) |
| Hausen, H. |
| Hautala, N(ina) |
| Hautala, T(imo) |
| Heape, A. |
| Herzig, K(arl)-H(einz) |
| Hillbom, M. |
| Hiltunen, J.K. |
| Hörkko, S. |
| Huikuri, H |
| Hukkanen J(anne) |
| Ignatius, J. |
| Isohanni, M. |
| Jaakkola, J. |
| Jaakkola, M(aritta) S. |
| Jaakola, V-P. |
| Jämsä, T(imo) |
| Janhonen, S. |
| Järvelin, M(arjo)-R(iitta) |
| Jokelainen, J(ari) |
| Juffer, A.H. |
| Junttila, J(uhani) |
| Juvonen, T. |
| Kaarteenaho, R(iitta) |
| Kajantie, E(ero)*(THL/OY) |
| Karppinen (Koivunen), P(eppi) |
| Karppinen, J(aro) |
| Karttunen, T.J. |
| Keinänen-Kiukaanniemi, S(irkka) |
| Kerkelä, R(isto) |
| Kesäniemi, Y.A. |
| Kettunen, J(ohannes) |
| Kietzmann, T(homas). |
| Kivirikko, K.I. |
| Knuuttila, M. |
| Koivukangas, J. |
| Kursula, P. |
| Kyngäs, H. |
| Larivaara, P. |
| Larmas, M. |
| Lehenkari, P(etri) |
| Lehtiö, L(ari) |
| Leppilahti, J. |
| Luukinen, H. |
| Mainio A |
| Majamaa, K. |
| Mäki, P(irjo) |
| Mäkikallio, T. |
| Männikkö, M(inna) |
| Manninen, A(ki). |
| Martikainen, H(annu) |
| Miettunen, J(ouko) |
| Myllyharju, J. |
| Myllylä, R. |
| Myllylä, V. |
| Näyhä, S. |
| Neubauer, P. |
| Nieminen, M(iika) T. |
| Nieminen, P(entti) |
| Niinimäki, J(aakko) |
| Ohukainen, P(auli) |
| Oikarinen, A. |
| Oikarinen, K. |
| Pelkonen, O(lavi) |
| Petäjä-Repo, U.E. |
| Pihlajaniemi, T. |
| Pirttiniemi, P(ertti) |
| Puistola, U(lla) |
| Rajaniemi, H.J. |
| Rämet, M(ika) |
| Räsänen, P. |
| Raustia, A. |
| Remes, A(nne) |
| Risteli, J. |
| Ristiniemi, J. |
| Ruddock, L.W. |
| Ruokonen, A. |
| Ruskoaho, H. |
| Ryynänen, M. |
| Saarakkala, S. |
| Saari, A. |
| Salo, T(uula) |
| Sándor, G(eorge) K. |
| Savolainen, E-R. |
| Savolainen, M.J. |
| Savolainen, O. |
| Sillanpää, M(ikko). |
| Soininen, R. |
| Sorri, M. |
| Taanila, A. |
| Tapiainen, T(erhi) |
| Tervonen, O(smo) |
| Timonen, M(arkku) |
| Tjäderhane, L. |
| Turpeenniemi-Hujanen, T. |
| Tuukkanen, J(uha) |
| Tuulonen, A. |
| Uhari, M. |
| Ukkola, O(lavi) |
| Uusimaa, J. |
| Vainio, O. |
| Vainio, S. |
| Veijola, J(uha) |
| Veijola, R(iitta) |
| Virokannas, H. |
| Voipio, H(anna)-M(arja) |
| Vuolteenaho, O. |
| Weckström, M. |
| Wei, GH. |
| Wierenga, R.K. |
| Winqvist, R. |
| Ylänne, J. |
| Ylitalo, K(ari) |
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| | Non-native proteins inhibit the ER oxidoreductin 1 (Ero1)-protein disulfide isomerase relay when protein folding capacity is exceeded. | Ruddock, L.W. | 127 days | save |  |  |  | |
| Production of Extracellular Matrix Proteins in the Cytoplasm of E. coli: Making Giants in Tiny Factories. | Ruddock, L.W. | 162 days | save | | | | |
| Applications of catalyzed cytoplasmic disulfide bond formation. | Ruddock, L.W. | 245 days | save | | | | |
| Efficient production of wild-type lipase B from Candida antarctica in the cytoplasm of Escherichia coli. | Ruddock, L.W. | 292 days | save | | | | |
| The crystal structure of human microsomal triglyceride transfer protein. | Ruddock, L.W. | 329 days | save | | | | |
| Molecular analysis of human Ero1 reveals novel regulatory mechanisms for oxidative protein folding. | Ruddock, L.W. | 592 days | save | | | | |
| Biallelic mutations in human NHLRC2 enhance myofibroblast differentiation in FINCA disease. | Ruddock, L.W. | 652 days | save | | | | |
| Structural analysis of human NHLRC2, mutations of which are associated with FINCA disease. | Ruddock, L.W. | 681 days | save | | | | |
| Crystal structure of human anterior gradient protein 3. | Ruddock, L.W. | 732 days | save | | | | |
| Structures of Angptl3 and Angptl4, modulators of triglyceride levels and coronary artery disease. | Ruddock, L.W. | 795 days | save | | | | |
| Complementarity determining regions and frameworks contribute to the disulfide bond independent folding of intrinsically stable scFv. | Ruddock, L.W. | 929 days | save | | | | |
| Efficient soluble expression of disulfide bonded proteins in the cytoplasm of Escherichia coli in fed-batch fermentations on chemically defined minimal media. | Ruddock, L.W. | 1112 days | save | | | | |
| ALS-linked protein disulfide isomerase variants cause motor dysfunction. | Ruddock, L.W. | 1603 days | save | | | | |
| Systematic screening of soluble expression of antibody fragments in the cytoplasm of E. coli. | Ruddock, L.W. | 1620 days | save | | | | |
| Division of labor between oxidoreductases: TMX1 preferentially acts upon transmembrane polypeptides. | Ruddock, L.W. | 1792 days | save | | | | |
| Efficient export of human growth hormone, interferonα2b and antibody fragments to the periplasm by the Escherichia coli Tat pathway in the absence of prior disulfide bond formation. | Ruddock, L.W. | 2009 days | save | | | | |
| Protein Disulfide-Isomerase Interacts with a Substrate Protein at All Stages along Its Folding Pathway. | Ruddock, L.W. | 2349 days | save | | | | |
| Efficient export of prefolded, disulfide-bonded recombinant proteins to the periplasm by the Tat pathway in Escherichia coli CyDisCo strains. | Ruddock, L.W. | 2377 days | save | | | | |
| Topological plasticity of enzymes involved in disulfide bond formation allows catalysis in either the periplasm or the cytoplasm. | Ruddock, L.W. | 2559 days | save | | | | |
| Disulfide bond formation in the cytoplasm. | Ruddock, L.W. | 2886 days | save | | | | |
| Low molecular weight oxidants involved in disulfide bond formation. | Ruddock, L.W. | 3109 days | save | | | | |
| Beyond KDEL: The role of positions 5 and 6 in determining ER localization. | Ruddock, L.W. | 3371 days | save | | | | |
| Re-examination of the role of interplay between glutathione and protein disulphide isomerase. | Ruddock, L.W. | 3388 days | save | | | | |
| Two endoplasmic reticulum PDI-peroxidases increase the efficiency of the use of peroxide during disulfide bond formation. | Ruddock, L.W. | 3462 days | save | | | | |
| Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E.coli. | Ruddock, L.W. | 3466 days | save | | | | |
| Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E.coli. | Ruddock, L.W. | 3581 days | save | | | | |
| Bacitracin is not a specific inhibitor of protein disulfide isomerase. | Ruddock, L.W. | 3700 days | save | | | | |
| Modulation of an active site cysteine pK(a) allows PDI to act both as a catalyst of disulfide bond formation and isomerization. | Ruddock, L.W. | 3846 days | save | | | | |
| The ligand-binding b' domain of human protein disulphide-isomerase mediates homo-dimerization. | Ruddock, L.W. | 3909 days | save | | | | |
| THE ROLE OF DEHYDROASCORBATE IN DISULFIDE BOND FORMATION. | Ruddock, L.W. | 3972 days | save | | | | |
| Mapping of the ligand binding site on the b' domain of human PDI; interaction with peptide ligands and the x-linker region. | Ruddock, L.W. | 4005 days | save | | | | |
| Modulating proteostasis: peptidomimetic inhibitors and activators of protein folding. | Ruddock, L.W. | 4006 days | save | | | | |
| PROTEIN DISULFIDE ISOMERASE: A CRITICAL EVALUATION OF ITS FUNCTION IN DISULFIDE BOND FORMATION. | Ruddock, L.W. | 4053 days | save | | | | |
| THE C-TERMINAL ACTIVE SITE CYSTEINE OF ESCHERICHIA COLI GLUTAREDOXIN 1 DETERMINES THE GLUTATHIONE SPECIFICITY OF THE SECOND STEP OF PEPTIDE DEGLUTATHIONYLATION. | Ruddock, L.W. | 4099 days | save | | | | |
| Solution Structure and Dynamics of ERp18: a Small ER Resident Oxidoreductase. | Ruddock, L.W. | 4099 days | save | | | | |
| EFFICIENT PEROXIDE MEDIATED OXIDATIVE REFOLDING OF A PROTEIN AT PHYSIOLOGICAL PH AND IMPLICATIONS FOR OXIDATIVE FOLDING IN THE ENDOPLASMIC RETICULUM. | Ruddock, L.W. | 4202 days | save | | | | |
| Alternative Conformations of the x Region of Human Protein Disulphide-Isomerase Modulate Exposure of the Substrate Binding b' Domain. | Ruddock, L.W. | 4305 days | save | | | | |
| Substrate recognition by the protein disulfide isomerases. | Ruddock, L.W. | 4666 days | save | | | | |
| Protein Disulfide Isomerases from C. elegans are Equally Efficient at Thiol-Disulfide Exchange in Simple Peptide-Based Systems But Show Differences in Reactivity Towards Protein Substrates. | Ruddock, L.W. | 4700 days | save | | | | |
| Glutathione S-transferase omega in the lung and sputum supernatants of COPD patients. | Ruddock, L.W. | 4744 days | save | | | | |
| Does s-methyl methanethiosulfonate trap the thiol-disulfide state of proteins? | Ruddock, L.W. | 4897 days | save | | | | |
| N-glycan processing in ER quality control. | Ruddock, L.W. | 4995 days | save | | | | |
| Modulation of glutaredoxin in the lung and sputum of cigarette smokers and chronic obstructive pulmonary disease. | Ruddock, L.W. | 5000 days | save | | | | |
| EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation. | Ruddock, L.W. | 5035 days | save | | | | |
| The human protein disulphide isomerase family: substrate interactions and functional properties. | Ruddock, L.W. | 5042 days | save | | | | |
| pH dependence of the peptide thiol-disulfide oxidase activity of six members of the human protein disulfide isomerase family. | Ruddock, L.W. | 5048 days | save | | | | |
| Insights into deglutathionylation reactions: Different intermediates in the glutaredoxin and protein disulphide isomerase catalysed reactions are defined by the gamma-linkage present in glutathione. | Ruddock, L.W. | 5049 days | save | | | | |
| ERP27, a new non-catalytic endoplasmic reticulum located human pdi-family member, interacts with ERP57. | Ruddock, L.W. | 5057 days | save | | | | |
| Gaining access to ERp57 function. | Ruddock, L.W. | 5073 days | save | | | | |
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