J. Kolkman

发表

Multivalent avimer proteins evolved by exon shuffling of a family of human receptor domains

W. Stemmer, E. Whitehorn, C. Swimmer, 2005, Nature biotechnology.

Directed evolution of proteins by exon shuffling

W. Stemmer, J. Kolkman, Willem P.C. Stemmer, 2001, Nature Biotechnology.

Nanobodies - from llamas to therapeutic proteins.

J. Kolkman, D. Law, 2010, Drug discovery today. Technologies.

Surface Loop 199–204 in Blood Coagulation Factor IX Is a Cofactor-dependent Site Involved in Macromolecular Substrate Interaction*

O. Christophe, P. Lenting, J. Kolkman, 1999, The Journal of Biological Chemistry.

Blood Coagulation Factor IX Residues Glu78 and Arg94 Provide a Link between Both Epidermal Growth Factor-like Domains That Is Crucial in the Interaction with Factor VIII Light Chain*

O. Christophe, P. Lenting, G. Brownlee, 1998, The Journal of Biological Chemistry.

Regions 301-303 and 333-339 in the catalytic domain of blood coagulation factor IX are factor VIII-interactive sites involved in stimulation of enzyme activity.

P. Lenting, J. Kolkman, K. Mertens, 1999, The Biochemical journal.

Factor VIII-Factor IX Interactions: Molecular Sites Involved in Enzyme-Cofactor Complex Assembly

P. Lenting, J. Kolkman, P. Celie, 1999, Thrombosis and Haemostasis.

On the two iron centers of desulfoferrodoxin

W. Hagen, J. Kolkman, M. Verhagen, 1993, FEBS letters.

The preclinical pharmacology of the high affinity anti-IL-6R Nanobody® ALX-0061 supports its clinical development in rheumatoid arthritis

B. '. ’t Hart, J. Kolkman, H. Ulrichts, 2015, Arthritis Research & Therapy.

Multivalent nanobodies targeting death receptor 5 elicit superior tumor cell killing through efficient caspase induction

W. Sellers, Guizhi Yang, C. Kowal, 2014, mAbs.

Nanobodies Targeting the Hepatocyte Growth Factor: Potential New Drugs for Molecular Cancer Therapy

G. V. van Dongen, J. Vercammen, J. Kolkman, 2012, Molecular Cancer Therapeutics.

Molecular evolution of mammalian ribonucleases 1.

J. Dubois, B. Ursing, J. Kolkman, 2003, Molecular phylogenetics and evolution.

Surface-loop residue Lys316 in blood coagulation Factor IX is a major determinant for Factor X but not antithrombin recognition.

J. Kolkman, K. Mertens, 2000, The Biochemical journal.

Universal protection against influenza infection by a multidomain antibody to influenza hemagglutinin

Jinquan Luo, Galina Obmolova, Andrew B. Ward, 2018, Science.

Residues Phe342–Asn346 of Activated Coagulation Factor IX Contribute to the Interaction with Low Density Lipoprotein Receptor-related Protein*

P. Lenting, J. Kolkman, K. Mertens, 2003, The Journal of Biological Chemistry.

Insertion loop 256-268 in coagulation factor IX restricts enzymatic activity in the absence but not in the presence of factor VIII.

J. Kolkman, K. Mertens, 2000, Biochemistry.

Multivalent avimer proteins evolved by exon shuffling of a family of human receptor domains

W. Stemmer, E. Whitehorn, C. Swimmer, 2005, Nature Biotechnology.