Mark Ultsch mainly investigates Receptor, Biochemistry, Binding site, Peptide sequence and Antibody. His Receptor research is multidisciplinary, incorporating perspectives in Extracellular, Phage display and Ternary complex. In his work, Plasma protein binding is strongly intertwined with Biophysics, which is a subfield of Biochemistry.
His Peptide sequence study combines topics in areas such as Peptide bond, Subtilisin, Stereochemistry and Hydrogen bond. His Stereochemistry research is multidisciplinary, relying on both Hydrolase and Hormone, Prolactin. His research investigates the connection with Antibody and areas like Molecular biology which intersect with concerns in Complement system, Glycosylation, Cytotoxicity and Mutagenesis.
Biochemistry, Stereochemistry, Receptor, Biophysics and Antibody are his primary areas of study. He works mostly in the field of Biochemistry, limiting it down to topics relating to In vivo and, in certain cases, In vitro. As part of one scientific family, he deals mainly with the area of Stereochemistry, narrowing it down to issues related to the Structure–activity relationship, and often Drug discovery and ADME.
His work in Receptor addresses subjects such as Extracellular, which are connected to disciplines such as Ternary complex, Internal medicine and Endocrinology. His Biophysics study combines topics from a wide range of disciplines, such as Binding protein, Plasma protein binding and Mechanism of action. His Antibody research includes elements of Molecular biology and Glycosylation.
His main research concerns Biochemistry, Stereochemistry, Antibody, Lactate dehydrogenase and Pharmacology. He incorporates Biochemistry and Identification in his research. His work carried out in the field of Stereochemistry brings together such families of science as Structure–activity relationship, Binding site and Gene isoform.
Mark Ultsch combines subjects such as Receptor, Cancer research and Molecular biology with his study of Antibody. His Receptor study deals with Effector intersecting with Mechanism of action. His Pharmacology study which covers Enzyme that intersects with In vivo.
Mark Ultsch mainly focuses on Biochemistry, Tyrosine kinase 2, Lactate dehydrogenase, Identification and Antibody. His biological study spans a wide range of topics, including Thio- and Crystal structure. Tyrosine kinase 2 combines with fields such as Structure–activity relationship, Genetics, Phenotype, Genomics and Gene in his work.
His studies deal with areas such as Potency, Benzamide, In vivo and Enzyme as well as Structure–activity relationship. His Lactate dehydrogenase research is multidisciplinary, relying on both Stereochemistry and Pyrazine. His Antibody research includes themes of Receptor, Cytokine and Mechanism of action.
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Human growth hormone and extracellular domain of its receptor: crystal structure of the complex.
AM de Vos;M Ultsch;AA Kossiakoff.
Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule
BC Cunningham;M Ultsch;AM De Vos;MG Mulkerrin.
Mapping of the C1q Binding Site on Rituxan, a Chimeric Antibody with a Human IgG1 Fc
E E Idusogie;L G Presta;H Gazzano-Santoro;K Totpal.
Journal of Immunology (2000)
Convergent solutions to binding at a protein-protein interface.
Warren L. DeLano;Mark H. Ultsch;Abraham M. de;Vos.
Bcl10 activates the NF-κB pathway through ubiquitination of NEMO
Honglin Zhou;Ingrid Wertz;Ingrid Wertz;Karen O'Rourke;Mark Ultsch.
Engineered Antibodies with Increased Activity to Recruit Complement
Esohe E. Idusogie;Pin Yee Wong;Leonard G. Presta;Helene Gazzano-Santoro.
Journal of Immunology (2001)
The X-ray structure of a growth hormone–prolactin receptor complex
W Somers;M Ultsch;A M De Vos;A A Kossiakoff.
Mechanism of MEK inhibition determines efficacy in mutant KRAS- versus BRAF-driven cancers
Georgia Hatzivassiliou;Jacob R. Haling;Huifen Chen;Kyung Song.
Peptide exosite inhibitors of factor VIIa as anticoagulants
Mark S. Dennis;Charles Eigenbrot;Nicholas J. Skelton;Mark H. Ultsch.
Structural plasticity in a remodeled protein-protein interface
Shane Atwell;Mark Ultsch;Mark Ultsch;Abraham M. De Vos;Abraham M. De Vos;James A. Wells;James A. Wells.
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