Zobrazeno 1 - 9 of 9 pro vyhledávání: '"Niklas Engler"'
1
Establishing a control system using QbD principles
Autor: Lynne A. Krummen, Brian D. Kelley, Niklas Engler, Raquel Iverson, Gerald Gellermann, Ron Taticek, Christof Finkler, Reed J. Harris, Lynn A. Gennaro, Mary E.M. Cromwell, J. Felix Kepert, Nathan McKnight, Paul Motchnik, Volker Schnaible
Publikováno v: Biologicals : journal of the International Association of Biological Standardization. 44(5)
Quality by design (QbD) is a global regulatory initiative with the goal of enhancing pharmaceutical development through the proactive design of pharmaceutical manufacturing process and controls to consistently deliver the intended performance of the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b38b658a3d778fd4dbaad2ce6e6806f
https://pubmed.ncbi.nlm.nih.gov/27430904
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2
A water network within a protein: temperature-dependent water ligation in H64V-metmyoglobin and relaxation to deoxymyoglobin
Autor: Andreas Ostermann, Fritz G. Parak, Valeri E. Prusakov, Niklas Engler
Publikováno v: Scopus-Elsevier
The sperm whale myoglobin mutant H64V, where the distal histidine is mutated to valine, is known to be five coordinated in the ferric state at room tem- perature and physiological pH. A change of the ligation in this H64V-Mbmet has been observed by o
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ca3693b9772270a178c246686415b5b
https://doi.org/10.1007/s00249-002-0255-x
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3
Hydrogen and deuterium in myoglobin as seen by a neutron structure determination at 1.5 Å resolution
Autor: Nobuo Niimura, Niklas Engler, Ichiro Tanaka, Fritz G. Parak, Andreas Ostermann
Publikováno v: Biophysical Chemistry. 95:183-193
From the first days of protein neutron structure determination sperm whale myoglobin was an object under investigation [Nature 224 (1969) 143, J. Mol. Biol. 220 (1991) 381]. Nevertheless myoglobin is still of interest [Proc. Natl. Acad. Sci. USA 97 (
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45ed0f615ccf5fd24016e66e3535313f
https://doi.org/10.1016/s0301-4622(01)00255-1
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4
High-throughput work flow for IgG Fc-glycosylation analysis of biotechnological samples
Autor: Niklas Engler, Maurice H. J. Selman, Dietmar Reusch, André M. Deelder, Manfred Wuhrer, Markus Haberger, Patrick Bulau
Publikováno v: Analytical Biochemistry, 432(2), 82-89
Immunoglobulin G (IgG) fragment crystallizable (Fc) glycosylation is crucial for antibody effector functions such as antibody-dependent cellular cytotoxicity and complement-dependent cytotoxicity. To monitor IgG Fc glycosylation, high-throughput tech
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6dcbb6ade3ffe1f598fc2bf29658330
http://hdl.handle.net/1887/98985
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5
Spectral broadening of the Soret band in myoglobin: an interpretation by the full spectrum of low-frequency modes from a normal modes analysis
Autor: Maurizio Leone, Antonio Cupane, Fritz G. Parak, Eugenio Vitrano, Niklas Engler, Lorenzo Cordone, Marco Cammarata
Publikováno v: European biophysics journal : EBJ. 34(7)
In this work the temperature dependence of the Soret band line shape in carbon-monoxy myoglobin is re-analyzed by using both the full correlator approach in the time domain and the frequency domain approach. The new analyses exploit the full density
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0969910dc7cdbbb7490444e766320138
https://pubmed.ncbi.nlm.nih.gov/16215751
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6
Hydrogen atoms in proteins: positions and dynamics
Autor: Andreas Ostermann, Nobuo Niimura, Fritz G. Parak, Niklas Engler
Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 100(18)
Hydrogen atoms constitute about half of the atoms in proteins. Thus they contribute to the complex energy landscape of proteins [Frauenfelder, H., Sligar, S. G. & Wolynes, P. G. (1991) Science 254, 1598-1603]. Neutron crystal structure analysis was u
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::180fda83b2dc0c455e16c26e82e41c6c
https://pubmed.ncbi.nlm.nih.gov/12937341
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7
Structural Relaxation from X- ray irradiated metastable Hbmet investigated by Mössbauer Spectroscopy
Autor: Andreas W. E. Dilg, Fritz G. Parak, Niklas Engler, O. Iakovleva, Valeri E. Prusakov, I. Ortalli, S. Croci
Publikováno v: Hyperfine Interactions (C) ISBN: 9781402010873
Protein functions are strictly connected to their structural dynamics. Actually, the study of haemoglobin metastable states is a useful way to have insight in to structural changes that lead the protein from one stable state to another. Mossbauer spe
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9a4c9f3878ab4f8c67135ca06b921b92
https://doi.org/10.1007/978-94-010-0281-3_59
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8
Protein dynamics in an intermediate state of myoglobin: optical absorption, resonance Raman spectroscopy, and x-ray structure analysis
Autor: Don C. Lamb, Andreas Ostermann, Niklas Engler, Valeri E. Prusakov, Fritz G. Parak, Alexandra Gassmann, Joachim Schott, Reinhard Schweitzer-Stenner
Publikováno v: Scopus-Elsevier
A metastable state of myoglobin is produced by reduction of metmyoglobin at low temperatures. This is done either by irradiation with x-rays at 80 K or by electron transfer from photoexcited tris(2, 2'-bipyridine)-ruthenium(II) at 20 K. At temperatur
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7464a36e7545f774167e781d2e136f36
https://europepmc.org/articles/PMC1300800/
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