Brent S. Kendrick

ORCID: 0009-0001-5187-7844
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About
Contact & Profiles
Research Areas
  • Protein purification and stability
  • Plant Pathogens and Fungal Diseases
  • Mycorrhizal Fungi and Plant Interactions
  • Monoclonal and Polyclonal Antibodies Research
  • Viral Infectious Diseases and Gene Expression in Insects
  • Analytical Chemistry and Chromatography
  • Fungal Biology and Applications
  • Yeasts and Rust Fungi Studies
  • Glycosylation and Glycoproteins Research
  • Protein Structure and Dynamics
  • Biosimilars and Bioanalytical Methods
  • Drug Solubulity and Delivery Systems
  • Enzyme Structure and Function
  • Blood properties and coagulation
  • Microencapsulation and Drying Processes
  • Protein Interaction Studies and Fluorescence Analysis
  • Mass Spectrometry Techniques and Applications
  • Enzyme Catalysis and Immobilization
  • Fluid Dynamics and Mixing
  • Plant and Fungal Species Descriptions
  • Metabolomics and Mass Spectrometry Studies
  • Lichen and fungal ecology
  • Plant Pathogens and Resistance
  • Crystallization and Solubility Studies
  • Plant tissue culture and regeneration

Amgen (United States)
2003-2015

Center for Drug Evaluation and Research
2014

United States Food and Drug Administration
2014

University of Colorado Health
1995-2002

University of Colorado Boulder
1997-2002

Canmore Museum and Geoscience Centre
1998

University of Waterloo
1986-1998

University of Colorado Hospital
1998

University of Colorado Denver
1998

We studied the non-native aggregation of recombinant human granulocyte stimulating factor (rhGCSF) in solution conditions where native rhGCSF is both conformationally stable compared to its unfolded state and at concentrations well below solubility limit. Aggregation first involves perturbation structure form a structurally expanded transition state, followed by assembly process an irreversible aggregate. The energy barriers two steps are reflected experimentally measured values free...

10.1110/ps.0235703 article EN Protein Science 2003-04-25

Understanding the mechanism for sucrose-induced protein stabilization is important in many diverse fields, ranging from biochemistry and environmental physiology to pharmaceutical science. Timasheff Lee [Lee, J. C. & Timasheff, S. N. (1981) Biol. Chem. 256, 7193–7201] have established that thermodynamic of proteins by sucrose due preferential exclusion sugar protein’s surface, which increases chemical potential. The current study measures 1 M a drug, recombinant interleukin receptor...

10.1073/pnas.94.22.11917 article EN Proceedings of the National Academy of Sciences 1997-10-28

Intraneuronal deposition of α-synuclein as fibrils and oxidative stress are both implicated in the pathogenesis Parkinson's disease. We found that critical rate-limiting step nucleation under physiological conditions is formation accumulation a dimeric, dityrosine cross-linked prenucleus. Dimer accelerated for pathogenic A30P A53T mutant α-synucleins, because their greater propensity to self-interact, which reflected smaller values osmotic second virial coefficient compared wild-type...

10.1021/bi026528t article EN Biochemistry 2002-12-20

Dry weight, ash-free protein and energy content of food faeces Gammarus pseudolimnaeus Bousfield on different diets were compared. When feeding elm or maple leaves, approximatately 10 % the dry 14-18 protein, 17-19 ingested material was assimilated. mycelium various fungi which commonly decompose leaves in streams offered, assimilated 42.6-75.6 73.3-96.4 67.9-83.2 ingested. These results presumable preference detritius-feeders for leaf areas with higheshyphal concentrations indicate that...

10.2307/3543277 article EN Oikos 1975-01-01

Aggregation of proteins, even under conditions favoring the native state, is a ubiquitous problem in biotechnology and biomedical engineering. Providing mechanistic basis for pathways that lead to aggregation should allow development rational approaches its prevention. We have chosen recombinant human interferon-γ (rhIFN-γ) as model protein study aggregation. In presence 0.9 M guanidinium hydrochloride, rhIFN-γ aggregates with first order kinetics, process inhibited by addition sucrose....

10.1073/pnas.95.24.14142 article EN Proceedings of the National Academy of Sciences 1998-11-24

Abstract Osmolytes increase the thermodynamic conformational stability of proteins, shifting equilibrium between native and denatured states to favor state. However, their effects on equilibria within native‐state ensembles proteins remain controversial. We investigated sucrose, a model osmolyte, fluctuations bovine pancreatic ribonuclease A S horse heart cytochrome c . In presence far‐ near‐UV circular dichroism spectra all three were slightly altered indicated that sugar shifted ensemble...

10.1110/ps.0242603 article EN Protein Science 2003-05-21
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