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Biophysical Reviews, ISSN 1867-2450, 6/2013, Volume 5, Issue 2, pp. 187 - 194
The intracellular milieu is complex, heterogeneous and crowded—an environment vastly different from dilute solutions in which most biophysical studies are... 
Biochemistry, general | Excluded volume | Membrane Biology | Second virial coefficient | Biological Techniques | Protein stability | Biophysics and Biological Physics | Crowding | Osmolytes | Cell Biology | Life Sciences | Synthetic polymers | Nanotechnology
Journal Article
Protein Science, ISSN 0961-8368, 09/2014, Volume 23, Issue 9, pp. 1161 - 1164
Journal Article
Neuron, ISSN 0896-6273, 08/2017, Volume 95, Issue 4, pp. 808 - 816.e9
Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are age-related neurodegenerative disorders with shared genetic etiologies and... 
low-complexity domain | liquid-liquid phase separation | TDP-43 | T cell-restricted intracellular antigen-1 | stress granules | frontotemporal dementia | amyotrophic lateral sclerosis | membrane-less organelle | frontotemporal lobar degeneration | MULTISYSTEM PROTEINOPATHY | DISTAL MYOPATHY | MESSENGER-RNA | LIQUID DROPLETS | SEQUENCING DATA | HEXANUCLEOTIDE REPEAT | DOMAINS | C9ORF72 | NEUROSCIENCES | FAMILIAL ALS | Humans | Middle Aged | Family Health | Male | Green Fluorescent Proteins - genetics | DNA-Binding Proteins - metabolism | Transfection | Time Factors | Adult | Female | T-Cell Intracellular Antigen-1 | Frontotemporal Dementia - pathology | Frontotemporal Dementia - genetics | Stress, Physiological - physiology | Green Fluorescent Proteins - metabolism | Poly(A)-Binding Proteins - genetics | Amyotrophic Lateral Sclerosis - genetics | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism | RNA-Binding Protein FUS - metabolism | Mutation - genetics | Heterogeneous Nuclear Ribonucleoprotein A1 | Microscopy, Confocal | Amyotrophic Lateral Sclerosis - pathology | Aged | HeLa Cells | Nervous system diseases | RNA | Analysis | Genetic research | Development and progression | Amyotrophic lateral sclerosis | Genetic aspects | T cells | Binding proteins | Protein binding | Dementia | Disease | Pathogenesis | Genes | Disorders | Lymphocytes T | Phase transitions | Proteins | Consortia | DNA-binding protein | Etiology | Dementia disorders | Age | Deoxyribonucleic acid--DNA | Phase transformations | Neurodegenerative diseases | Metabolism | Ribonucleic acid--RNA | Pathology | Phase separation | Mutation | Frontotemporal dementia | Dismantling | Phase transition | T-cell-restricted intracellular antigen-1
Journal Article
Biochemistry, ISSN 0006-2960, 2014, Volume 53, Issue 10, pp. 1601 - 1606
Macromolecular crowding effects arise from steric repulsions and weak, nonspecific, chemical interactions. Steric repulsions stabilize globular proteins, but... 
CELLS | NMR | CI-2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | DYNAMICS | BINDING | HYDROGEN-EXCHANGE | GLOBULAR-PROTEIN | NUCLEIC-ACIDS | Kinetics | Protein Stability | Peptides - chemistry | Escherichia coli - chemistry | Escherichia coli Proteins - chemistry | Plant Proteins - chemistry | Proteins | Physiological aspects | Thermodynamics | Research | Analysis | Escherichia coli
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 05/2011, Volume 133, Issue 18, pp. 7116 - 7120
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 10/2012, Volume 134, Issue 40, pp. 16614 - 16618
Journal Article
Journal of Clinical Investigation, ISSN 0021-9738, 03/2018, Volume 128, Issue 3, pp. 1164 - 1177
Journal Article
Cell, ISSN 0092-8674, 10/2016, Volume 167, Issue 3, pp. 774 - 788.e17
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2013, Volume 110, Issue 48, p. 19342
  Protein stability is usually studied in simple buffered solutions, but most proteins function inside cells, where the heterogeneous and crowded environment... 
Proteins | Nuclear magnetic resonance--NMR | E coli | Cytoplasm | Cells
Journal Article
Journal of Physical Chemistry C, ISSN 1932-7447, 04/2009, Volume 113, Issue 16, pp. 6839 - 6844
Journal Article
Protein Science, ISSN 0961-8368, 10/2013, Volume 22, Issue 10, pp. 1313 - 1319
Journal Article
01/2014, ISBN 9781303942327
The intracellular milieu is complex, heterogeneous and crowded—an environment vastly different from dilute, buffered solutions where most biophysical studies... 
Biochemistry | Biophysics
Dissertation
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