Connecting the Dots: Macromolecular Crowding and Protein Aggregation

[1]  V. Uversky,et al.  On the Role of Normal Aging Processes in the Onset and Pathogenesis of Diseases Associated with the Abnormal Accumulation of Protein Aggregates , 2021, Biochemistry (Moscow).

[2]  A. Naeem,et al.  The contrasting effect of macromolecular crowding and confinement on fibril formation of globular protein: Underlying cause of proteopathies , 2020 .

[3]  S. Deep,et al.  Thinking beyond tradition: Polyphenols as effective refolding modulators. , 2020, International journal of biological macromolecules.

[4]  Faez Iqbal Khan,et al.  An In Vitro elucidation of the antiaggregatory potential of Diosminover thermally induced unfolding of hen egg white lysozyme; A preventive quest for lysozyme amyloidosis. , 2019, International journal of biological macromolecules.

[5]  Harshini K. Ashar,et al.  Dual role for fungal-specific outer kinetochore proteins during cell cycle and development in Magnaporthe oryzae , 2018, Journal of Cell Science.

[6]  D. Holtzman,et al.  Intercellular Spread of Protein Aggregates in Neurodegenerative Disease. , 2018, Annual review of cell and developmental biology.

[7]  S. Moin,et al.  Inhibition of advanced glycation end products by isoferulic acid and its free radical scavenging capacity: An in vitro and molecular docking study. , 2018, International journal of biological macromolecules.

[8]  R. H. Khan,et al.  Probing the binding of phenolic aldehyde vanillin with bovine serum albumin: Evidence from spectroscopic and docking approach. , 2018, Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy.

[9]  A. Naeem,et al.  Aggregation of globular protein as a consequences of macromolecular crowding: A time and concentration dependent study. , 2018, International journal of biological macromolecules.

[10]  A. Boersma,et al.  Microorganisms maintain crowding homeostasis , 2017, Nature Reviews Microbiology.

[11]  J. Frydman,et al.  Protein misfolding in neurodegenerative diseases: implications and strategies , 2017, Translational Neurodegeneration.

[12]  D. Hatters,et al.  When proteostasis goes bad: Protein aggregation in the cell , 2017, IUBMB life.

[13]  Anas Shamsi,et al.  Characterizing harmful advanced glycation end-products (AGEs) and ribosylated aggregates of yellow mustard seed phytocystatin: Effects of different monosaccharides. , 2017, Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy.

[14]  Shruti Mittal,et al.  Macromolecular crowding: Macromolecules friend or foe. , 2015, Biochimica et biophysica acta.

[15]  A. Naeem,et al.  Rifampicin Induced Aggregation of Ovalbumin: Malicious Behaviour of Antibiotics. , 2015, Protein and peptide letters.

[16]  S. Mittal,et al.  Macromolecular Crowding Induces Holo α-Lactalbumin Aggregation by Converting to Its Apo Form , 2014, PloS one.

[17]  S. Mittal,et al.  Macromolecular crowding decelerates aggregation of a β-rich protein, bovine carbonic anhydrase: a case study. , 2014, Journal of biochemistry.

[18]  T. Dar,et al.  Ignored avenues in alpha-synuclein associated proteopathy. , 2014, CNS & neurological disorders drug targets.

[19]  T. Dar,et al.  RECENT TRENDS IN TREATING NEURONAL PROTEINOPATHIES , 2013 .

[20]  S. Mittal,et al.  Denatured State Structural Property Determines Protein Stabilization by Macromolecular Crowding: A Thermodynamic and Structural Approach , 2013, PloS one.

[21]  Gary J. Pielak,et al.  Impact of reconstituted cytosol on protein stability , 2013, Proceedings of the National Academy of Sciences.

[22]  A. Naeem,et al.  Understanding protein folding from globular to amyloid state Aggregation: Darker side of protein , 2013 .

[23]  N. Sugimoto,et al.  Study on effects of molecular crowding on G-quadruplex-ligand binding and ligand-mediated telomerase inhibition. , 2013, Methods.

[24]  L. Tan,et al.  Epidemiology and etiology of Alzheimer's disease: from genetic to non-genetic factors. , 2013, Current Alzheimer research.

[25]  Mathias Jucker,et al.  Self-propagation of pathogenic protein aggregates in neurodegenerative diseases , 2013, Nature.

[26]  Yuji Sugita,et al.  Reduced native state stability in crowded cellular environment due to protein-protein interactions. , 2013, Journal of the American Chemical Society.

[27]  Wei Li,et al.  Macromolecular crowding modulates the kinetics and morphology of amyloid self-assembly by β-lactoglobulin. , 2013, International journal of biological macromolecules.

[28]  M. Ramirez-Alvarado,et al.  Systemic amyloidoses. , 2013, Annual review of biochemistry.

[29]  J. Kundu,et al.  Myoglobin unfolding in crowding and confinement. , 2012, The journal of physical chemistry. B.

[30]  Jun-Mo Yang,et al.  Effects of macromolecular crowding on refolding of recombinant human brain-type creatine kinase. , 2012, International journal of biological macromolecules.

[31]  Jie Chen,et al.  The Contrasting Effect of Macromolecular Crowding on Amyloid Fibril Formation , 2012, PloS one.

[32]  Y. Sugita,et al.  Protein crowding affects hydration structure and dynamics. , 2012, Journal of the American Chemical Society.

[33]  R. K. Mitra,et al.  Role of hydration on the functionality of a proteolytic enzyme α-chymotrypsin under crowded environment. , 2011, Biochimie.

[34]  Claudio Soto,et al.  Misfolded protein aggregates: mechanisms, structures and potential for disease transmission. , 2011, Seminars in cell & developmental biology.

[35]  Raimon Sabate,et al.  Prediction of the aggregation propensity of proteins from the primary sequence: Aggregation properties of proteomes , 2011, Biotechnology journal.

[36]  Joost Schymkowitz,et al.  Gain of function of mutant p53 by coaggregation with multiple tumor suppressors. , 2011, Nature chemical biology.

[37]  Andrew C. Miklos,et al.  Protein crowding tunes protein stability. , 2011, Journal of the American Chemical Society.

[38]  N. Malys,et al.  What is the true enzyme kinetics in the biological system? An investigation of macromolecular crowding effect upon enzyme kinetics of glucose-6-phosphate dehydrogenase. , 2011, Biochemical and biophysical research communications.

[39]  M. Cascante,et al.  Effect of crowding by dextrans on the hydrolysis of N-Succinyl-L-phenyl-Ala-p-nitroanilide catalyzed by α-chymotrypsin. , 2011, The journal of physical chemistry. B.

[40]  Igor Tsigelny,et al.  Cell-to-cell transmission of non-prion protein aggregates , 2010, Nature Reviews Neurology.

[41]  Dirar Homouz,et al.  Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding , 2010, Proceedings of the National Academy of Sciences.

[42]  Gengfu Xiao,et al.  Macromolecular crowding converts the human recombinant PrPc to the soluble neurotoxic β‐oligomers , 2010, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[43]  Qian Wang,et al.  Factors defining effects of macromolecular crowding on protein stability: an in vitro/in silico case study using cytochrome c. , 2010, Biochemistry.

[44]  N. Faridi,et al.  The Effects of Molecular Crowding on the Amyloid Fibril Formation of α-Lactalbumin and the Chaperone Action of α-Casein , 2010, The protein journal.

[45]  Ronald Melki,et al.  Prion-like transmission of protein aggregates in neurodegenerative diseases , 2010, Nature Reviews Molecular Cell Biology.

[46]  P. Bross,et al.  Protein misfolding and cellular stress: an overview. , 2010, Methods in molecular biology.

[47]  Zhengguo Zhou,et al.  Crowded Cell-like Environment Accelerates the Nucleation Step of Amyloidogenic Protein Misfolding* , 2009, The Journal of Biological Chemistry.

[48]  S. Bottomley,et al.  Serpin polymerization and its role in disease—The molecular basis of α1‐antitrypsin deficiency , 2009, IUBMB life.

[49]  D. Oesterhelt,et al.  From shell to cell: neutron scattering studies of biological water dynamics and coupling to activity. , 2009, Faraday discussions.

[50]  Niccolò Taddei,et al.  Aggregation Propensity of the Human Proteome , 2008, PLoS Comput. Biol..

[51]  Vladimir N Uversky,et al.  Guiding protein aggregation with macromolecular crowding. , 2008, Biochemistry.

[52]  C. Mamotte,et al.  Phenylketonuria: an inborn error of phenylalanine metabolism. , 2008, The Clinical biochemist. Reviews.

[53]  George Perry,et al.  Oxidative stress and neurotoxicity. , 2008, Chemical research in toxicology.

[54]  P. Wittung-Stafshede,et al.  Molecular crowding enhances native structure and stability of α/β protein flavodoxin , 2007, Proceedings of the National Academy of Sciences.

[55]  P. Wittung-Stafshede,et al.  Macromolecular crowding increases structural content of folded proteins , 2007, FEBS letters.

[56]  A. Roque,et al.  Macromolecular crowding induces a molten globule state in the C-terminal domain of histone H1. , 2007, Biophysical journal.

[57]  Gideon Schreiber,et al.  Protein-protein association in polymer solutions: from dilute to semidilute to concentrated. , 2007, Biophysical journal.

[58]  Zhihong Guo,et al.  Effects of macromolecular crowding on the intrinsic catalytic efficiency and structure of enterobactin-specific isochorismate synthase. , 2007, Journal of the American Chemical Society.

[59]  Zhihong Guo,et al.  Effects of macromolecular crowding on the intrinsic catalytic efficiency and structure of enterobactin-specific isochorismate synthase. , 2007, Journal of the American Chemical Society.

[60]  R. Swaminathan,et al.  Effect of crowding by dextrans and Ficolls on the rate of alkaline phosphatase-catalyzed hydrolysis: a size-dependent investigation. , 2006, Biopolymers.

[61]  Zhengguo Zhou,et al.  Mixed macromolecular crowding accelerates the refolding of rabbit muscle creatine kinase: implications for protein folding in physiological environments. , 2006, Journal of molecular biology.

[62]  B. Derham,et al.  The effect of the presence of globular proteins and elongated polymers on enzyme activity. , 2006, Biochimica et biophysica acta.

[63]  Christopher M Dobson,et al.  Probing the pressure-temperature stability of amyloid fibrils provides new insights into their molecular properties. , 2006, Biochimica et biophysica acta.

[64]  Vladimir N. Uversky,et al.  Forcing Nonamyloidogenic β-Synuclein To Fibrillate† , 2005 .

[65]  D. Thirumalai,et al.  Molecular crowding enhances native state stability and refolding rates of globular proteins. , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[66]  I. Kholová,et al.  Amyloid in the cardiovascular system: a review , 2005, Journal of Clinical Pathology.

[67]  Zhengguo Zhou,et al.  Mixed Macromolecular Crowding Accelerates the Oxidative Refolding of Reduced, Denatured Lysozyme , 2004, Journal of Biological Chemistry.

[68]  V. Uversky,et al.  The effect of macromolecular crowding on protein aggregation and amyloid fibril formation , 2004, Journal of molecular recognition : JMR.

[69]  C. Ross,et al.  Protein aggregation and neurodegenerative disease , 2004, Nature Medicine.

[70]  Yaakov Levy,et al.  Water and proteins: a love-hate relationship. , 2004, Proceedings of the National Academy of Sciences of the United States of America.

[71]  John F. Carpenter,et al.  Physical Stability of Proteins in Aqueous Solution: Mechanism and Driving Forces in Nonnative Protein Aggregation , 2003, Pharmaceutical Research.

[72]  C. Dobson,et al.  Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution , 2003, Journal of Molecular Medicine.

[73]  Zong Lin,et al.  Effects of Macromolecular Crowding on the Unfolding and the Refolding of d-Glyceraldehyde-3-Phosophospate Dehydrogenase , 2003, Journal of protein chemistry.

[74]  L. Bolund,et al.  Protein misfolding, aggregation, and degradation in disease. , 2003, Methods in molecular biology.

[75]  C. Dobson,et al.  Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases , 2002, Nature.

[76]  Kiowa S. Bower,et al.  Accelerated α‐synuclein fibrillation in crowded milieu , 2002 .

[77]  A. Minton,et al.  Macromolecular Crowding Accelerates Amyloid Formation by Human Apolipoprotein C-II* , 2002, The Journal of Biological Chemistry.

[78]  R. Ellis,et al.  Macromolecular crowding: an important but neglected aspect of the intracellular environment. , 2001, Current opinion in structural biology.

[79]  C. Dobson,et al.  Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell , 2000, The EMBO journal.

[80]  C M Dobson,et al.  Effects of macromolecular crowding on protein folding and aggregation , 1999, The EMBO journal.

[81]  V. Bloomfield,et al.  Crowding effects on EcoRV kinetics and binding. , 1999, Biophysical journal.

[82]  G. Rivas,et al.  Direct observation of the self-association of dilute proteins in the presence of inert macromolecules at high concentration via tracer sedimentation equilibrium: theory, experiment, and biological significance. , 1999, Biochemistry.

[83]  B. Korzeniewski,et al.  Dextran strongly increases the Michaelis constants of oxidative phosphorylation and of mitochondrial creatine kinase in heart mitochondria. , 1998, European journal of biochemistry.

[84]  John Maynard Smith,et al.  The major evolutionary transitions , 1995, Nature.

[85]  M. Mattson,et al.  A model for beta-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[86]  J. Herzfeld,et al.  Macromolecular diffusion in crowded solutions. , 1993, Biophysical journal.

[87]  S. Zimmerman,et al.  Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli. , 1991, Journal of molecular biology.

[88]  G. Careri,et al.  Protein hydration and function. , 1991, Advances in protein chemistry.

[89]  A. Minton,et al.  Tracer diffusion of globular proteins in concentrated protein solutions. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[90]  J. Clegg,et al.  Cellular and molecular consequences of reduced cell water content. , 1982, Cryobiology.

[91]  A. Minton,et al.  Effect of macromolecular crowding upon the structure and function of an enzyme: glyceraldehyde-3-phosphate dehydrogenase. , 1981, Biochemistry.