inclusion bodies

Summary

Summary: A generic term for any circumscribed mass of foreign (e.g., lead or viruses) or metabolically inactive materials (e.g., ceroid or MALLORY BODIES), within the cytoplasm or nucleus of a cell. Inclusion bodies are in cells infected with certain filtrable viruses, observed especially in nerve, epithelial, or endothelial cells. (Stedman, 25th ed)

Top Publications

  1. Singh S, Sharma A, Upadhyay A, Singh A, Garg L, Panda A. Solubilization of inclusion body proteins using n-propanol and its refolding into bioactive form. Protein Expr Purif. 2012;81:75-82 pubmed publisher
    b>Inclusion bodies of recombinant human growth hormone (r-hGH) were isolated from Escherichia coli, enriched and solubilized in 100mM Tris buffer containing 6M n-propanol and 2M urea...
  2. Bruinzeel W, Masure S. Recombinant expression, purification and dimerization of the neurotrophic growth factor Artemin for in vitro and in vivo use. Protein Expr Purif. 2012;81:25-32 pubmed publisher
    ..Escherichia coli expression of an NH(2)-terminal SUMO-Artemin fusion protein and subsequent refolding from inclusion bodies followed by cleavage of the SUMO fusion part, mature Artemin with a native NH(2)-terminal amino acid sequence ..
  3. Schipper Krom S, Juenemann K, Jansen A, Wiemhoefer A, van den Nieuwendijk R, Smith D, et al. Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies. FEBS Lett. 2014;588:151-9 pubmed publisher
    ..Whether proteasomes are irreversibly recruited into inclusion bodies in these protein misfolding disorders is a controversial subject...
  4. Ito D, Yagi T, Ikawa M, Suzuki N. Characterization of inclusion bodies with cytoprotective properties formed by seipinopathy-linked mutant seipin. Hum Mol Genet. 2012;21:635-46 pubmed publisher
    ..Furthermore, cells expressing mutant seipin contain unique cytoplasmic inclusion bodies (IB) that form via a different mechanism from that of ubiquitinated inclusions, or aggresomes...
  5. Zhou B, Xing L, Wu W, Zhang X, Lin Z. Small surfactant-like peptides can drive soluble proteins into active aggregates. Microb Cell Fact. 2012;11:10 pubmed publisher
    Inactive protein inclusion bodies occur commonly in Escherichia coli (E. coli) cells expressing heterologous proteins...
  6. Coutard B, Danchin E, Oubelaid R, Canard B, Bignon C. Single pH buffer refolding screen for protein from inclusion bodies. Protein Expr Purif. 2012;82:352-9 pubmed publisher
    ..reported the set up of an automated test for screening the refolding of recombinant proteins expressed as inclusion bodies in Escherichia coli[1]...
  7. Villar Piqué A, Espargaro A, Sabate R, de Groot N, Ventura S. Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors. Microb Cell Fact. 2012;11:55 pubmed publisher
    ..In particular, the presence of endogenous metal ions has been linked to the pathogenesis of AD and other neurodegenerative disorders...
  8. Bentmann E, Neumann M, Tahirovic S, Rodde R, Dormann D, Haass C. Requirements for stress granule recruitment of fused in sarcoma (FUS) and TAR DNA-binding protein of 43 kDa (TDP-43). J Biol Chem. 2012;287:23079-94 pubmed publisher
  9. Fusco C, Micale L, Egorov M, Monti M, D Addetta E, Augello B, et al. The E3-ubiquitin ligase TRIM50 interacts with HDAC6 and p62, and promotes the sequestration and clearance of ubiquitinated proteins into the aggresome. PLoS ONE. 2012;7:e40440 pubmed publisher
    ..We speculate that when the proteasome activity is impaired, TRIM50 fails to drive its substrates to the proteasome-mediated degradation, and promotes their storage in the aggresome for successive clearance...

More Information

Publications76

  1. Huang Z, Zhang C, Chen S, Ye F, Xing X. Active inclusion bodies of acid phosphatase PhoC: aggregation induced by GFP fusion and activities modulated by linker flexibility. Microb Cell Fact. 2013;12:25 pubmed publisher
    Biologically active inclusion bodies (IBs) have gained much attention in recent years. Fusion with IB-inducing partner has been shown to be an efficient strategy for generating active IBs...
  2. Furgerson M, Fechheimer M, Furukawa R. Model Hirano bodies protect against tau-independent and tau-dependent cell death initiated by the amyloid precursor protein intracellular domain. PLoS ONE. 2012;7:e44996 pubmed publisher
    ..In addition, apoptosis was determined to contribute to cell death. The presence of model Hirano bodies protected against cell death, indicating Hirano bodies may play a protective role in neurodegeneration...
  3. Nonaka T, Masuda Suzukake M, Arai T, Hasegawa Y, Akatsu H, Obi T, et al. Prion-like properties of pathological TDP-43 aggregates from diseased brains. Cell Rep. 2013;4:124-34 pubmed publisher
    ..These results indicate that insoluble TDP-43 has prion-like properties that may play a role in the progression of TDP-43 proteinopathy. ..
  4. Pandey N, Sachan A, Chen Q, Ruebling Jass K, Bhalla R, Panguluri K, et al. Screening and identification of genetic loci involved in producing more/denser inclusion bodies in Escherichia coli. Microb Cell Fact. 2013;12:43 pubmed publisher
    ..Producing proteins/peptides as inclusion bodies in the hosts has the potential to achieve both high titers in fermentation and cost-effective downstream ..
  5. Li M, Fan H, Liu J, Wang M, Wang L, Wang C. High pH solubilization and chromatography-based renaturation and purification of recombinant human granulocyte colony-stimulating factor from inclusion bodies. Appl Biochem Biotechnol. 2012;166:1264-74 pubmed publisher
    ..In this study, rhG-CSF was solubilized from inclusion bodies by using a high-pH solution containing low concentration of urea...
  6. Liovic M, Ozir M, Zavec A, Peternel S, Komel R, Zupancic T. Inclusion bodies as potential vehicles for recombinant protein delivery into epithelial cells. Microb Cell Fact. 2012;11:67 pubmed publisher
    We present the potential of inclusion bodies (IBs) as a protein delivery method for polymeric filamentous proteins. We used as cell factory a strain of E...
  7. Farg M, Soo K, Warraich S, Sundaramoorthy V, Blair I, Atkin J. Ataxin-2 interacts with FUS and intermediate-length polyglutamine expansions enhance FUS-related pathology in amyotrophic lateral sclerosis. Hum Mol Genet. 2013;22:717-28 pubmed publisher
    ..These findings describe new cellular mechanisms linking ALS with ataxin-2 intermediate length polyQ expansions and provide further evidence linking disruption to ER-Golgi compartments and FUS pathology in ALS...
  8. Gunda V, Boosani C, Verma R, Guda C, Sudhakar Y. L-arginine mediated renaturation enhances yield of human, ?6 Type IV collagen non-collagenous domain from bacterial inclusion bodies. Protein Pept Lett. 2012;19:1112-21 pubmed
    ..effect of L-arginine mediated renaturation in enhancing the relative yields of this protein from bacterial inclusion bodies has not been evaluated...
  9. Elwell C, Engel J. Lipid acquisition by intracellular Chlamydiae. Cell Microbiol. 2012;14:1010-8 pubmed publisher
    ..In this review, we highlight recent findings that have significantly expanded our understanding of how Chlamydia exploit lipid trafficking pathways to ensure the survival of this important human pathogen...
  10. Cooper Knock J, Hewitt C, Highley J, Brockington A, Milano A, Man S, et al. Clinico-pathological features in amyotrophic lateral sclerosis with expansions in C9ORF72. Brain. 2012;135:751-64 pubmed publisher
    ..0005) discriminated C9ORF72 cases strongly from the rest of the cohort. Inclusions in CA4 neurons were not present in non-C9ORF72 cases, indicating that this pathology predicts mutation status. ..
  11. Skibinski G, Nakamura K, Cookson M, Finkbeiner S. Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies. J Neurosci. 2014;34:418-33 pubmed publisher
    ..Neurons ectopically expressing mutant LRRK2 formed inclusion bodies (IBs), retracted neurites, accumulated synuclein, and died prematurely, recapitulating key features of PD...
  12. Seras Franzoso J, Díez Gil C, Vazquez E, García Fruitós E, Cubarsi R, Ratera I, et al. Bioadhesiveness and efficient mechanotransduction stimuli synergistically provided by bacterial inclusion bodies as scaffolds for tissue engineering. Nanomedicine (Lond). 2012;7:79-93 pubmed publisher
    Bacterial inclusion bodies (IBs), mechanically stable, submicron protein particles of 50-500 nm dramatically favor mammalian cell spread when used for substrate surface decoration...
  13. Budini M, Buratti E, Stuani C, Guarnaccia C, Romano V, De Conti L, et al. Cellular model of TAR DNA-binding protein 43 (TDP-43) aggregation based on its C-terminal Gln/Asn-rich region. J Biol Chem. 2012;287:7512-25 pubmed publisher
    ..In addition, it will be a powerful tool to test novel therapeutic strategies/effectors aimed at preventing/reducing this phenomenon...
  14. Kim H, Kim N, Wang Y, Scarborough E, Moore J, Diaz Z, et al. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature. 2013;495:467-73 pubmed publisher
    ..Related proteins with PrLDs should therefore be considered candidates for initiating and perhaps propagating proteinopathies of muscle, brain, motor neuron and bone. ..
  15. Mori K, Lammich S, Mackenzie I, Forne I, Zilow S, Kretzschmar H, et al. hnRNP A3 binds to GGGGCC repeats and is a constituent of p62-positive/TDP43-negative inclusions in the hippocampus of patients with C9orf72 mutations. Acta Neuropathol. 2013;125:413-23 pubmed publisher
    ..Thus, we have identified one protein component of these pathognomonic inclusions...
  16. Feng Y, Liu L, Wang J, Liu J, Hu W, Wang X, et al. Integrated refolding techniques for Schistosoma japonicum MTH1 overexpressed as inclusion bodies in Escherichia coli. Protein Expr Purif. 2012;84:181-7 pubmed publisher
    ..5l medium. Integrated refolding techniques proved to be excellent for obtaining the native monomer of S. japonicum MTH1 from inclusion bodies, paving the way for future biological and biophysical studies.
  17. Tanji K, Zhang H, Mori F, Kakita A, Takahashi H, Wakabayashi K. p62/sequestosome 1 binds to TDP-43 in brains with frontotemporal lobar degeneration with TDP-43 inclusions. J Neurosci Res. 2012;90:2034-42 pubmed publisher
    ..Our results suggest that the interaction of TDP-43 and p62 is disrupted and may participate in the pathogenesis of TDP-43 proteinopathy...
  18. Villaverde A, García Fruitós E, Rinas U, Seras Franzoso J, Kosoy A, Corchero J, et al. Packaging protein drugs as bacterial inclusion bodies for therapeutic applications. Microb Cell Fact. 2012;11:76 pubmed publisher
    A growing number of insights on the biology of bacterial inclusion bodies (IBs) have revealed intriguing utilities of these protein particles...
  19. Espargaro A, Villar Piqué A, Sabate R, Ventura S. Yeast prions form infectious amyloid inclusion bodies in bacteria. Microb Cell Fact. 2012;11:89 pubmed publisher
    ..The best-characterized examples are the Sup35 and Ure2 yeast proteins, corresponding to [PSI+] and [URE3] phenotypes, respectively...
  20. Robinson J, Geser F, Stieber A, Umoh M, Kwong L, Van Deerlin V, et al. TDP-43 skeins show properties of amyloid in a subset of ALS cases. Acta Neuropathol. 2013;125:121-31 pubmed publisher
  21. Ogura K, Kobashigawa Y, Saio T, Kumeta H, Torikai S, Inagaki F. Practical applications of hydrostatic pressure to refold proteins from inclusion bodies for NMR structural studies. Protein Eng Des Sel. 2013;26:409-16 pubmed publisher
    ..pressure refolding method was reported as a practical tool for solubilizing and refolding proteins from inclusion bodies; however, there have been only a few applications for protein structural studies...
  22. Neumann M, Valori C, Ansorge O, Kretzschmar H, Munoz D, Kusaka H, et al. Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutations. Acta Neuropathol. 2012;124:705-16 pubmed publisher
    ..Moreover, the absence of Trn1 in ALS-FUS provides further evidence that ALS-FUS and FTLD-FUS have different underlying pathomechanisms...
  23. Collins M, Riascos D, Kovalik T, An J, Krupa K, Krupa K, et al. The RNA-binding motif 45 (RBM45) protein accumulates in inclusion bodies in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration with TDP-43 inclusions (FTLD-TDP) patients. Acta Neuropathol. 2012;124:717-32 pubmed publisher
    ..By confocal microscopy, RBM45 co-localizes with ubiquitin and TDP-43 in inclusion bodies. In neurons containing RBM45 cytoplasmic inclusions we often detected the protein in a punctate pattern ..
  24. Verbeeck C, Deng Q, DeJesus Hernandez M, Taylor G, Ceballos Diaz C, Kocerha J, et al. Expression of Fused in sarcoma mutations in mice recapitulates the neuropathology of FUS proteinopathies and provides insight into disease pathogenesis. Mol Neurodegener. 2012;7:53 pubmed publisher
    ..In this paper we report the development of somatic brain transgenic (SBT) mice using recombinant adeno-associated virus (rAAV) to investigate how FUS mutations lead to neurodegeneration...
  25. Brettschneider J, Van Deerlin V, Robinson J, Kwong L, Lee E, Ali Y, et al. Pattern of ubiquilin pathology in ALS and FTLD indicates presence of C9ORF72 hexanucleotide expansion. Acta Neuropathol. 2012;123:825-39 pubmed publisher
    ..Our study indicates that this pathology is associated with alterations in clinical phenotype, and suggests that the presence of C9ORF72 repeat expansions may indicate a worse prognosis in ALS...
  26. Yamaguchi A, Kitajo K. The effect of PRMT1-mediated arginine methylation on the subcellular localization, stress granules, and detergent-insoluble aggregates of FUS/TLS. PLoS ONE. 2012;7:e49267 pubmed publisher
    ..These findings indicate that PRMT1-mediated arginine methylation could be implicated in the nucleus-cytoplasmic shuttling of FUS/TLS and in the SGs formation and the detergent-insoluble inclusions of ALS-linked FUS/TLS mutants...
  27. Zhu S, Gong C, Ren L, Li X, Song D, Zheng G. A simple and effective strategy for solving the problem of inclusion bodies in recombinant protein technology: His-tag deletions enhance soluble expression. Appl Microbiol Biotechnol. 2013;97:837-45 pubmed publisher
    The formation of inclusion bodies (IBs) in recombinant protein biotechnology has become one of the most frequent undesirable occurrences in both research and industrial applications...
  28. Al Sarraj S, King A, Troakes C, Smith B, Maekawa S, Bodi I, et al. p62 positive, TDP-43 negative, neuronal cytoplasmic and intranuclear inclusions in the cerebellum and hippocampus define the pathology of C9orf72-linked FTLD and MND/ALS. Acta Neuropathol. 2011;122:691-702 pubmed publisher
    ..Our results suggest that proteins other than TDP-43 are binding p62 and aggregating in response to the mutation which may play a mechanistic role in neurodegeneration. ..
  29. Hwang P, Pan J, Sykes B. Targeted expression, purification, and cleavage of fusion proteins from inclusion bodies in Escherichia coli. FEBS Lett. 2014;588:247-52 pubmed publisher
    ..approach to protein production using fusion partners specifically designed to accumulate in insoluble inclusion bodies. The strategy is appropriate for the mass production of short peptides, intrinsically disordered proteins, ..
  30. Daigle J, Lanson N, Smith R, Casci I, Maltare A, Monaghan J, et al. RNA-binding ability of FUS regulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutations. Hum Mol Genet. 2013;22:1193-205 pubmed publisher
    ..In summary, we demonstrate that the RNA-binding ability of FUS is essential for the neurodegenerative phenotype in vivo of mutant FUS (either through direct contact with RNA or through interactions with other RBPs)...
  31. Talafová K, Hrabarova E, Chorvat D, Nahalka J. Bacterial inclusion bodies as potential synthetic devices for pathogen recognition and a therapeutic substance release. Microb Cell Fact. 2013;12:16 pubmed publisher
    ..Currently, glyco-nanomaterials provide potential tool for antimicrobial therapy. We demonstrate that properly glyco-tailored inclusion bodies can specifically bind pathogen adhesins and release therapeutic substances.
  32. Vazquez E, Corchero J, Burgueño J, Seras Franzoso J, Kosoy A, Bosser R, et al. Functional inclusion bodies produced in bacteria as naturally occurring nanopills for advanced cell therapies. Adv Mater. 2012;24:1742-7 pubmed publisher
    b>Inclusion bodies (50-500 nm in diameter) produced in recombinant bacteria can be engineered to contain functional proteins with therapeutic potential...
  33. Klingstedt T, Blechschmidt C, Nogalska A, Prokop S, Häggqvist B, Danielsson O, et al. Luminescent conjugated oligothiophenes for sensitive fluorescent assignment of protein inclusion bodies. Chembiochem. 2013;14:607-16 pubmed publisher
    Small hydrophobic ligands identifying intracellular protein deposits are of great interest, as protein inclusion bodies are the pathological hallmark of several degenerative diseases...
  34. Howard A, Moss B. Formation of orthopoxvirus cytoplasmic A-type inclusion bodies and embedding of virions are dynamic processes requiring microtubules. J Virol. 2012;86:5905-14 pubmed publisher
    ..The data indicate an important role for microtubules in the coalescence of ATIs into larger structures, transport of MVs to ATIs, and embedment of MVs within the ATI matrix...
  35. Mitchell J, McGoldrick P, Vance C, Hortobagyi T, Sreedharan J, Rogelj B, et al. Overexpression of human wild-type FUS causes progressive motor neuron degeneration in an age- and dose-dependent fashion. Acta Neuropathol. 2013;125:273-88 pubmed publisher
    ..Furthermore, these mice will provide a new model to study disease mechanism, and test therapies. ..
  36. Cruts M, Gijselinck I, Van Langenhove T, van der Zee J, Van Broeckhoven C. Current insights into the C9orf72 repeat expansion diseases of the FTLD/ALS spectrum. Trends Neurosci. 2013;36:450-9 pubmed publisher
    ..We review genetic, clinical, and pathological highlights and discuss current insights into the biology of this novel type of repeat expansion disease. ..
  37. Hübener J, Vauti F, Funke C, Wolburg H, Ye Y, Schmidt T, et al. N-terminal ataxin-3 causes neurological symptoms with inclusions, endoplasmic reticulum stress and ribosomal dislocation. Brain. 2011;134:1925-42 pubmed publisher
    ..Consistent with the disease in humans, gene trap mice develop cytoplasmic inclusion bodies and implicate impaired unfolded protein response in the pathogenesis of spinocerebellar ataxia type 3.
  38. Prudencio M, Durazo A, Whitelegge J, Borchelt D. An examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1. Hum Mol Genet. 2010;19:4774-89 pubmed publisher
    ..of the normal SOD1 allele in fALS has potential to influence the toxicity of mutant SOD1 and that complex interactions with the mutant protein may influence the formation of aggregates and inclusion bodies generated by mutant SOD1.
  39. Goedert M, Clavaguera F, Tolnay M. The propagation of prion-like protein inclusions in neurodegenerative diseases. Trends Neurosci. 2010;33:317-25 pubmed publisher
  40. Mahajan V, Klingstedt T, Simon R, Nilsson K, Thueringer A, Kashofer K, et al. Cross ?-sheet conformation of keratin 8 is a specific feature of Mallory-Denk bodies compared with other hepatocyte inclusions. Gastroenterology. 2011;141:1080-1090.e1-7 pubmed publisher
    ..LCOs might be used in diagnosis of liver disorders; they can be applied to formalin-fixed, paraffin-embedded tissues to characterize protein aggregates in liver cells. ..
  41. Waxman E, Giasson B. Characterization of kinases involved in the phosphorylation of aggregated ?-synuclein. J Neurosci Res. 2011;89:231-47 pubmed publisher
  42. Gendron T, Petrucelli L. Rodent models of TDP-43 proteinopathy: investigating the mechanisms of TDP-43-mediated neurodegeneration. J Mol Neurosci. 2011;45:486-99 pubmed publisher
    ..The aim of this review is to highlight the key findings emerging from TDP-43 transgenic animal models and the insight they provide into the mechanisms driving TDP-43-mediated neurodegeneration. ..
  43. Dworeck T, Petri A, Muhammad N, Fioroni M, Schwaneberg U. FhuA deletion variant ?1-159 overexpression in inclusion bodies and refolding with Polyethylene-Poly(ethylene glycol) diblock copolymer. Protein Expr Purif. 2011;77:75-9 pubmed publisher
    ..to the outer membrane was deleted (FhuA ?1-159 ?signal), resulting in protein accumulation in easy to isolate inclusion bodies. Urea was used to solubilise the unfolded protein and dialysis against phosphate-buffer containing the ..
  44. Ito D, Seki M, Tsunoda Y, Uchiyama H, Suzuki N. Nuclear transport impairment of amyotrophic lateral sclerosis-linked mutations in FUS/TLS. Ann Neurol. 2011;69:152-62 pubmed publisher
    ..identified as a cause of familial amyotrophic lateral sclerosis (ALS), as well as a major component of the inclusion bodies found in subtypes of frontotemporal lobar degeneration (FTLD)...
  45. Rank R, Whittimore J, Bowlin A, Wyrick P. In vivo ultrastructural analysis of the intimate relationship between polymorphonuclear leukocytes and the chlamydial developmental cycle. Infect Immun. 2011;79:3291-301 pubmed publisher
  46. Rodríguez Carmona E, Cano Garrido O, Seras Franzoso J, Villaverde A, García Fruitós E. Isolation of cell-free bacterial inclusion bodies. Microb Cell Fact. 2010;9:71 pubmed publisher
    Bacterial inclusion bodies are submicron protein clusters usually found in recombinant bacteria that have been traditionally considered as undesirable products from protein production processes...
  47. Capmany A, Damiani M. Chlamydia trachomatis intercepts Golgi-derived sphingolipids through a Rab14-mediated transport required for bacterial development and replication. PLoS ONE. 2010;5:e14084 pubmed publisher
    ..Novel anti-chlamydial therapies could be developed based on the knowledge of how bacteria subvert host vesicular transport events through Rabs manipulation. ..
  48. Sabate R, de Groot N, Ventura S. Protein folding and aggregation in bacteria. Cell Mol Life Sci. 2010;67:2695-715 pubmed publisher
    ..When these redundant protective strategies are overcome, misfolded polypeptides are recruited into insoluble inclusion bodies. The protein embedded in these intracellular deposits might display different conformations including ..
  49. Bernstein H, Johnson M, Perry R, LeBeau F, Dobrowolny H, Bogerts B, et al. Partial loss of parvalbumin-containing hippocampal interneurons in dementia with Lewy bodies. Neuropathology. 2011;31:1-10 pubmed publisher
    ..It remains to be elucidated if the numerical decrease of this particular subset of hippocampal interneurons has consequences for the gamma (20-80 Hz) frequency activity in DLB patients. ..
  50. Lajoie P, Snapp E. Formation and toxicity of soluble polyglutamine oligomers in living cells. PLoS ONE. 2010;5:e15245 pubmed publisher
    ..mHtt) and other polyglutamine expansion mutant proteins exist as monomers, soluble oligomers, and insoluble inclusion bodies (IBs). Determining which of these forms constitute a toxic species has proven difficult...
  51. Leite J, da Fonseca F, de Souza Trindade G, Abrahão J, Arantes R, de Almeida Leite C, et al. A-type inclusion bodies: a factor influencing cowpox virus lesion pathogenesis. Arch Virol. 2011;156:617-28 pubmed publisher
    The family Poxviridae comprises the most complex animal DNA viruses. During some poxvirus infections, A-type inclusion bodies (ATIs), codified by the ati gene, are produced...
  52. Gamerdinger M, Kaya A, Wolfrum U, Clement A, Behl C. BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins. EMBO Rep. 2011;12:149-56 pubmed publisher
    ..Notably, aggresome-targeting by BAG3 is distinct from previously described mechanisms, as it does not depend on substrate ubiquitination...
  53. Dasari M, Espargaro A, Sabate R, Lopez Del Amo J, Fink U, Grelle G, et al. Bacterial inclusion bodies of Alzheimer's disease ?-amyloid peptides can be employed to study native-like aggregation intermediate states. Chembiochem. 2011;12:407-23 pubmed publisher
    ..Bacterial inclusion bodies contain large amounts of small heat shock proteins (sHSPs), which are highly homologous to those found in the ..
  54. Cohen T, Lee V, Trojanowski J. TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies. Trends Mol Med. 2011;17:659-67 pubmed publisher
    ..Finally, we review current mouse models of TDP-43 and discuss their similarities and potential relevance to human TDP-43 proteinopathies including ALS and FTLD-TDP...
  55. Parrilli E, Giuliani M, Marino G, Tutino M. Influence of production process design on inclusion bodies protein: the case of an Antarctic flavohemoglobin. Microb Cell Fact. 2010;9:19 pubmed publisher
    Protein over-production in Escherichia coli often results in formation of inclusion bodies (IBs)...
  56. de Albuquerque J, Keim C, Lins U. Comparative analysis of Beggiatoa from hypersaline and marine environments. Micron. 2010;41:507-17 pubmed publisher
    ..We observed that cell envelopes from narrow Beggiatoa consist of five layers, whereas cell envelopes from large trichomes contain four layers...
  57. Hagen M, Murrell J, Delisle M, Andermann E, Andermann F, Guiot M, et al. Encephalopathy with neuroserpin inclusion bodies presenting as progressive myoclonus epilepsy and associated with a novel mutation in the Proteinase Inhibitor 12 gene. Brain Pathol. 2011;21:575-82 pubmed publisher
    ..In summary, we report a case of neuroserpin encephalopathy associated with a novel PI12 mutation and complicated by coexistent multiple sclerosis...
  58. Tsumoto K, Abe R, Ejima D, Arakawa T. Non-denaturing solubilization of inclusion bodies. Curr Pharm Biotechnol. 2010;11:309-12 pubmed
    It has been a conventional notion that cytoplasmic recombinant expression leads to either soluble protein or inclusion bodies. In the latter case, it was always assumed that proteins in inclusion bodies (IBs) are more or less unfolded and ..
  59. Mitraki A. Protein aggregation from inclusion bodies to amyloid and biomaterials. Adv Protein Chem Struct Biol. 2010;79:89-125 pubmed publisher
    b>Inclusion bodies and amyloid are two different outcomes of the same fundamental biological process: protein aggregation...
  60. Nonaka T, Watanabe S, Iwatsubo T, Hasegawa M. Seeded aggregation and toxicity of {alpha}-synuclein and tau: cellular models of neurodegenerative diseases. J Biol Chem. 2010;285:34885-98 pubmed publisher
    ..Our cellular models thus provide evidence of nucleation-dependent and protein-specific polymerization of intracellular amyloid-like proteins in cultured cells...
  61. Peternel S, Komel R. Isolation of biologically active nanomaterial (inclusion bodies) from bacterial cells. Microb Cell Fact. 2010;9:66 pubmed publisher
    In recent years bacterial inclusion bodies (IBs) were recognised as highly pure deposits of active proteins inside bacterial cells...
  62. Mital J, Miller N, Fischer E, Hackstadt T. Specific chlamydial inclusion membrane proteins associate with active Src family kinases in microdomains that interact with the host microtubule network. Cell Microbiol. 2010;12:1235-49 pubmed publisher
    ..Together, the data suggest that a specific structure on the C. trachomatis inclusion membrane may be responsible for the known interactions of chlamydiae with the microtubule network and resultant effects on centrosome stability. ..
  63. Ichimura Y, Komatsu M. Selective degradation of p62 by autophagy. Semin Immunopathol. 2010;32:431-6 pubmed publisher
    ..In this review, we discuss the physiological roles of the selective turnover of p62 by autophagy and their molecular mechanisms...
  64. Yamada T, Sunagawa K, Homma T, Uehara K, Mizutani T, Kawabata Y. Ubiquitin-positive pneumocytes and inclusion bodies are present in secondary organizing pneumonia. Intern Med. 2011;50:277-83 pubmed
    ..In the present study, we examined tissues with the organizing pneumonia pattern (OP) to determine if they contain inclusions and Ub+ pneumocytes using lobectomized specimens...
  65. Gatti Lafranconi P, Natalello A, Ami D, Doglia S, Lotti M. Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology. FEBS J. 2011;278:2408-18 pubmed publisher
    ..As a result, in the bacterial cytoplasm several recombinant proteins aggregate as insoluble inclusion bodies. The recent discovery that aggregated proteins can retain native-like conformation and biological activity ..
  66. García Fruitós E, Sabate R, de Groot N, Villaverde A, Ventura S. Biological role of bacterial inclusion bodies: a model for amyloid aggregation. FEBS J. 2011;278:2419-27 pubmed publisher
    b>Inclusion bodies are insoluble protein aggregates usually found in recombinant bacteria when they are forced to produce heterologous protein species...
  67. Waxman E, Giasson B. A novel, high-efficiency cellular model of fibrillar alpha-synuclein inclusions and the examination of mutations that inhibit amyloid formation. J Neurochem. 2010;113:374-88 pubmed publisher
    ..This novel high-efficiency cellular model of alpha-syn aggregation is a valuable system that may be used to further understand alpha-syn aggregation and allow for the generation of future therapeutics...