Page 1 | Search Results | Biochemical Journal

1-32 of 32

Sort by

Sort Order Select

Articles

A central role for amyloid fibrin microclots in long COVID/PASC: origins and therapeutic implications

In Collection

Coronavirus

Douglas B. Kell, Gert Jacobus Laubscher, Etheresia Pretorius

Biochem J (2022) 479 (4): 537–559.

https://doi.org/10.1042/BCJ20220016

Published: 23 February 2022

... this syndrome as a separate disease entity, and refer to it under the broad terminology of ‘COVID’, although its demographics are quite different from those of acute COVID-19. A few years ago, we discovered that fibrinogen in blood can clot into an anomalous ‘amyloid’ form of fibrin that (like other β-rich...

View article titled, A central role for amyloid fibrin microclots in long COVID/PASC: origins and therapeutic implications

Articles

The kinetics of islet amyloid polypeptide phase-separated system and hydrogel formation are critically influenced by macromolecular crowding

Lior Pytowski, David J. Vaux, Létitia Jean

Biochem J (2021) 478 (15): 3025–3046.

https://doi.org/10.1042/BCJ20210384

Published: 13 August 2021

...Lior Pytowski; David J. Vaux; Létitia Jean Many protein misfolding diseases (e.g. type II diabetes and Alzheimer's disease) are characterised by amyloid deposition. Human islet amyloid polypeptide (hIAPP, involved in type II diabetes) spontaneously undergoes liquid–liquid phase separation (LLPS...

View article titled, The kinetics of islet amyloid polypeptide phase-separated system and hydrogel formation are critically influenced by macromolecular crowding

Includes: Multimedia, Supplementary data

Articles

Scutellarin inhibits the uninduced and metal-induced aggregation of α-Synuclein and disaggregates preformed fibrils: implications for Parkinson's disease

Fatima Kamal Zaidi, Shashank Deep

Biochem J (2020) 477 (3): 645–670.

https://doi.org/10.1042/BCJ20190705

Published: 11 February 2020

... in seperate sets. The samples withdrawn after ∼54 h were centrifuged (14 000 rpm/30 min), the pellet washed with PBS and the process was repeated a couple of times to remove the unbound metal ions as well as scutellarin. The resulting amyloid fibrils, Fe 3+ and Al 3+ generated aggregates, scutellarin...

View article titled, Scutellarin inhibits the uninduced and metal-induced aggregation of α-Synuclein and disaggregates preformed fibrils: implications for Parkinson's disease

Includes: Supplementary data

Articles

Biophysical characterization of p53 core domain aggregates

Igor Lima, Ambuja Navalkar, Samir K. Maji, Jerson L. Silva, Guilherme A.P. de Oliveira, Elio A. Cino

Biochem J (2020) 477 (1): 111–120.

https://doi.org/10.1042/BCJ20190778

Published: 08 January 2020

..., such as oligomers and amyloid fibrils. p53 is an essential tumor suppressor that is prone to such conformational transitions, resulting in its compromised ability to avert cancer. This work explores the biophysical properties of early-, mid-, and late-stage p53 core domain (p53C) aggregates. Atomistic and coarse...

View article titled, Biophysical characterization of p53 core domain aggregates

Articles

The growth of amyloid fibrils: rates and mechanisms

In Collection

Editors' pick of review article highlights published in the Biochemical Journal in 2018 & 2019

Alexander K. Buell

Biochem J (2019) 476 (19): 2677–2703.

https://doi.org/10.1042/BCJ20160868

Published: 11 October 2019

...Alexander K. Buell Amyloid fibrils are β -sheet-rich linear protein polymers that can be formed by a large variety of different proteins. These assemblies have received much interest in recent decades, due to their role in a range of human disorders. However, amyloid fibrils are also found...

View article titled, The growth of amyloid fibrils: rates and mechanisms

Articles

ADS-J1 disaggregates semen-derived amyloid fibrils

Jinqing Li, Zichao Yang, Han Liu, Mengjie Qiu, Tingting Zhang, Wenjuan Li, Zhaofeng Li, Tao Qi, Yurong Qiu, Lin Li, Xuefeng Zhou, Shuwen Liu, Suiyi Tan

Biochem J (2019) 476 (6): 1021–1035.

https://doi.org/10.1042/BCJ20180886

Published: 29 March 2019

...Jinqing Li; Zichao Yang; Han Liu; Mengjie Qiu; Tingting Zhang; Wenjuan Li; Zhaofeng Li; Tao Qi; Yurong Qiu; Lin Li; Xuefeng Zhou; Shuwen Liu; Suiyi Tan Semen-derived amyloid fibrils, comprising SEVI (semen-derived enhancer of viral infection) fibrils and SEM1 fibrils, could remarkably enhance HIV-1...

View article titled, ADS-J1 disaggregates semen-derived amyloid fibrils

Articles

Azadirachtin inhibits amyloid formation, disaggregates pre-formed fibrils and protects pancreatic β-cells from human islet amyloid polypeptide/amylin-induced cytotoxicity

Richa Dubey, Ketaki Patil, Sarath C. Dantu, Devika M. Sardesai, Parnika Bhatia, Nikita Malik, Jhankar D. Acharya, Soham Sarkar, Soumadwip Ghosh, Rajarshi Chakrabarti, Shilpy Sharma, Ashutosh Kumar

Biochem J (2019) 476 (5): 889–907.

https://doi.org/10.1042/BCJ20180820

Published: 15 March 2019

...Richa Dubey; Ketaki Patil; Sarath C. Dantu; Devika M. Sardesai; Parnika Bhatia; Nikita Malik; Jhankar D. Acharya; Soham Sarkar; Soumadwip Ghosh; Rajarshi Chakrabarti; Shilpy Sharma; Ashutosh Kumar The human islet amyloid polypeptide (hIAPP) or amylin is the major constituent of amyloidogenic...

View article titled, Azadirachtin inhibits amyloid formation, disaggregates pre-formed fibrils and protects pancreatic β-cells from human islet amyloid polypeptide/amylin-induced cytotoxicity

Includes: Supplementary data

Articles

Multiphasic effect of vinyl pyrrolidone polymers on amyloidogenesis, from macromolecular crowding to inhibition

Richard Berwick, David J. Vaux, Létitia Jean

Biochem J (2018) 475 (21): 3417–3436.

https://doi.org/10.1042/BCJ20180715

Published: 09 November 2018

...Richard Berwick; David J. Vaux; Létitia Jean Deposition of misfolded amyloid polypeptides, associated with cell death, is the hallmark of many degenerative diseases (e.g. type II diabetes mellitus and Alzheimer's disease). In vivo , cellular and extracellular spaces are occupied by a high volume...

View article titled, Multiphasic effect of vinyl pyrrolidone polymers on amyloidogenesis, from macromolecular crowding to inhibition

Includes: Supplementary data

Articles

Recombinant human islet amyloid polypeptide forms shorter fibrils and mediates β-cell apoptosis via generation of oxidative stress

Richa Dubey, Pooja Minj, Nikita Malik, Devika M. Sardesai, Shruti H. Kulkarni, Jhankar D. Acharya, Neel Sarovar Bhavesh, Shilpy Sharma, Ashutosh Kumar

Biochem J (2017) 474 (23): 3915–3934.

https://doi.org/10.1042/BCJ20170323

Published: 16 November 2017

... (T2DM). The human islet amyloid polypeptide (hIAPP) forms amyloid plaques in the pancreas of T2DM subjects (>95%) that are involved in deteriorating islet function and in mediating β - cell apoptosis. However, the detailed mechanism of action, structure and nature of toxic hIAPP species responsible...

View article titled, Recombinant human islet amyloid polypeptide forms shorter fibrils and mediates β-cell apoptosis via generation of oxidative stress

Includes: Supplementary data

Articles

Sialylated glycosylphosphatidylinositols suppress the production of toxic amyloid-β oligomers

William Nolan, Harriet McHale-Owen, Clive Bate

Biochem J (2017) 474 (17): 3045–3058.

https://doi.org/10.1042/BCJ20170239

Published: 22 August 2017

...William Nolan; Harriet McHale-Owen; Clive Bate The production of amyloid-β (Aβ) is a key factor driving pathogenesis in Alzheimer's disease (AD). Increasing concentrations of soluble Aβ oligomers within the brain lead to synapse degeneration and the progressive dementia characteristic of AD. Since...

View article titled, Sialylated glycosylphosphatidylinositols suppress the production of toxic amyloid-β oligomers

Articles

Effect of position-specific single-point mutations and biophysical characterization of amyloidogenic peptide fragments identified from lattice corneal dystrophy patients

Venkatraman Anandalakshmi, Elavazhagan Murugan, Eunice Goh Tze Leng, Lim Wei Ting, Shyam S. Chaurasia, Toshio Yamazaki, Toshio Nagashima, Benjamin Lawrence George, Gary Swee Lim Peh, Konstantin Pervushin, Rajamani Lakshminarayanan, Jodhbir S. Mehta

Biochem J (2017) 474 (10): 1705–1725.

https://doi.org/10.1042/BCJ20170125

Published: 09 May 2017

..., morphological features of deposits (amyloid, amorphous powder or a mixture of both forms) and the severity of disease presentation. It has been suggested that abnormal turnover and aberrant proteolytic processing of the mutant proteins result in the accumulation of insoluble protein deposits. Using mass...

View article titled, Effect of position-specific single-point mutations and biophysical characterization of amyloidogenic peptide fragments identified from lattice corneal dystrophy patients

Includes: Supplementary data

Articles

Modulation of prion polymerization and toxicity by rationally designed peptidomimetics

Ankit Srivastava, Sakshi Sharma, Sandhya Sadanandan, Sakshi Gupta, Jasdeep Singh, Sarika Gupta, V. Haridas, Bishwajit Kundu

Biochem J (2017) 474 (1): 123–147.

https://doi.org/10.1042/BCJ20160737

Published: 22 December 2016

...@chemistry.iitd.ac.in ) or Bishwajit Kundu ( bkundu@bioschool.iitd.ac.in ) 6 8 2016 25 10 2016 31 10 2016 1 11 2016 © 2017 The Author(s); published by Portland Press Limited on behalf of the Biochemical Society 2017 amyloid bispidine cytotoxicity oligomer prion protein misfolding...

View article titled, Modulation of prion polymerization and toxicity by rationally designed peptidomimetics

Includes: Supplementary data

Articles

BRICHOS binds to a designed amyloid-forming β-protein and reduces proteasomal inhibition and aggresome formation

Lisa Dolfe, Bengt Winblad, Jan Johansson, Jenny Presto

Biochem J (2016) 473 (2): 167–178.

https://doi.org/10.1042/BJ20150920

Published: 05 January 2016

...Lisa Dolfe; Bengt Winblad; Jan Johansson; Jenny Presto The BRICHOS domain is associated with proliferative, degenerative and amyloid diseases, and it has been shown to inhibit fibril formation and toxicity of the Alzheimer's disease-associated amyloid β-peptide. ProSP-C (prosurfactant protein C...

View article titled, BRICHOS binds to a designed amyloid-forming β-protein and reduces proteasomal inhibition and aggresome formation

Includes: Supplementary data

Articles

Distinct higher-order α-synuclein oligomers induce intracellular aggregation

Eva Illes-Toth, Mafalda Ribeiro Ramos, Roberto Cappai, Caroline Dalton, David P Smith

Biochem J (2015) 468 (3): 485–493.

https://doi.org/10.1042/BJ20150159

Published: 15 June 2015

... been linked to soluble amyloid oligomer populations that precede Lewy body formation. Oligomers produced in vitro under certain conditions have been demonstrated to induce intracellular aggregation in cell culture models. In the present study, we characterize, by ESI–ion mobility spectrometry (IMS)–MS...

View article titled, Distinct higher-order α-synuclein oligomers induce intracellular aggregation

Includes: Supplementary data

Articles

Cu 2+ accentuates distinct misfolding of Aβ (1–40) and Aβ (1–42) peptides, and potentiates membrane disruption

Christian J. Matheou, Nadine D. Younan, John H. Viles

Biochem J (2015) 466 (2): 233–242.

https://doi.org/10.1042/BJ20141168

Published: 20 February 2015

...Christian J. Matheou; Nadine D. Younan; John H. Viles Central to Alzheimer's disease is the misfolding of amyloid-beta (Aβ) peptide, which generates an assorted population of amorphous aggregates, oligomers and fibres. Metal ion homoeostasis is disrupted in the brains of sufferers of Alzheimer's...

View article titled, Cu 2+ accentuates distinct misfolding of Aβ (1–40) and Aβ (1–42) peptides, and potentiates membrane disruption

Articles

Specific aromatic foldamers potently inhibit spontaneous and seeded Aβ42 and Aβ43 fibril assembly

Katelyn M. Seither, Heather A. McMahon, Nikita Singh, Hejia Wang, Mimi Cushman-Nick, Geronda L. Montalvo, William F. DeGrado, James Shorter

Biochem J (2014) 464 (1): 85–98.

https://doi.org/10.1042/BJ20131609

Published: 23 October 2014

...Katelyn M. Seither; Heather A. McMahon; Nikita Singh; Hejia Wang; Mimi Cushman-Nick; Geronda L. Montalvo; William F. DeGrado; James Shorter Amyloid fibrils are self-propagating entities that spread pathology in several devastating disorders including Alzheimer's disease (AD). In AD, amyloid-β (Aβ...

View article titled, Specific aromatic foldamers potently inhibit spontaneous and seeded Aβ42 and Aβ43 fibril assembly

Articles

Exploring the sequence–structure relationship for amyloid peptides

Kyle L. Morris, Alison Rodger, Matthew R. Hicks, Maya Debulpaep, Joost Schymkowitz, Frederic Rousseau, Louise C. Serpell

Biochem J (2013) 450 (2): 275–283.

https://doi.org/10.1042/BJ20121773

Published: 15 February 2013

...Kyle L. Morris; Alison Rodger; Matthew R. Hicks; Maya Debulpaep; Joost Schymkowitz; Frederic Rousseau; Louise C. Serpell Amyloid fibril formation is associated with misfolding diseases, as well as fulfilling a functional role. The cross-β molecular architecture has been reported in increasing...

View article titled, Exploring the sequence–structure relationship for amyloid peptides

Includes: Supplementary data

Articles

Ca 2+ enhances Aβ polymerization rate and fibrillar stability in a dynamic manner

Kristoffer Brännström, Anders Öhman, Malin Lindhagen-Persson, Anders Olofsson

Biochem J (2013) 450 (1): 189–197.

https://doi.org/10.1042/BJ20121583

Published: 24 January 2013

...Kristoffer Brännström; Anders Öhman; Malin Lindhagen-Persson; Anders Olofsson Identifying factors that affect the self-assembly of Aβ (amyloid-β peptide) is of utmost importance in the quest to understand the molecular mechanisms causing AD (Alzheimer's disease). Ca 2+ has previously been shown...

View article titled, Ca 2+ enhances Aβ polymerization rate and fibrillar stability in a dynamic manner

Articles

Flexibility of the Ure2 prion domain is important for amyloid fibril formation

Yong Yu, Hai-Yan Wang, Ming Bai, Sarah Perrett

Biochem J (2011) 434 (1): 143–151.

https://doi.org/10.1042/BJ20101895

Published: 27 January 2011

...Yong Yu; Hai-Yan Wang; Ming Bai; Sarah Perrett Ure2, the protein determinant of the Saccharomyces cerevisiae prion [ URE3 ], has a natively disordered N-terminal domain that is important for prion formation in vivo and amyloid formation in vitro ; the globular C-domain has a glutathione transferase...

View article titled, Flexibility of the Ure2 prion domain is important for amyloid fibril formation

Articles

Mutations linked to interstitial lung disease can abrogate anti-amyloid function of prosurfactant protein C

Charlotte Nerelius, Emily Martin, Siwei Peng, Magnus Gustafsson, Kerstin Nordling, Timothy Weaver, Jan Johansson

Biochem J (2008) 416 (2): 201–209.

https://doi.org/10.1042/BJ20080981

Published: 12 November 2008

... in mature SP-C. In the present study, we showed that: (i) human embryonic kidney cells expressing the ILD-associated mutants proSP-C L188Q and proSP-C ΔExon4 accumulate Congo Red-positive amyloid-like inclusions, whereas cells transfected with the mutant proSP-C I73T do not; (ii) transfection of CTC...

View article titled, Mutations linked to interstitial lung disease can abrogate anti-amyloid function of prosurfactant protein C

Articles

Effect of glycosylation on the extracellular domain of the Ag43 bacterial autotransporter: enhanced stability and reduced cellular aggregation

Stine K. Knudsen, Allan Stensballe, Magnus Franzmann, Uffe B. Westergaard, Daniel E. Otzen

Biochem J (2008) 412 (3): 563–577.

https://doi.org/10.1042/BJ20071497

Published: 28 May 2008

..., glycosylation also reduces the stabilizing effect of Ca 2+ ions, removes the ability of Ca 2+ to promote cell adhesion, reduces the ability of Ag43α-containing cells to form bacterial amyloid and increases the susceptibility of the resulting amyloid to proteolysis. In addition, our results indicate that Ag43α...

View article titled, Effect of glycosylation on the extracellular domain of the Ag43 bacterial autotransporter: enhanced stability and reduced cellular aggregation

Articles

Intracellular copper deficiency increases amyloid-β secretion by diverse mechanisms

Michael A. Cater, Kelly T. McInnes, Qiao-Xin Li, Irene Volitakis, Sharon La Fontaine, Julian F. B. Mercer, Ashley I. Bush

Biochem J (2008) 412 (1): 141–152.

https://doi.org/10.1042/BJ20080103

Published: 25 April 2008

...Michael A. Cater; Kelly T. McInnes; Qiao-Xin Li; Irene Volitakis; Sharon La Fontaine; Julian F. B. Mercer; Ashley I. Bush In Alzheimer's disease there is abnormal brain copper distribution, with accumulation of copper in amyloid plaques and a deficiency of copper in neighbouring cells. Excess...

View article titled, Intracellular copper deficiency increases amyloid-β secretion by diverse mechanisms

Articles

Comparative in vitro and ex vivo activities of selected inhibitors of transthyretin aggregation: relevance in drug design

Isabel Cardoso, Maria Rosário Almeida, Nelson Ferreira, Gemma Arsequell, Gregorio Valencia, Maria João Saraiva

Biochem J (2007) 408 (1): 131–138.

https://doi.org/10.1042/BJ20070689

Published: 29 October 2007

...Isabel Cardoso; Maria Rosário Almeida; Nelson Ferreira; Gemma Arsequell; Gregorio Valencia; Maria João Saraiva Destabilization of the tetrameric fold of TTR (transthyretin) is important for aggregation of the protein which culminates in amyloid fibril formation. Many TTR mutations interfere...

View article titled, Comparative in vitro and ex vivo activities of selected inhibitors of transthyretin aggregation: relevance in drug design

Articles

Differential modulation of Alzheimer's disease amyloid β-peptide accumulation by diverse classes of metal ligands

Aphrodite Caragounis, Tai Du, Gulay Filiz, Katrina M. Laughton, Irene Volitakis, Robyn A. Sharples, Robert A. Cherny, Colin L. Masters, Simon C. Drew, Andrew F. Hill, Qiao-Xin Li, Peter J. Crouch, Kevin J. Barnham, Anthony R. White

Biochem J (2007) 407 (3): 435–450.

https://doi.org/10.1042/BJ20070579

Published: 12 October 2007

... investigated. We previously reported that CQ–metal complexes up-regulated MMP (matrix metalloprotease) activity in vitro by activating PI3K (phosphoinositide 3-kinase) and JNK (c-jun N-terminal kinase), and that the increased MMP activity resulted in enhanced degradation of secreted Aβ (amyloid β) peptide...

View article titled, Differential modulation of Alzheimer's disease amyloid β-peptide accumulation by diverse classes of metal ligands

Articles

Mimicking phosphorylation of αB-crystallin affects its chaperone activity

Heath Ecroyd, Sarah Meehan, Joseph Horwitz, J. Andrew Aquilina, Justin L. P. Benesch, Carol V. Robinson, Cait E. Macphee, John A. Carver

Biochem J (2007) 401 (1): 129–141.

https://doi.org/10.1042/BJ20060981

Published: 11 December 2006

... these mimics to undertake a mechanistic and structural invest-igation of the effect of phosphorylation on the chaperone activity of αB-crystallin to protect against two types of protein misfolding, i.e. amorphous aggregation and amyloid fibril assembly. We show that mimicking phosphorylation of αB-crystallin...

View article titled, Mimicking phosphorylation of αB-crystallin affects its chaperone activity

Articles

Binding of amyloid β-peptide to ganglioside micelles is dependent on histidine-13

Mike P. Williamson, Yu Suzuki, Nathan T. Bourne, Tetsuo Asakura

Biochem J (2006) 397 (3): 483–490.

https://doi.org/10.1042/BJ20060293

Published: 13 July 2006

...Mike P. Williamson; Yu Suzuki; Nathan T. Bourne; Tetsuo Asakura Amyloid β-peptide (Aβ) is a major component of plaques in Alzheimer's disease, and formation of senile plaques has been suggested to originate from regions of neuronal membrane rich in gangliosides. Here we demonstrate using NMR on 15...

View article titled, Binding of amyloid β-peptide to ganglioside micelles is dependent on histidine-13

Articles

The in situ observation of the temperature and pressure stability of recombinant Aspergillus aculeatus pectin methylesterase with Fourier transform IR spectroscopy reveals an unusual pressure stability of β-helices

Carolien Dirix, Thomas Duvetter, Ann Van Loey, Marc Hendrickx, Karel Heremans

Biochem J (2005) 392 (3): 565–571.

https://doi.org/10.1042/BJ20050721

Published: 06 December 2005

... above 60 °C were necessary to cause significant PME unfolding and loss of activity. These results may be relevant for an understanding of the extreme stability of amyloid fibrils for which β-helices have been proposed as a structural element. 1 These authors contributed equally to this work...

View article titled, The in situ observation of the temperature and pressure stability of recombinant Aspergillus aculeatus pectin methylesterase with Fourier transform IR spectroscopy reveals an unusual pressure stability of β-helices

Articles

Argpyrimidine, a methylglyoxal-derived advanced glycation end-product in familial amyloidotic polyneuropathy

Ricardo GOMES, Marta SOUSA SILVA, Alexandre QUINTAS, Carlos CORDEIRO, António FREIRE, Paulino PEREIRA, Américo MARTINS, Estela MONTEIRO, Eduardo BARROSO, Ana PONCES FREIRE

Biochem J (2005) 385 (2): 339–345.

https://doi.org/10.1042/BJ20040833

Published: 07 January 2005

...Ricardo GOMES; Marta SOUSA SILVA; Alexandre QUINTAS; Carlos CORDEIRO; António FREIRE; Paulino PEREIRA; Américo MARTINS; Estela MONTEIRO; Eduardo BARROSO; Ana PONCES FREIRE FAP (familial amyloidotic polyneuropathy) is a systemic amyloid disease characterized by the formation of extracellular...

View article titled, Argpyrimidine, a methylglyoxal-derived advanced glycation end-product in familial amyloidotic polyneuropathy

Articles

Selective binding to transthyretin and tetramer stabilization in serum from patients with familial amyloidotic polyneuropathy by an iodinated diflunisal derivative

Maria Rosário ALMEIDA, Bárbara MACEDO, Isabel CARDOSO, Isabel ALVES, Gregorio VALENCIA, Gemma ARSEQUELL, Antoni PLANAS, Maria João SARAIVA

Biochem J (2004) 381 (2): 351–356.

https://doi.org/10.1042/BJ20040011

Published: 06 July 2004

...Maria Rosário ALMEIDA; Bárbara MACEDO; Isabel CARDOSO; Isabel ALVES; Gregorio VALENCIA; Gemma ARSEQUELL; Antoni PLANAS; Maria João SARAIVA In familial amyloidotic polyneuropathy, TTR (transthyretin) variants are deposited as amyloid fibrils. It is thought that this process involves TTR tetramer...

View article titled, Selective binding to transthyretin and tetramer stabilization in serum from patients with familial amyloidotic polyneuropathy by an iodinated diflunisal derivative

Articles

Designing transthyretin mutants affecting tetrameric structure: implications in amyloidogenicity

Clara REDONDO, Ana M. DAMAS, Maria João M. SARAIVA

Biochem J (2000) 348 (1): 167–172.

https://doi.org/10.1042/bj3480167

Published: 09 May 2000

...Clara REDONDO; Ana M. DAMAS; Maria João M. SARAIVA The molecular mechanisms that convert soluble transthyretin (TTR) tetramers into insoluble amyloid fibrils are still unknown; dissociation of the TTR tetramer is a pre-requisite for amyloid formation in vitro and involvement of monomers...

View article titled, Designing transthyretin mutants affecting tetrameric structure: implications in amyloidogenicity

Articles

Molecular determinants of the physicochemical properties of a critical prion protein region comprising residues 106–126

Mario SALMONA, Paolo MALESANI, Luca DE GIOIA, Stefano GORLA, Maurizio BRUSCHI, Antonio MOLINARI, Franco DELLA VEDOVA, Barbara PEDROTTI, Maria Anna MARRARI, Tazeen AWAN, Orso BUGIANI, Gianluigi FORLONI, Fabrizio TAGLIAVINI

Biochem J (1999) 342 (1): 207–214.

https://doi.org/10.1042/bj3420207

Published: 10 August 1999

... analogues showed the following. (1) His 111 is central to the conformational changes of PrP peptides. (2) Amidation of the C-terminal Gly 126 yields a predominantly random coil structure, abolishes the molecular polymorphism and decreases the propensity of PrP106-126 to generate amyloid fibrils. (3) PrP106...

View article titled, Molecular determinants of the physicochemical properties of a critical prion protein region comprising residues 106–126

Articles

Effects of the amyloid precursor protein Glu693→Gln ‘Dutch’ mutation on the production and stability of amyloid β-protein

Deborah J. WATSON, Dennis J. SELKOE, David B. TEPLOW

Biochem J (1999) 340 (3): 703–709.

https://doi.org/10.1042/bj3400703

Published: 08 June 1999

... the amyloid precursor protein (APP), resulting in a Glu → Gln amino acid substitution at position 22 of the amyloid β-protein (Aβ) region. The pathogenetic mechanisms of HCHWA-D are unknown but could involve alterations in the proteolytic processing of APP and in amyloid fibril formation. We examined Aβ...

View article titled, Effects of the amyloid precursor protein Glu693→Gln ‘Dutch’ mutation on the production and stability of amyloid β-protein

NARROW

Filters

A central role for amyloid fibrin microclots in long COVID/PASC: origins and therapeutic implications

The kinetics of islet amyloid polypeptide phase-separated system and hydrogel formation are critically influenced by macromolecular crowding

Scutellarin inhibits the uninduced and metal-induced aggregation of α-Synuclein and disaggregates preformed fibrils: implications for Parkinson's disease

Biophysical characterization of p53 core domain aggregates

The growth of amyloid fibrils: rates and mechanisms

ADS-J1 disaggregates semen-derived amyloid fibrils

Azadirachtin inhibits amyloid formation, disaggregates pre-formed fibrils and protects pancreatic β-cells from human islet amyloid polypeptide/amylin-induced cytotoxicity

Multiphasic effect of vinyl pyrrolidone polymers on amyloidogenesis, from macromolecular crowding to inhibition

Recombinant human islet amyloid polypeptide forms shorter fibrils and mediates β-cell apoptosis via generation of oxidative stress

Sialylated glycosylphosphatidylinositols suppress the production of toxic amyloid-β oligomers

Effect of position-specific single-point mutations and biophysical characterization of amyloidogenic peptide fragments identified from lattice corneal dystrophy patients

Modulation of prion polymerization and toxicity by rationally designed peptidomimetics

BRICHOS binds to a designed amyloid-forming β-protein and reduces proteasomal inhibition and aggresome formation

Distinct higher-order α-synuclein oligomers induce intracellular aggregation

Cu 2+ accentuates distinct misfolding of Aβ (1–40) and Aβ (1–42) peptides, and potentiates membrane disruption

Specific aromatic foldamers potently inhibit spontaneous and seeded Aβ42 and Aβ43 fibril assembly

Exploring the sequence–structure relationship for amyloid peptides

Ca 2+ enhances Aβ polymerization rate and fibrillar stability in a dynamic manner

Flexibility of the Ure2 prion domain is important for amyloid fibril formation

Mutations linked to interstitial lung disease can abrogate anti-amyloid function of prosurfactant protein C

Effect of glycosylation on the extracellular domain of the Ag43 bacterial autotransporter: enhanced stability and reduced cellular aggregation

Intracellular copper deficiency increases amyloid-β secretion by diverse mechanisms

Comparative in vitro and ex vivo activities of selected inhibitors of transthyretin aggregation: relevance in drug design

Differential modulation of Alzheimer's disease amyloid β-peptide accumulation by diverse classes of metal ligands

Mimicking phosphorylation of αB-crystallin affects its chaperone activity

Binding of amyloid β-peptide to ganglioside micelles is dependent on histidine-13

The in situ observation of the temperature and pressure stability of recombinant Aspergillus aculeatus pectin methylesterase with Fourier transform IR spectroscopy reveals an unusual pressure stability of β-helices

Argpyrimidine, a methylglyoxal-derived advanced glycation end-product in familial amyloidotic polyneuropathy

Selective binding to transthyretin and tetramer stabilization in serum from patients with familial amyloidotic polyneuropathy by an iodinated diflunisal derivative

Designing transthyretin mutants affecting tetrameric structure: implications in amyloidogenicity

Molecular determinants of the physicochemical properties of a critical prion protein region comprising residues 106–126

Effects of the amyloid precursor protein Glu693→Gln ‘Dutch’ mutation on the production and stability of amyloid β-protein

Email alerts

CONNECT

EXPLORE

Email alerts

CONNECT

EXPLORE

This Feature Is Available To Subscribers Only