Cucurbit[8]uril Reactivation of an Inactivated Caspase‐8 Mutant Reveals Differentiated Enzymatic Substrate Processing

Authors: Dung T. Dang, Arthur H. A. M. van Onzen, Yvonne L. Dorland, Luc Brunsveld

Source: Chembiochem

Subject Terms: Bridged-Ring Compounds, 0301 basic medicine, Caspase 8, Caspase 8/genetics, Imidazoles, protein assembly, protein engineering, Full Papers, Protein Multimerization/drug effects, 01 natural sciences, supramolecular chemistry, Catalysis, 0104 chemical sciences, Catalysis/drug effects, 03 medical and health sciences, Enzyme Reactivators, caspases, cucurbit[8]uril, Enzyme Reactivators/chemistry, Imidazoles/chemistry, Humans, Point Mutation, Bridged-Ring Compounds/chemistry, Protein Multimerization

Access URL: https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/cbic.201800521
https://pubmed.ncbi.nlm.nih.gov/30300966
https://chemistry-europe.onlinelibrary.wiley.com/doi/abs/10.1002/cbic.201800521
https://www.onlinelibrary.wiley.com/doi/abs/10.1002/cbic.201800521
https://europepmc.org/abstract/MED/30300966
https://www.onlinelibrary.wiley.com/doi/10.1002/cbic.201800521
https://chemistry-europe.onlinelibrary.wiley.com/doi/pdf/10.1002/cbic.201800521
https://www.narcis.nl/publication/RecordID/oai%3Apure.tue.nl%3Apublications%2F414d47ec-dd89-46a6-aa55-5b17a226aec3

Structural Insights Into the Disruption of Tnf-tnfr1 Signalling by Small Molecules Stabilising a Distorted Tnf

Authors: McMillan, David, Martinez-Fleites, Carlos, Porter, John, Fox, David, Davis, Rachel E., Mori, Prashant, Ceska, Tom, Carrington, Bruce, Lawson, Alastair, Bourne, Tim, O'Connell, James

Source: Faculty Publications

Subject Terms: molecules, TNF-TNFR1, TNF, Tumour necrosis factor, tumor, Algorithms, Animals, Binding, Competitive (drug effects), Humans, Models, Molecular, Protein Binding (drug effects), Protein Conformation (drug effects), Protein Multimerization (drug effects), Receptors, Tumor Necrosis Factor, Type I (chemistry, metabolism), Signal Transduction (drug effects), Small Molecule Libraries (chemistry, pharmacology), Tumor Necrosis Factor-alpha (chemistry, Public Health Education and Promotion

File Description: application/pdf

Relation: https://scholarcommons.sc.edu/sph_health_promotion_education_behavior_facpub/373; https://scholarcommons.sc.edu/context/sph_health_promotion_education_behavior_facpub/article/1374/viewcontent/s41467_020_20828_3.pdf

Availability: https://scholarcommons.sc.edu/sph_health_promotion_education_behavior_facpub/373
https://doi.org/10.1038/s41467-020-20828-3;
https://scholarcommons.sc.edu/context/sph_health_promotion_education_behavior_facpub/article/1374/viewcontent/s41467_020_20828_3.pdf

Structural insights into the disruption of TNF-TNFR1 signalling by small molecules stabilising a distorted TNF

Authors: David A. Fox, Alastair D. G. Lawson, Rachel Davis, Carlos Martinez-Fleites, Tim Bourne, Tom Ceska, David McMillan, Bruce Carrington, John Robert Porter, O'connell James Philip, Prashant Mori

Source: Nat Commun
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)

Subject Terms: Models, Molecular, 0301 basic medicine, tumor, pharmacology), Protein Conformation, Science, TNF-TNFR1, TNF, Binding, Competitive, Article, Small Molecule Libraries, 03 medical and health sciences, Protein Multimerization (drug effects), Models, Receptors, Animals, Humans, molecules, Tumor Necrosis Factor-alpha (chemistry, 0303 health sciences, metabolism), Tumor Necrosis Factor-alpha, Protein Binding (drug effects), Protein Conformation (drug effects), Molecular, Type I (chemistry, Binding, Receptors, Tumor Necrosis Factor, Type I, Signal Transduction (drug effects), Tumour necrosis factor, Protein Multimerization, Competitive (drug effects), Tumor Necrosis Factor, Small Molecule Libraries (chemistry, Public Health Education and Promotion, Algorithms, Protein Binding, Signal Transduction

File Description: application/pdf

Access URL: https://www.nature.com/articles/s41467-020-20828-3.pdf
https://pubmed.ncbi.nlm.nih.gov/33495441
https://doaj.org/article/7b680bc50b1f4b8588a84e2e0adb588a
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7835368/
https://www.nature.com/articles/s41467-020-20828-3
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7835368/
https://europepmc.org/article/PMC/PMC7835368
https://pubmed.ncbi.nlm.nih.gov/33495441/
https://www.nature.com/articles/s41467-020-20828-3.pdf

Inhibition of hIAPP Amyloid Aggregation and Pancreatic β-Cell Toxicity by OH-Terminated PAMAM Dendrimer

Authors: Gurzov, EN, Wang, B, Pilkington, EH, Chen, P, Kakinen, A, Stanley, WJ, Litwak, SA, Hanssen, EG, Davis, TP, Ding, F, Ke, PC

Source: Small. 12:1615-1626

Subject Terms: Models, Molecular, 0301 basic medicine, Engineering, high-throughput dynamic light scattering, Materials Science and Engineering, Models, Dendrimers -- toxicity, Insulin-Secreting Cells, Insulin, Diabetes-Mellitus, Alzheimers-Disease, Oil Dispersants, 2. Zero hunger, 0303 health sciences, Cell Death, Physics, Amyloid -- metabolism, Sciences bio-médicales et agricoles, Islet Amyloid Polypeptide, 3. Good health, Cytoprotection -- drug effects, Iapp, cytotoxicity, Islet, Amyloid, Dendrimers, human islet amyloid polypeptide, amyloid fibrillation, Science, hydroxyl-terminated polyamidoamine dendrimer, Hydroxylation, Protein Multimerization -- drug effects, protein aggregation, Protein Aggregates -- drug effects, Protein Aggregates, 03 medical and health sciences, Thiazoles -- metabolism, Islet Amyloid Polypeptide -- metabolism, Humans, Cell Death -- drug effects, Benzothiazoles, discrete molecular dynamics simulations, hydroxyl‐terminated polyamidoamine dendrimer, Polypeptide Fibril Formation, Molecular, Discrete Molecular-Dynamics, Insulin-Secreting Cells -- drug effects -- pathology, Thiazoles, high‐throughput dynamic light scattering, In-Vitro, Cytoprotection, Branched Polyamines, Protein Multimerization

File Description: No full-text files; application/pdf

Access URL: http://minerva-access.unimelb.edu.au/bitstream/11343/290861/1/smll.201502317.pdf
https://pubmed.ncbi.nlm.nih.gov/26808649
http://europepmc.org/abstract/MED/26808649
https://www.ncbi.nlm.nih.gov/pubmed/26808649
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/260224/Details
https://onlinelibrary.wiley.com/doi/full/10.1002/smll.201502317
https://research.monash.edu/en/publications/inhibition-of-hiapp-amyloid-aggregation-and-pancreatic-%CE%B2-cell-tox
https://onlinelibrary.wiley.com/doi/10.1002/smll.201502317/full

Small Molecules That Inhibit Tnf Signalling by Stabilising an Asymmetric Form of the Trimer

Authors: O'Connell, James, Porter, John, Kroeplien, Boris, Norman, Tim, Rapecki, Stephen, Davis, Rachel E., McMillan, David, Arakaki, Tracy, Burgin, Alex, Fox Iii, David, Ceska, Tom, Lecomte, Fabien, Maloney, Alison, Vugler, Alex, Carrington, Bruce, Cossins, Benjamin P, Bourne, Tim, Lawson, Alastair

Source: Faculty Publications

Subject Terms: Drug discovery and development, Screening, Structure-based drug design, Tumour necrosis factor, Animals, Anti-Inflammatory Agents (pharmacology, therapeutic use), Arthritis, Experimental (drug therapy, immunology), Cell Line, Crystallography, X-Ray, Drug Discovery, Male, Mice, Molecular Dynamics Simulation, Neutrophil Infiltration (drug effects), Neutrophils (drug effects, Protein Multimerization (drug effects), Protein Stability (drug effects), Protein Structure, Quaternary (drug effects), Receptors, Tumor Necrosis Factor, Type I (immunology, metabolism), Recombinant Proteins (isolation & purification, metabolism, ultrastructure)

File Description: application/pdf

Relation: https://scholarcommons.sc.edu/sph_health_promotion_education_behavior_facpub/376; https://scholarcommons.sc.edu/context/sph_health_promotion_education_behavior_facpub/article/1377/viewcontent/s41467_019_13616_1.pdf

Availability: https://scholarcommons.sc.edu/sph_health_promotion_education_behavior_facpub/376
https://doi.org/10.1038/s41467-019-13616-1;
https://scholarcommons.sc.edu/context/sph_health_promotion_education_behavior_facpub/article/1377/viewcontent/s41467_019_13616_1.pdf

Identification of Open Stomata1-Interacting Proteins Reveals Interactions with Sucrose Non-fermenting1-Related Protein Kinases2 and with Type 2A Protein Phosphatases That Function in Abscisic Acid Responses

Authors: Rainer Waadt, Bianca Manalansan, Navin Rauniyar, Shintaro Munemasa, Matthew A. Booker, Benjamin Brandt, Christian Waadt, Dmitri A. Nusinow, Steve A. Kay, Hans-Henning Kunz, Karin Schumacher, Alison DeLong, John R. Yates, Julian I. Schroeder

Source: Plant Physiology. 169:760-779

Subject Terms: Protein Interaction Maps - drug effects, 0301 basic medicine, Arabidopsis Proteins - metabolism, Genetically Modified, Germination, Protein Serine-Threonine Kinases, Fluorescence, 03 medical and health sciences, Mutation - genetics, Two-Hybrid System Techniques, Immunoprecipitation, Protein Interaction Maps, Protein Phosphatase 2, Protein-Serine-Threonine Kinases - metabolism, 0303 health sciences, Protein Phosphatase 2 - metabolism, Arabidopsis Proteins, Protein Subunits - metabolism, Germination - drug effects, Protein Binding - drug effects, Reproducibility of Results, Protein Kinases - metabolism, Plants, Plants, Genetically Modified, Protein Multimerization - drug effects, Protein Subunits, Abscisic Acid - pharmacology, Mutation, Protein Multimerization, Protein Kinases, Abscisic Acid, Protein Binding

Access URL: http://www.plantphysiol.org/content/plantphysiol/169/1/760.full.pdf
https://pubmed.ncbi.nlm.nih.gov/26175513
https://pubmed.ncbi.nlm.nih.gov/26175513/
https://europepmc.org/article/MED/26175513
https://www.cabdirect.org/cabdirect/abstract/20153317534
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4577397
https://okayama.pure.elsevier.com/en/publications/identification-of-open-stomata1-interacting-proteins-reveals-inte
https://www.ncbi.nlm.nih.gov/pubmed/26175513

Small molecules that inhibit TNF signalling by stabilising an asymmetric form of the trimer

Authors: James O’Connell, John Porter, Boris Kroeplien, Tim Norman, Stephen Rapecki, Rachel Davis, David McMillan, Tracy Arakaki, Alex Burgin, David Fox III, Tom Ceska, Fabien Lecomte, Alison Maloney, Alex Vugler, Bruce Carrington, Benjamin P Cossins, Tim Bourne, Alastair Lawson

Source: Nat Commun
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)

Subject Terms: Male, 0301 basic medicine, isolation & purification, Neutrophils, Anti-Inflammatory Agents, Tumor Necrosis Factor-alpha (antagonists & inhibitors, Crystallography, X-Ray, Neutrophils (drug effects, immunology, Mice, Receptors, Drug Discovery, Protein Stability (drug effects), Signal Transduction (drug effects, 0303 health sciences, Crystallography, metabolism), Protein Stability, Quaternary (drug effects), Neutrophil Infiltration (drug effects), Recombinant Proteins, 3. Good health, Treatment Outcome, Neutrophil Infiltration, therapeutic use), Receptors, Tumor Necrosis Factor, Type I, Screening, Structure-based drug design, Type I (immunology, Public Health Education and Promotion, Signal Transduction, Protein Structure, Science, Recombinant Proteins (isolation & purification, Molecular Dynamics Simulation, Article, Cell Line, Structure-Activity Relationship, 03 medical and health sciences, Protein Multimerization (drug effects), Animals, Drug discovery and development, Protein Structure, Quaternary, Experimental (drug therapy, Tumor Necrosis Factor-alpha, Arthritis, ultrastructure), immunology), Arthritis, Experimental, X-Ray, Tumour necrosis factor, Protein Multimerization, Tumor Necrosis Factor, metabolism, Anti-Inflammatory Agents (pharmacology

File Description: application/pdf

Access URL: https://www.nature.com/articles/s41467-019-13616-1.pdf
https://pubmed.ncbi.nlm.nih.gov/31857588
https://doaj.org/article/cd8aea08c83948d3a69fc5302494dedc
https://www2.rcsb.org/structure/6OP0
https://www4.rcsb.org/structure/6OOZ
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6923382
https://www.nature.com/articles/s41467-019-13616-1.pdf
https://www.nature.com/articles/s41467-019-13616-1
http://www.rcsb.org/structure/6OOY

Secretion of VEGF-165 has unique characteristics, including shedding from the plasma membrane

Authors: Guzmán-Hernández, Maria Luisa, Potter, Gael, Egervari, Kristof Levente, Kiss, Jozsef Zoltan, Balla, Tamas

Source: Mol Biol Cell
Molecular Biology of the Cell, Vol. 25, No 7 (2014) pp. 1061-72

Subject Terms: Phosphatidylinositol 4,5-Diphosphate, Vascular Endothelial Growth Factor A, 0301 basic medicine, 616.8, Glycosylation, Cell Membrane/drug effects/metabolism/ultrastructure, Phosphatidylinositol 4,5-Diphosphate/metabolism, Recombinant Fusion Proteins, Green Fluorescent Proteins, Glycosylation/drug effects, Golgi Apparatus, Endoplasmic Reticulum/drug effects/metabolism, Endoplasmic Reticulum, Cercopithecus aethiops, GTP Phosphohydrolases, 03 medical and health sciences, Vascular Endothelial Growth Factor A/secretion/ultrastructure, Chlorocebus aethiops, Human Umbilical Vein Endothelial Cells, Animals, Humans, Green Fluorescent Proteins/metabolism, Sirolimus, 0303 health sciences, Cell Membrane, Sirolimus/pharmacology, Articles, Golgi Apparatus/drug effects/metabolism, Protein Multimerization/drug effects, Protein Transport/drug effects, 6. Clean water, ddc:616.8, Protein Transport, Human Umbilical Vein Endothelial Cells/drug effects/metabolism, COS Cells, Recombinant Fusion Proteins/metabolism, GTP Phosphohydrolases/metabolism, Protein Multimerization

File Description: application/pdf

Access URL: https://pubmed.ncbi.nlm.nih.gov/24501421
https://archive-ouverte.unige.ch/unige:74474
https://doi.org/10.1091/mbc.e13-07-0418
https://archive-ouverte.unige.ch/unige:74474

AMD3100 disrupts the cross-talk between chronic lymphocytic leukemia cells and a mesenchymal stromal or nurse-like cell-based microenvironment: pre-clinical evidence for its association with chronic lymphocytic leukemia treatments

Authors: Stamatopoulos, Basile, Meuleman, Nathalie, De Bruyn, Cécile, Pieters, Karlien, Mineur, Philippe, Le Roy, Christine, Saint-Georges, Stéphane, Varin-Blank, Nadine, Cymbalista, Florence, Bron, Dominique, Lagneaux, Laurence

Contributors: Boualem, Karim, USC EA 3671 Mycoplasmal and chlamydial infections in humans, Université de Bordeaux (UB), Adaptateurs de signalisation en hématologie (ASIH), Université Paris 13 (UP13)-Université Sorbonne Paris Cité (USPC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Paris 13 (UP13), Service d'hématologie clinique Avicenne, Université Paris 13 (UP13)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpital Avicenne AP-HP, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)

Source: Haematologica, Vol 97, Iss 4 (2012)

Subject Terms: 0301 basic medicine, Benzylamines, [SDV]Life Sciences [q-bio], Mesenchymal stromal cells, Apoptosis, Cell Communication, Cyclams, Actins -- metabolism, Cell Movement, Heterocyclic Compounds, Receptors, Leukocytes, Protein Binding -- drug effects -- immunology, Tumor Microenvironment, Chronic, 0303 health sciences, Leukemia, Antibodies, Monoclonal, Cell Survival -- drug effects, Lymphocytic, 3. Good health, [SDV] Life Sciences [q-bio], CXCR4 -- antagonists & inhibitors -- immunology -- metabolism, Tumor Microenvironment -- drug effects, Protein Binding, Receptors, CXCR4, Microenvironment, Cell Survival, Antineoplastic Agents -- pharmacology -- therapeutic use, Antineoplastic Agents, Protein Multimerization -- drug effects, Antibodies, Cell Communication -- drug effects, Monoclonal -- immunology -- metabolism, 03 medical and health sciences, Chemokine CXCL12 -- pharmacology, Nurse-like cells, Humans, Diseases of the blood and blood-forming organs, Mesenchymal Stromal Cells -- drug effects -- metabolism, Cell Movement -- drug effects, Mesenchymal Stem Cells, Mononuclear -- drug effects -- metabolism, Amd3100, Leukemia, Lymphocytic, Chronic, B-Cell, Actins, Chemokine CXCL12, Coculture Techniques, Cancérologie, B-Cell -- drug therapy -- metabolism, Leukocytes, Mononuclear, Chronic lymphocytic leukemia, RC633-647.5, Protein Multimerization, Apoptosis -- drug effects, Heterocyclic Compounds -- pharmacology -- therapeutic use

File Description: 1 full-text file(s): application/pdf

Access URL: https://pubmed.ncbi.nlm.nih.gov/22058221
https://doaj.org/article/e90b65b96e1a41afa3fe0fc80b30ead6
http://www.haematologica.org/content/haematol/suppl/2012/04/06/haematol.2011.052779.DC1/2011.052779.Stamatopoulos_suppl.pdf
http://europepmc.org/articles/PMC3347654
https://pubmed.ncbi.nlm.nih.gov/22058221/
https://www.ncbi.nlm.nih.gov/pubmed/22058221
https://haematologica.org/article/view/6278
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/144367/Details

Role of ERK1/2 activation in microtubule stabilization and glucose transport in cardiomyocytes

Authors: Mohamed Asrih, Irène Papageorgiou, René Lerch, Corinne Pellieux, Christophe Albert Montessuit

Source: American Journal of Physiology. Endocrinology and Metabolism, Vol. 301, No 5 (2011) pp. E836-43
American journal of physiology. Endocrinology and metabolism

Subject Terms: Male, 0301 basic medicine, Insulin/pharmacology, MAP Kinase Signaling System, Primary Cell Culture, Tretinoin, Microtubules, Rats, Sprague-Dawley, 03 medical and health sciences, Stress, Physiological/physiology, Stress, Physiological, Protein Stability/drug effects, Glucose/metabolism, Animals, Insulin, Myocytes, Cardiac, Enzyme Activation/drug effects/physiology, Alitretinoin, Cells, Cultured, ddc:616, 0303 health sciences, Mitogen-Activated Protein Kinase 3, Tretinoin/pharmacology, Microtubules/drug effects/metabolism, Protein Stability, Biological Transport, Mitogen-Activated Protein Kinase 3/metabolism, Protein Multimerization/drug effects, Rats, Myocytes, Cardiac/drug effects/metabolism/physiology, Enzyme Activation, Biological Transport/drug effects/physiology, Glucose, MAP Kinase Signaling System/drug effects/physiology, Protein Multimerization

File Description: application/pdf

Access URL: https://pubmed.ncbi.nlm.nih.gov/21771966
https://journals.physiology.org/doi/full/10.1152/ajpendo.00160.2011
https://www.physiology.org/doi/10.1152/ajpendo.00160.2011
https://core.ac.uk/display/60997633
https://ajpendo.physiology.org/content/ajpendo/301/5/E836.full.pdf
https://archive-ouverte.unige.ch/unige:88465
https://www.physiology.org/doi/pdf/10.1152/ajpendo.00160.2011
https://archive-ouverte.unige.ch/unige:88465

Local Cytosolic Ca2+ Elevations Are Required for Stromal Interaction Molecule 1 (STIM1) De-oligomerization and Termination of Store-operated Ca2+ Entry

Authors: Shen, Weiwei, Frieden, Maud, Demaurex, Nicolas

Source: J Biol Chem
Journal of Biological Chemistry, Vol. 286, No 42 (2011) pp. 36448-59
The Journal of biological chemistry

Subject Terms: 0301 basic medicine, 0303 health sciences, Calcium/metabolism, Fluorescence Resonance Energy Transfer/methods, Membrane Proteins, Membrane Proteins/genetics/metabolism, Endoplasmic Reticulum, Neoplasm Proteins/genetics/metabolism, Neoplasm Proteins, Protein Multimerization/drug effects/physiology, 03 medical and health sciences, Fluorescence Resonance Energy Transfer, Humans, Endoplasmic Reticulum/genetics/metabolism, Calcium, Stromal Interaction Molecule 1, Protein Multimerization, ddc:612, Chelating Agents/pharmacology, Signal Transduction, Chelating Agents, HeLa Cells

File Description: application/pdf

Access URL: http://www.jbc.org/content/286/42/36448.full.pdf
https://pubmed.ncbi.nlm.nih.gov/21880734
https://archive-ouverte.unige.ch/unige:21499/ATTACHMENT01
https://www.ncbi.nlm.nih.gov/pubmed/%20%20%20%20%20%2021880734
https://archive-ouverte.unige.ch/unige:21499
https://www.jbc.org/content/286/42/36448
http://www.jbc.org/content/early/2011/08/31/jbc.M111.269415.full.pdf
https://www.ncbi.nlm.nih.gov/pubmed/21880734
https://archive-ouverte.unige.ch/unige:21499
https://doi.org/10.1074/jbc.m111.269415
https://archive-ouverte.unige.ch/unige:21499
http://www.jbc.org/content/286/42/36448.long

Hetero-oligomerization of CCR2, CCR5, and CXCR4 and the Protean Effects of 'Selective' Antagonists

Authors: Sohy, Denis, Yano, Hideaki, De Nadai, Patricia, Urizar Andrieu, Eneko, Guillabert, Aude, Javitch, Jonathan A, Parmentier, Marc, Springael, Jean-Yves

Contributors: de Nadaï, Patricia

Source: The Journal of biological chemistry, 284 (45

Subject Terms: 0301 basic medicine, Benzylamines, Receptors, CXCR4, Receptors, CCR2 -- antagonists & inhibitors, Receptors, CCR5, Receptors, CCR2, Cells, T-Lymphocytes, CCR2 -- antagonists & inhibitors, Receptors, CCR2 -- chemistry, Cyclams, Protein Multimerization -- drug effects, Receptors, CXCR4 -- chemistry, Monocytes, Cell Line, Mice, 03 medical and health sciences, Receptors, CCR5 -- antagonists & inhibitors, Heterocyclic Compounds, Receptors, Animals, Humans, Receptors, CXCR4 -- antagonists & inhibitors, Inbred BALB C, Cells, Cultured, T-Lymphocytes -- metabolism, Mice, Inbred BALB C, 0303 health sciences, Cultured, T-Lymphocytes -- chemistry, CCR5 -- antagonists & inhibitors, Monocytes -- chemistry, Sciences bio-médicales et agricoles, CXCR4 -- chemistry, Monocytes -- metabolism, Quaternary Ammonium Compounds -- pharmacology, Amides, Heterocyclic Compounds -- pharmacology, 3. Good health, CCR2 -- chemistry, [SDV] Life Sciences [q-bio], Quaternary Ammonium Compounds, CCR5 Receptor Antagonists, Amides -- pharmacology, Receptors, CCR5 -- chemistry, CXCR4 -- antagonists & inhibitors, Protein Multimerization, CCR5 -- chemistry

File Description: 1 full-text file(s): application/pdf

Access URL: http://www.jbc.org/content/284/45/31270.full.pdf
https://pubmed.ncbi.nlm.nih.gov/19758998
https://hal.science/hal-04462646v1
https://doi.org/10.1074/jbc.m109.054809
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/52294/Details
https://europepmc.org/article/PMC/PMC2781525
https://www.sciencedirect.com/science/article/pii/S0021925820380285
http://www.jbc.org/content/284/45/31270.full.pdf
https://pubmed.ncbi.nlm.nih.gov/19758998/
https://www.ncbi.nlm.nih.gov/pubmed/19758998
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/52294

A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity

Authors: Perni, Michele, Galvagnion, Céline, Maltsev, Alexander, Meisl, Georg, Müller, Martin B D, Challa, Pavan K, Kirkegaard, Julius B, Flagmeier, Patrick, Cohen, Samuel I A, Cascella, Roberta, Chen, Serene W, Limbocker, Ryan, Sormanni, Pietro, Heller, Gabriella T, Aprile, Francesco A, Cremades, Nunilo, Cecchi, Cristina, Chiti, Fabrizio, Nollen, Ellen A A, Knowles, Tuomas P J, Vendruscolo, Michele, Bax, Adriaan, Zasloff, Michael, Dobson, Christopher M

Source: Perni , M , Galvagnion , C , Maltsev , A , Meisl , G , Müller , M B D , Challa , P K , Kirkegaard , J B , Flagmeier , P , Cohen , S I A , Cascella , R , Chen , S W , Limbocker , R , Sormanni , P , Heller , G T , Aprile , F A , Cremades , N , Cecchi , C , Chiti , F , Nollen , E A A , Knowles , T P J , Vendruscolo , M , Bax , ....

Subject Terms: Algorithms, Amino Acid Sequence, Animals, Genetically Modified, Biological Products/chemistry, Caenorhabditis elegans/genetics, Cell Line, Tumor, Cholestanols/chemistry, Humans, Membrane Lipids/chemistry, Molecular Structure, Neuroblastoma/metabolism, Paresis/genetics, Parkinson Disease/metabolism, Protein Aggregates/drug effects, Protein Aggregation, Pathological/prevention & control, Protein Binding/drug effects, Protein Multimerization/drug effects, alpha-Synuclein/chemistry

Availability: https://researchprofiles.ku.dk/da/publications/66f5d50b-c4dc-4871-aa17-b0b795c35b1e
https://doi.org/10.1073/pnas.1610586114

Phosphatidylinositol-4,5-bisphosphate is required for KCNQ1/KCNE1 channel function but not anterograde trafficking

Authors: Royal, Alice A, Tinker, Andrew, Harmer, Stephen C

Source: Royal, A A, Tinker, A & Harmer, S C 2017, 'Phosphatidylinositol-4,5-bisphosphate is required for KCNQ1/KCNE1 channel function but not anterograde trafficking', PLOS ONE, vol. 12, no. 10, e0186293. https://doi.org/10.1371/journal.pone.0186293

Subject Terms: Animals, CHO Cells, Cell Membrane/drug effects, Cricetinae, Cricetulus, Endoplasmic Reticulum/drug effects, Genes, Reporter, Golgi Apparatus/drug effects, HEK293 Cells, Humans, Ion Channel Gating/drug effects, KCNQ1 Potassium Channel/metabolism, Mutation/genetics, Phosphatidylinositol 4,5-Diphosphate/metabolism, Potassium Channels, Voltage-Gated/metabolism, Protein Binding/drug effects, Protein Multimerization/drug effects, Protein Transport/drug effects, Sirolimus/pharmacology

File Description: application/pdf

Availability: https://hdl.handle.net/1983/e514aac4-3f9f-4fe8-bf0c-8fe083982c1b
https://research-information.bris.ac.uk/en/publications/e514aac4-3f9f-4fe8-bf0c-8fe083982c1b
https://doi.org/10.1371/journal.pone.0186293
https://research-information.bris.ac.uk/ws/files/184566443/Royal_2017_PLoSOne_Phosphatidylinositol_4_5_bisphosphate_is_required_for_KCNQ1_KCNE1_channel_function_but_not_anterograde_trafficking.pdf

Acidic pH Mediates Changes in Antigenic and Oligomeric Conformation of Herpes Simplex Virus gB and Is a Determinant of Cell-Specific Entry

Authors: Weed, Darin J, Dollery, Stephen J, Komala Sari, Tri, Nicola, Anthony V

Source: Journal of Virology. 92

Subject Terms: 0301 basic medicine, Protein Folding, 0303 health sciences, Herpesvirus 1, Protein Conformation, Protein Conformation - drug effects, Temperature, Viral Envelope Proteins - immunology, Herpesvirus 1, Human, Viral Envelope Proteins - metabolism, Hydrogen-Ion Concentration, Virus Internalization, Human - drug effects, Human - radiation effects, 3. Good health, Protein Multimerization - drug effects, 03 medical and health sciences, Viral Envelope Proteins, Viral Envelope Proteins - chemistry, Humans, Human - physiology, Protein Multimerization, Protein Folding - drug effects

Access URL: https://jvi.asm.org/content/jvi/92/17/e01034-18.full.pdf
https://pubmed.ncbi.nlm.nih.gov/29925660
https://europepmc.org/article/MED/29925660
https://pubmed.ncbi.nlm.nih.gov/29925660/
https://journals.asm.org/doi/pdf/10.1128/JVI.01034-18
https://www.ncbi.nlm.nih.gov/pubmed/29925660

A huntingtin peptide inhibits polyQ-huntingtin associated defects

Authors: Arribat, Yoan, Bonneaud, Nathalie, Talmat-Amar, Yasmina, Layalle, Sophie, Parmentier, Marie-Laure, Maschat, Florence

Contributors: Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS)

Source: ISSN: 1932-6203.

Subject Terms: Amino Acid Sequence, Animals, Disease Models, Animal, Drosophila melanogaster/*drug effects/genetics/growth & development/metabolism, Eye/drug effects/metabolism/pathology, Female, Gene Expression Regulation, HeLa Cells, Humans, Huntington Disease/genetics/*metabolism/pathology, Larva/*drug effects/genetics/growth & development/metabolism, Male, Molecular Sequence Data, Motor Activity, Mutation, Nerve Tissue Proteins/*chemistry/genetics/metabolism, Neurons/drug effects/metabolism/pathology, Oligopeptides/chemistry/isolation & purification/*pharmacology, Peptides/*chemistry/metabolism, Protein Binding, Protein Multimerization/drug effects, Protein Transport, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology

Relation: hal-01984749; https://hal.archives-ouvertes.fr/hal-01984749; https://hal.archives-ouvertes.fr/hal-01984749/document; https://hal.archives-ouvertes.fr/hal-01984749/file/pone.0068775.pdf

Availability: https://hal.archives-ouvertes.fr/hal-01984749
https://hal.archives-ouvertes.fr/hal-01984749/document
https://hal.archives-ouvertes.fr/hal-01984749/file/pone.0068775.pdf
https://doi.org/10.1371/journal.pone.0068775

An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils.

Authors: Agerschou, Emil Dandanell, Flagmeier, Patrick, Voigt, Aaron, Falkenburger, Bjoern, Hoyer, Wolfgang, Buell, Alexander K, Saridaki, Theodora, Galvagnion, Céline, Komnig, Daniel, Heid, Laetitia, Prasad, Vibha, Shaykhalishahi, Hamed, Willbold, Dieter, Dobson, Christopher M

Source: eLife 8, e46112 (2019). doi:10.7554/eLife.46112

Subject Terms: info:eu-repo/classification/ddc/600, Amyloid: antagonists & inhibitors, HEK293 Cells, Humans, Protein Aggregation, Pathological, Protein Multimerization: drug effects, Recombinant Proteins: genetics, Recombinant Proteins: metabolism, alpha-Synuclein: metabolism

Subject Geographic: DE

Relation: info:eu-repo/semantics/altIdentifier/issn/2050-084X; info:eu-repo/semantics/altIdentifier/pmid/pmid:31389332; https://pub.dzne.de/record/140939

Availability: https://pub.dzne.de/record/140939
https://pub.dzne.de/search?p=id:%22DZNE-2020-07261%22

A General Strategy for Discovery of Inhibitors and Activators of RING and U-box E3 Ligases with Ubiquitin Variants

Authors: Gabrielsen, Mads, Buetow, Lori, Nakasone, Mark A., Ahmed, Syed Feroj, Sibbet, Gary J., Smith, Brian O., Zhang, Wei, Sidhu, Sachdev S., Huang, Danny T.

Source: Mol Cell
Molecular Cell

Subject Terms: 0301 basic medicine, 0303 health sciences, Tumor Suppressor Proteins/agonists, Tumor Suppressor Proteins, Ubiquitin-Protein Ligases, Enzyme Activators, Ubiquitin-Protein Ligase Complexes, X-Linked Inhibitor of Apoptosis Protein, Protein Multimerization/drug effects, Article, Enzyme Activators/chemistry, 3. Good health, Enzyme Inhibitors/chemistry, X-Linked Inhibitor of Apoptosis Protein/agonists, 03 medical and health sciences, HEK293 Cells, Ubiquitin-Protein Ligase Complexes/antagonists & inhibitors, Drug Discovery, Humans, Drug Discovery/methods, Enzyme Inhibitors, Protein Multimerization, HeLa Cells

File Description: application/pdf

Access URL: http://www.cell.com/article/S1097276517307050/pdf
https://pubmed.ncbi.nlm.nih.gov/29053960
https://eprints.gla.ac.uk/150528/1/150528.pdf
https://www.sciencedirect.com/science/article/pii/S1097276517307050
http://www.cell.com/molecular-cell/references/S1097-2765(17)30705-0
https://www.cell.com/molecular-cell/fulltext/S1097-2765(17)30705-0
https://core.ac.uk/display/111558086
http://europepmc.org/articles/PMC5655547
https://pubmed.ncbi.nlm.nih.gov/29053960/

Inhibition of hIAPP Amyloid Aggregation and Pancreatic Beta-Cell Toxicity by OH-Terminated PAMAM Dendrimer.

Authors: Gurzov, Esteban Nicolas, Wang, Bo, Pilkington, Emily H, Chen, Pengyu, Kakinen, Aleksandr, Stanley, William J, Litwak, Sara A, Hanssen, Eric G, Davis, Thomas P, Ding, Feng, Ke, Pu Chun

Source: Small, 12 (12

Subject Terms: Sciences bio-médicales et agricoles, Amyloid -- metabolism, Cell Death -- drug effects, Cytoprotection -- drug effects, Dendrimers -- toxicity, Humans, Hydroxylation, Insulin-Secreting Cells -- drug effects -- pathology, Islet Amyloid Polypeptide -- metabolism, Models, Molecular, Protein Aggregates -- drug effects, Protein Multimerization -- drug effects, Thiazoles -- metabolism, amyloid fibrillation, cytotoxicity, discrete molecular dynamics simulations, high-throughput dynamic light scattering, human islet amyloid polypeptide, hydroxyl-terminated polyamidoamine dendrimer, protein aggregation

File Description: No full-text files

Relation: uri/info:doi/10.1002/smll.201502317; uri/info:pmid/26808649

Availability: http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/260224

Identification of Small Molecule Inhibitors of Tau Aggregation by Targeting Monomeric Tau As a Potential Therapeutic Approach for Tauopathies.

Authors: Pickhardt, Marcus, Neumann, Thomas, Mandelkow, Eckhard, Tóth, Gergely, Schwizer, Daniel, Callaway, Kari, Vendruscolo, Michele, Schenk, Dale, St George-Hyslop, Peter, Mandelkow, Eva M, Dobson, Christopher M, McConlogue, Lisa

Source: Current Alzheimer research 12(9), 814-828 (2015). doi:10.2174/156720501209151019104951

Subject Terms: info:eu-repo/classification/ddc/610, Animals, Benzothiazoles, Cell Line, Tumor, Cell Survival: drug effects, Dose-Response Relationship, Drug, Drug Evaluation, Preclinical, Fluorescent Dyes, High-Throughput Screening Assays, Humans, Mice, Microarray Analysis, Microscopy, Fluorescence, Molecular Structure, Neuroprotective Agents: chemistry, Neuroprotective Agents: pharmacology, Protein Aggregates: drug effects, Protein Multimerization: drug effects, Tauopathies: drug therapy, Tauopathies: metabolism, Thiazoles, tau Proteins: genetics, tau Proteins: metabolism, MAPT protein, human, Neuroprotective Agents

Subject Geographic: DE

Relation: info:eu-repo/semantics/altIdentifier/issn/1567-2050; info:eu-repo/semantics/altIdentifier/pmid/pmid:26510979; info:eu-repo/semantics/altIdentifier/issn/1875-5828; https://pub.dzne.de/record/138183

Availability: https://pub.dzne.de/record/138183
https://pub.dzne.de/search?p=id:%22DZNE-2020-04505%22