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are now well-established examples of carriers and pores which facilitate the transfer of ions across thin lipid membranes. In the absence of such agents, lipid bilayer membranes are extremely impermeable to the common inorganic ions. Thus, the conductance of a pure lecithin + decane or glyceryl mono-oleate + decane membrane in M\u002F10 NaCl is less than10\u003Cjats:sup>−9\u003C\u002Fjats:sup>Ω\u003Cjats:sup>−1\u003C\u002Fjats:sup>cm\u003Cjats:sup>−2\u003C\u002Fjats:sup>. However, on the addition of small lipid-soluble molecules such as valinomycin, or surface-active polypeptides such as gramicidin A, the conductance may become so high (> 10\u003Cjats:sup>−1\u003C\u002Fjats:sup>ω\u003Cjats:sup>−l\u003C\u002Fjats:sup>cm\u003Cjats:sup>−2\u003C\u002Fjats:sup>) that the resistance of the membrane merges into that of the aqueous phase. This review is concerned with the extent to which we now understand how these added substances transfer ions across lipid membranes. Attention has been concentrated on the simpler systems, i.e. the lipid-soluble ions, the 1–1 carriets, a simple pore and, with some loss of simplicity, a substance which prodeces interacting pores. 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In this context, the three-dimensional\n \nstructure has a pivotal role, its knowledge being essential to understand\n the \nphysical, chemical and biological properties of a protein (Branden &\n Tooze, 1991; \nCreighton, 1993). Until 1984 structural information at atomic resolution\n could \nonly be determined by X-ray diffraction techniques with protein single\n crystals \n(Drenth, 1994). The introduction of nuclear magnetic resonance (NMR) \nspectroscopy (Abragam, 1961) as a technique for protein structure determination\n \n(Wüthrich, 1986) has made it possible to obtain structures with comparable\n \naccuracy also in a solution environment that is much closer to the natural\n situation \nin a living being than the single crystals required for protein crystallography.\u003C\u002Fjats:p>",{"EN":2018},"Structure calculation of biological macromolecules from NMR data",{"VOID":2020},"9794034",{"VOID":2022},"10.1017\u002Fs0033583598003436",[126],"https:\u002F\u002Fwww.cambridge.org\u002Fcore\u002Fproduct\u002Fidentifier\u002FS0033583598003436\u002Ftype\u002Fjournal_article",[2026],{"id":2027,"sortIndex":25,"researcher":24,"roles":2028,"affiliations":2029,"properties":2041},"a3b3754f-2272-4d44-ac38-12b5a1a8226d",[],[2030],{"id":2031,"sortIndex":25,"affiliation":2032,"properties":24},"0acc9b0c-75a0-4dfc-9b94-71046192567c",{"id":2033,"createTime":2034,"updateTime":2035,"relativeEntities":2036,"slug":2037,"properties":2038,"entityType":45,"verifyStatus":23,"verifyTime":24,"verifyNote":24,"syncStatus":23,"languages":24,"translateLanguages":24,"viewCount":25},"a482441f-8879-4312-83e6-67ed137c6fcc","2024-01-09T17:21:22.717+00:00","2024-12-20T19:46:45.472+00:00",[],"Institut-f%C3%BCr-Molekularbiologie-und-Biophysik-Eidgen%C3%B6ssische-Technische-Hochschule-CH-8093-Z%C3%BCrich-Switzerland",{"title":2039},{"VI":2040},"Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule, CH-8093 Zürich, Switzerland",{"openalex":2042,"orcid":2044,"title":2046},{"VOID":2043},"A5059078778",{"VOID":2045},"https:\u002F\u002Forcid.org\u002F0000-0002-2911-7574",{"EN":2047},"Peter Güntert",{"url":24,"publisher":2049,"properties":2074},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":2050,"slug":10,"properties":2051,"entityType":22,"verifyStatus":23,"verifyTime":24,"verifyNote":24,"syncStatus":23,"languages":24,"translateLanguages":24,"viewCount":25,"subjectFields":2057,"manageAffiliations":2058,"indexDatabases":2059,"url":98,"thumbnailPath":24,"statistic":24,"gsStatistic":24,"type":24,"analyzePriority":24},[],{"country":2052,"issn":2053,"introduce":2054,"eissn":2055,"title":2056},{"VOID":13},{"VOID":15},{"EN":17},{"VOID":19},{"EN":21},[],[],[2060,2067],{"id":61,"indexDatabase":2061,"url":74,"indexYears":75,"academicFieldIds":2066,"indexDatabaseRanking":78},{"id":63,"createTime":64,"updateTime":65,"relativeEntities":2062,"label":2063,"description":2064,"key":71,"publicationTags":2065,"standard":24},[],{"EN":68,"VI":68},{"EN":68,"VI":70},[73],[77],{"id":80,"indexDatabase":2068,"url":95,"indexYears":24,"academicFieldIds":2073,"indexDatabaseRanking":24},{"id":82,"createTime":83,"updateTime":84,"relativeEntities":2069,"label":2070,"description":2071,"key":91,"publicationTags":2072,"standard":24},[],{"EN":87,"VI":87},{"VI":89,"EN":90},[93,94],[97],{"volume":2075,"pages":2077,"issue":2079},{"VOID":2076},"31",{"VOID":2078},"145-237",{"VOID":205},183,{"total":2080,"publishYear":24,"statisticByYear":2082},{"2012":2083,"2013":2084,"2014":57,"2015":214,"2016":2085,"2017":57,"2018":213,"2019":213,"2020":57,"2021":57,"2022":57,"2023":213,"2024":213},16,10,4,"1998-05-01",1998,[],{"id":2090,"createTime":2091,"updateTime":2091,"relativeEntities":2092,"slug":2093,"properties":2094,"entityType":122,"verifyStatus":123,"verifyTime":2091,"verifyNote":124,"syncStatus":23,"languages":2108,"translateLanguages":24,"viewCount":25,"primaryUrl":2109,"fullTextUrl":24,"authors":2110,"publicationType":172,"publisherRelationship":2165,"citationCount":2197,"citationInfo":2198,"publishDate":2211,"publishYear":2212,"citationAnalyzeStatus":23,"lastCitationAnalyze":24,"indexDatabases":24,"openAccess":24,"references":2213,"isForceReanalyzing":918},"f12603c9-a4f4-45cc-81d0-7fcd63a95918","2024-09-18T19:16:32.494+00:00",[],"Physical-principles-of-membrane-organization",{"mag":2095,"keywords":2097,"openalex":2098,"abstract":2100,"title":2102,"pm":2104,"doi":2106},{"VOID":2096},"2165852855",{},{"VOID":2099},"W2165852855",{"EN":2101},"\u003Cjats:p>Membranes are the most common cellular structures in both plants and animals. They are now recognized as being involved in almost all aspects of cellular activity ranging from motility and food entrapment in simple unicellular organisms, to energy transduction, immunorecognition, nerve conduction and biosynthesis in plants and higher organisms. This functional diversity is reflected in the wide variety of lipids and particularly of proteins that compose different membranes. An understanding of the physical principles that govern the molecular organization of membranes is essential for an understanding of their physiological roles since\u003Cjats:italic>structure\u003C\u002Fjats:italic>and\u003Cjats:italic>function\u003C\u002Fjats:italic>are much more interdependent in membranes than in, say, simple chemical reactions in solution. 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Naturf., 28, 693, 10.1515\u002Fznc-1973-11-1209",{"doi":2818},"10.1515\u002Fznc-1973-11-1209",{"id":24,"text":2820,"url":24,"identifiers":2821},"10.1126\u002Fscience.402030",{"doi":2820},{"id":24,"text":2823,"url":24,"identifiers":2824},"10.1039\u002Fcs9770600025",{"doi":2823},{"id":24,"text":2826,"url":24,"identifiers":2827},"Mitchell D. J. & Ninham B. W. (1980). Micelles, vesicles and microemulsions. J. Chem. Soc. Faraday Trans. 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These potentials are applicable to any system in a state of equilibrium but are especially useful in the study of the behaviour, or, as we may say, the functional chemistry, of a macromolecule in the presence of its ligands. In this paper I show how these potentials may be represented by a set of contour graphs which embody the results of observation and are transformable into one another by a group of graphical permutations equivalent to the Legendre group.\u003C\u002Fjats:p>",{"EN":2845},"Linkage graphs: a study in the thermodynamics of macromolecules",{"VOID":2847},"6398878",{"VOID":2849},"10.1017\u002Fs0033583500004881",[126],"https:\u002F\u002Fwww.cambridge.org\u002Fcore\u002Fproduct\u002Fidentifier\u002FS0033583500004881\u002Ftype\u002Fjournal_article",[2853],{"id":2854,"sortIndex":25,"researcher":24,"roles":2855,"affiliations":2856,"properties":2867},"ebc4046d-ee04-4358-9086-de47397b5129",[],[2857],{"id":2858,"sortIndex":25,"affiliation":2859,"properties":24},"bff117f8-977d-4910-a20d-6ca1b3538e3c",{"id":2860,"createTime":2861,"updateTime":2861,"relativeEntities":2862,"slug":2863,"properties":2864,"entityType":45,"verifyStatus":23,"verifyTime":24,"verifyNote":24,"syncStatus":23,"languages":24,"translateLanguages":24,"viewCount":25},"e9e7fc4e-ef3a-49f2-9b3e-80d0f977d5e9","2024-10-04T18:33:48.144+00:00",[],"CNR-Center-for-Molecular-Biology-Istituto-di-Chimica-Facolt%C3%A0-di-Medicina-Universit%C3%A0-di-Roma-I-00185-Rome-Italy-and-Department-of-Chemistry-University-of-Colorado-Boulder-CO-80309",{"title":2865},{"EN":2866},"CNR Center for Molecular Biology, Istituto di Chimica Facoltà di Medicina, Università di Roma I 00185 Rome Italy, and Department of Chemistry, University of Colorado, Boulder, CO 80309",{"openalex":2868,"title":2870},{"VOID":2869},"A5059914372",{"EN":2871},"Jeffries Wyman",{"url":24,"publisher":2873,"properties":2898},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":2874,"slug":10,"properties":2875,"entityType":22,"verifyStatus":23,"verifyTime":24,"verifyNote":24,"syncStatus":23,"languages":24,"translateLanguages":24,"viewCount":25,"subjectFields":2881,"manageAffiliations":2882,"indexDatabases":2883,"url":98,"thumbnailPath":24,"statistic":24,"gsStatistic":24,"type":24,"analyzePriority":24},[],{"country":2876,"issn":2877,"introduce":2878,"eissn":2879,"title":2880},{"VOID":13},{"VOID":15},{"EN":17},{"VOID":19},{"EN":21},[],[],[2884,2891],{"id":61,"indexDatabase":2885,"url":74,"indexYears":75,"academicFieldIds":2890,"indexDatabaseRanking":78},{"id":63,"createTime":64,"updateTime":65,"relativeEntities":2886,"label":2887,"description":2888,"key":71,"publicationTags":2889,"standard":24},[],{"EN":68,"VI":68},{"EN":68,"VI":70},[73],[77],{"id":80,"indexDatabase":2892,"url":95,"indexYears":24,"academicFieldIds":2897,"indexDatabaseRanking":24},{"id":82,"createTime":83,"updateTime":84,"relativeEntities":2893,"label":2894,"description":2895,"key":91,"publicationTags":2896,"standard":24},[],{"EN":87,"VI":87},{"VI":89,"EN":90},[93,94],[97],{"volume":2899,"pages":2901,"issue":2903},{"VOID":2900},"17",{"VOID":2902},"453-488",{"VOID":2904},"4",53,{"total":2905,"publishYear":24,"statisticByYear":2907},{"2012":46,"2013":131},"1984-11-01",1984,[2911,2914,2917,2920,2923,2926,2929,2932,2935,2938,2941,2944,2947,2950,2953,2956,2959,2962,2965,2968,2971,2974,2977,2980],{"id":24,"text":2912,"url":24,"identifiers":2913},"10.1016\u002F0301-4622(81)85014-4",{"doi":2912},{"id":24,"text":2915,"url":24,"identifiers":2916},"10.1073\u002Fpnas.72.4.1464",{"doi":2915},{"id":24,"text":2918,"url":24,"identifiers":2919},"Wyman, 1976, The turning wheel: a study in steady states, Proc. natn. 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At that time, it was possible to describe the field in terms of a limited amount of exciting new structural information, and a long list of unanswered questions. While the stoichiometry of oxygen binding was understood, virtually nothing was known about the active site. Even the oxidation state of the copper was a matter of conjecture. The size of the haemocyanin polypeptide chains was the subject of intense debate, with very little substantive knowledge available. While the haemocyanins were known to be allosteric proteins, there were virtually no experimental studies of oxygen binding on a level that could be meaningfully interpreted in terms of extant theories.\u003C\u002Fjats:p>",{"EN":2987},{"VOID":2996},"7048392",{"VOID":2998},"10.1017\u002Fs0033583500002705","2024-10-04T18:33:47.820+00:00",[126],"https:\u002F\u002Fwww.cambridge.org\u002Fcore\u002Fproduct\u002Fidentifier\u002FS0033583500002705\u002Ftype\u002Fjournal_article",[3003,3025],{"id":3004,"sortIndex":25,"researcher":24,"roles":3005,"affiliations":3006,"properties":3018},"08373f6b-1166-459e-9db5-eca4ba31b0f9",[],[3007],{"id":3008,"sortIndex":25,"affiliation":3009,"properties":24},"1cd010af-2f0f-4942-96e6-720d8c3435ab",{"id":3010,"createTime":3011,"updateTime":3012,"relativeEntities":3013,"slug":3014,"properties":3015,"entityType":45,"verifyStatus":23,"verifyTime":24,"verifyNote":24,"syncStatus":23,"languages":24,"translateLanguages":24,"viewCount":25},"4cd13c88-1cf7-468b-817e-ea71f36fe357","2023-12-11T10:07:56.620+00:00","2024-10-04T18:33:47.837+00:00",[],"Department-of-Biochemistry-and-Biophysics-Oregon-State-University-Corvallis-Oregon-97331",{"title":3016},{"VI":3017},"Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331",{"openalex":3019,"orcid":3021,"title":3023},{"VOID":3020},"A5087812852",{"VOID":3022},"https:\u002F\u002Forcid.org\u002F0009-0004-0232-855X",{"EN":3024},"Kensal E. van Holde",{"id":3026,"sortIndex":131,"researcher":24,"roles":3027,"affiliations":3028,"properties":3035},"39bd4783-3ab2-45b1-86a7-f0d5e13f6d7f",[],[3029],{"id":3030,"sortIndex":25,"affiliation":3031,"properties":24},"d274ad4b-a70a-4de4-bdf1-22ffdde3dc7e",{"id":3010,"createTime":3011,"updateTime":3012,"relativeEntities":3032,"slug":3014,"properties":3033,"entityType":45,"verifyStatus":23,"verifyTime":24,"verifyNote":24,"syncStatus":23,"languages":24,"translateLanguages":24,"viewCount":25},[],{"title":3034},{"VI":3017},{"openalex":3036,"title":3038},{"VOID":3037},"A5034211811",{"EN":3039},"Karen I. 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Biol., 63, 661, 10.1242\u002Fjeb.63.3.661",{"doi":3125},"10.1242\u002Fjeb.63.3.661",{"id":24,"text":3127,"url":24,"identifiers":3128},"10.1002\u002Fjez.1401910213",{"doi":3127},{"id":24,"text":3130,"url":24,"identifiers":3131},"10.1093\u002Foxfordjournals.jbchem.a129611",{"doi":3130},{"id":24,"text":3133,"url":24,"identifiers":3134},"10.1016\u002F0005-2736(80)90534-9",{"doi":3133},{"id":24,"text":3136,"url":24,"identifiers":3137},"10.1007\u002F978-3-642-66679-7_7",{"doi":3136},{"id":24,"text":3139,"url":24,"identifiers":3140},"10.1016\u002F0006-291X(74)90872-9",{"doi":3139},{"id":24,"text":3142,"url":24,"identifiers":3143},"10.1016\u002F0014-5793(72)80204-7",{"doi":3142},{"id":24,"text":3145,"url":24,"identifiers":3146},"10.1016\u002F0006-291X(73)91378-8",{"doi":3145},{"id":24,"text":3148,"url":24,"identifiers":3149},"Linzen, 1977, Structure and Function of Haemocyanin, 271",{},{"id":24,"text":3151,"url":24,"identifiers":3152},"Lontie, 1979, Metalloproteins, 62",{},{"id":24,"text":3154,"url":24,"identifiers":3155},"10.1016\u002F0014-5793(76)80675-8",{"doi":3154},{"id":24,"text":3157,"url":24,"identifiers":3158},"10.2307\u002F1540760",{"doi":3157},{"id":24,"text":3160,"url":24,"identifiers":3161},"10.1042\u002Fbst0070389",{"doi":3160},{"id":24,"text":3163,"url":24,"identifiers":3164},"10.2307\u002F1538515",{"doi":3163},{"id":24,"text":3166,"url":24,"identifiers":3167},"10.1093\u002Ficb\u002F20.1.19",{"doi":3166},{"id":24,"text":3169,"url":24,"identifiers":3170},"Lamy, 1981, Invertebrate Oxygen Binding Proteins: Structure, Active Site and Function, 425",{},{"id":24,"text":3172,"url":24,"identifiers":3173},"10.1016\u002F0005-2736(75)90155-8",{"doi":3172},{"id":24,"text":3175,"url":24,"identifiers":3176},"10.1021\u002Fbi00510a021",{"doi":3175},{"id":24,"text":3178,"url":24,"identifiers":3179},"10.1038\u002F250154a0",{"doi":3178},{"id":24,"text":3181,"url":24,"identifiers":3182},"Lontie, 1974, Metal Ions in Biological Systems, 182",{},{"id":24,"text":3184,"url":24,"identifiers":3185},"Wolf, 1980, Immunological evidence for haemocyanin-related proteins in mature eggs and embryos of Sepia officinalis L, Arch. int. 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Biol., 87, 73",{},{"id":24,"text":3211,"url":24,"identifiers":3212},"Konings W. (1969). Structure and function of hemocyanins. Ph.D. thesis, Groningin.",{},{"id":24,"text":3214,"url":24,"identifiers":3215},"10.1007\u002FBF01868110",{"doi":3214},{"id":24,"text":3217,"url":24,"identifiers":3218},"Ryan M. C. (1980). Characterization and subunit structure of the hemocyanin of a polyplacophoran, Katherina tunicata (Wood). M.S. Thesis, University of Oregon.",{},{"id":24,"text":3220,"url":24,"identifiers":3221},"Verschueren, 1981, Invertebrate Oxygen Binding Proteins: Structure, Active Site and Function, 285",{},{"id":24,"text":3223,"url":24,"identifiers":3224},"10.1021\u002Fbi00564a004",{"doi":3223},{"id":24,"text":3226,"url":24,"identifiers":3227},"Lontie, 1973, Inorganic Biochemistry, 344",{},{"id":24,"text":3229,"url":24,"identifiers":3230},"Hall, 1975, The hemocyanin of Lymnaea stagnalis L. (Gastropoda pulmonata), Comp. Biochem. 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The first enzyme in the electron transfer chain, NADH:ubiquinone oxidoreductase (or complex I), is the subject of this review. It removes electrons from NADH and passes them via a series of enzyme-bound redox centres (FMN and Fe-S clusters) to the electron acceptor ubiquinone. For each pair of electrons transferred from NADH to ubiquinone it is usually considered that four protons are removed from the matrix (see section 4.1 for further discussion of this point).\u003C\u002Fjats:p>",{"EN":3944},"The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains",{"VOID":3946},"1470679",{"VOID":3948},"10.1017\u002Fs003358350000425x",[126],"https:\u002F\u002Fwww.cambridge.org\u002Fcore\u002Fproduct\u002Fidentifier\u002FS003358350000425X\u002Ftype\u002Fjournal_article",[3952],{"id":3953,"sortIndex":25,"researcher":24,"roles":3954,"affiliations":3955,"properties":3967},"0a8a5705-688d-4e2c-ad3b-3da29d7c72cc",[],[3956],{"id":3957,"sortIndex":25,"affiliation":3958,"properties":24},"043a78f7-8bf0-400b-b0a2-f94bca60d4c5",{"id":3959,"createTime":3960,"updateTime":3961,"relativeEntities":3962,"slug":3963,"properties":3964,"entityType":45,"verifyStatus":23,"verifyTime":24,"verifyNote":24,"syncStatus":23,"languages":24,"translateLanguages":24,"viewCount":25},"28942e79-89b9-4e48-b062-8225944ac429","2024-04-09T20:32:53.228+00:00","2025-02-11T03:17:03.374+00:00",[],"MRC-Laboratory-of-Molecular-Biology-Cambridge-UK",{"title":3965},{"EN":3966},"MRC Laboratory of Molecular Biology, Cambridge, UK",{"openalex":3968,"orcid":3970,"title":3972},{"VOID":3969},"A5007387177",{"VOID":3971},"https:\u002F\u002Forcid.org\u002F0000-0001-7929-2162",{"EN":3973},"John E. 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J. Pathol., 134, 1167",{},{"id":24,"text":5023,"url":24,"identifiers":5024},"10.1212\u002FWNL.40.8.1231",{"doi":5023},{"id":24,"text":5026,"url":24,"identifiers":5027},"10.1038\u002F290457a0",{"doi":5026},{"id":24,"text":5029,"url":24,"identifiers":5030},"10.1016\u002FS0006-291X(05)80099-3",{"doi":5029},{"id":24,"text":5032,"url":24,"identifiers":5033},"10.1016\u002F0005-2728(87)90151-4",{"doi":5032},{"id":5035,"createTime":5036,"updateTime":5037,"relativeEntities":5038,"slug":5039,"properties":5040,"entityType":122,"verifyStatus":123,"verifyTime":5036,"verifyNote":124,"syncStatus":23,"languages":5057,"translateLanguages":5058,"viewCount":25,"primaryUrl":5060,"fullTextUrl":24,"authors":5061,"publicationType":172,"publisherRelationship":5104,"citationCount":5136,"citationInfo":5137,"publishDate":5143,"publishYear":5144,"citationAnalyzeStatus":23,"lastCitationAnalyze":24,"indexDatabases":24,"openAccess":24,"references":5145,"isForceReanalyzing":918},"cbb60079-1ae5-48df-a9b6-f5c33a7c6b12","2024-09-03T05:52:03.400+00:00","2024-12-24T17:33:39.324+00:00",[],"Are-amyloid-diseases-caused-by-protein-aggregates-that-mimic-bacterial-pore-forming-toxins-",{"mag":5041,"keywords":5043,"openalex":5045,"abstract":5047,"title":5050,"pm":5053,"doi":5055},{"VOID":5042},"2129583700",{"VI":5044},"Amyloid diseases, protein fibrillization, protofibrils, neurodegenerative diseases, amyloid pore, protein aggregation, pathogenesis, membrane permeabilization, proteasome inhibition",{"VOID":5046},"W2129583700",{"EN":5048,"VI":5049},"\u003Cjats:p>\u003Cjats:bold>1. Introduction 2\u003C\u002Fjats:bold>\u003C\u002Fjats:p>\u003Cjats:p>\u003Cjats:bold>2. What is the significance of the shared structural properties of disease-associated protein fibrils? 3\u003C\u002Fjats:bold>\u003C\u002Fjats:p>\u003Cjats:p>2.1 Mechanism of amyloid fibril formation \u003Cjats:italic>in vitro\u003C\u002Fjats:italic> 6\u003C\u002Fjats:p>\u003Cjats:p>2.1.1 \u003Cjats:italic>In vitro\u003C\u002Fjats:italic> fibril formation involves transient population of ordered aggregates of intermediate stability, or protofibrils 6\u003C\u002Fjats:p>\u003Cjats:p>\u003Cjats:bold>3. Toxic properties of protofibrils 7\u003C\u002Fjats:bold>\u003C\u002Fjats:p>\u003Cjats:p>3.1 Protofibrils, rather than fibrils, are likely to be pathogenic 7\u003C\u002Fjats:p>\u003Cjats:p>3.2 The toxic protofibril may be a mixture of related species 8\u003C\u002Fjats:p>\u003Cjats:p>3.3 Morphological similarities of protofibrils suggest a common mechanism of toxicity 9\u003C\u002Fjats:p>\u003Cjats:p>3.4 Are the amyloid diseases a subset of a much larger class of previously unrecognized protofibril diseases? 9\u003C\u002Fjats:p>\u003Cjats:p>3.5 Fibrils, in the form of aggresomes, may function to sequester toxic protofibrils 9\u003C\u002Fjats:p>\u003Cjats:p>\u003Cjats:bold>4. Amyloid pores, a common structural link among protein aggregation neurodegenerative diseases 10\u003C\u002Fjats:bold>\u003C\u002Fjats:p>\u003Cjats:p>4.1 Mechanistic studies of amyloid fibril formation reveal common features, including pore-like protofibrils 10\u003C\u002Fjats:p>\u003Cjats:p>4.1.1 Amyloid-β (Aβ) (Alzheimer's disease) 10\u003C\u002Fjats:p>\u003Cjats:p>4.1.2 α-Synuclein (PD and diffuse Lewy body disease) 12\u003C\u002Fjats:p>\u003Cjats:p>4.1.3 ABri (familial British dementia) 13\u003C\u002Fjats:p>\u003Cjats:p>4.1.4 Superoxide dismutase-1 (amyotrophic lateral sclerosis) 13\u003C\u002Fjats:p>\u003Cjats:p>4.1.5 Prion protein (Creutzfeldt–Jakob disease, bovine spongiform encephalopathy, etc.) 14\u003C\u002Fjats:p>\u003Cjats:p>4.1.6 Huntingtin (Huntington's disease) 14\u003C\u002Fjats:p>\u003Cjats:p>4.2 Amyloidogenic proteins that are not linked to disease also from pore-like protofibrils 15\u003C\u002Fjats:p>\u003Cjats:p>4.3 Amyloid proteins form non-fibrillar aggregates that have properties of protein channels or pores 15\u003C\u002Fjats:p>\u003Cjats:p>4.3.1 Aβ ‘channels’ 15\u003C\u002Fjats:p>\u003Cjats:p>4.3.2 α-Synuclein ‘pores’ 16\u003C\u002Fjats:p>\u003Cjats:p>4.3.3 PrP ‘channels’ 16\u003C\u002Fjats:p>\u003Cjats:p>4.3.4 Polyglutamine ‘channels’ 17\u003C\u002Fjats:p>\u003Cjats:p>4.4 Nature uses β-strand-mediated protein oligomerization to construct pore-forming toxins 17\u003C\u002Fjats:p>\u003Cjats:p>\u003Cjats:bold>5. Mechanisms of protofibril induced toxicity in protein aggregation diseases 19\u003C\u002Fjats:bold>\u003C\u002Fjats:p>\u003Cjats:p>5.1 The amyloid pore can explain the age-association and cell-type selectivity of the neurodegenerative diseases 19\u003C\u002Fjats:p>\u003Cjats:p>5.2 Protofibrils may promote their own accumulation by inhibiting the proteasome 20\u003C\u002Fjats:p>\u003Cjats:p>\u003Cjats:bold>6. Testing the amyloid pore hypothesis by attempting to disprove it 21\u003C\u002Fjats:bold>\u003C\u002Fjats:p>\u003Cjats:p>\u003Cjats:bold>7. Acknowledgments 22\u003C\u002Fjats:bold>\u003C\u002Fjats:p>\u003Cjats:p>\u003Cjats:bold>8. References 22\u003C\u002Fjats:bold>\u003C\u002Fjats:p>\u003Cjats:p>Protein fibrillization is implicated in the pathogenesis of most, if not all, age-associated neurodegenerative diseases, but the mechanism(s) by which it triggers neuronal death is unknown. Reductionist \u003Cjats:italic>in vitro\u003C\u002Fjats:italic> studies suggest that the amyloid protofibril may be the toxic species and that it may amplify itself by inhibiting proteasome-dependent protein degradation. Although its pathogenic target has not been identified, the properties of the protofibril suggest that neurons could be killed by unregulated membrane permeabilization, possibly by a type of protofibril referred to here as the ‘amyloid pore’. The purpose of this review is to summarize the existing supportive circumstantial evidence and to stimulate further studies designed to test the validity of this hypothesis.\u003C\u002Fjats:p>","\u003Cjats:p>\u003Cjats:bold>1. Giới thiệu 2\u003C\u002Fjats:bold>\u003C\u002Fjats:p>\u003Cjats:p>\u003Cjats:bold>2. Ý nghĩa của các đặc tính cấu trúc chung của các sợi amyloid liên quan đến bệnh? 3\u003C\u002Fjats:bold>\u003C\u002Fjats:p>\u003Cjats:p>2.1 Cơ chế hình thành sợi amyloid \u003Cjats:italic>in vitro\u003C\u002Fjats:italic> 6\u003C\u002Fjats:p>\u003Cjats:p>2.1.1 Quá trình hình thành sợi \u003Cjats:italic>in vitro\u003C\u002Fjats:italic> bao gồm sự tập hợp tạm thời của các chất kết tập có độ ổn định trung gian, hoặc protofibrils 6\u003C\u002Fjats:p>\u003Cjats:p>\u003Cjats:bold>3. Các đặc tính độc hại của protofibrils 7\u003C\u002Fjats:bold>\u003C\u002Fjats:p>\u003Cjats:p>3.1 Các protofibrils, chứ không phải sợi fibrils, có khả năng là chất gây bệnh 7\u003C\u002Fjats:p>\u003Cjats:p>3.2 Protofibrils độc hại có thể là một hỗn hợp của các loài liên quan 8\u003C\u002Fjats:p>\u003Cjats:p>3.3 Các đặc điểm hình thái của protofibrils gợi ý một cơ chế độc tính chung 9\u003C\u002Fjats:p>\u003Cjats:p>3.4 Liệu các bệnh amyloid có phải là một tập hợp con của một lớp bệnh protofibrils lớn hơn chưa được công nhận? 9\u003C\u002Fjats:p>\u003Cjats:p>3.5 Sợi fibrils, dưới dạng aggresomes, có thể hoạt động để cô lại các protofibrils độc hại 9\u003C\u002Fjats:p>\u003Cjats:p>\u003Cjats:bold>4. Lỗ amyloid, một liên kết cấu trúc chung giữa các bệnh thoái hóa thần kinh do kết tập protein 10\u003C\u002Fjats:bold>\u003C\u002Fjats:p>\u003Cjats:p>4.1 Các nghiên cứu cơ chế về sự hình thành sợi amyloid tiết lộ các đặc điểm chung, bao gồm protofibrils giống như lỗ 10\u003C\u002Fjats:p>\u003Cjats:p>4.1.1 Amyloid-β (Aβ) (bệnh Alzheimer) 10\u003C\u002Fjats:p>\u003Cjats:p>4.1.2 α-Synuclein (bệnh Parkinson và bệnh thể Lewy lan tỏa) 12\u003C\u002Fjats:p>\u003Cjats:p>4.1.3 ABri (bệnh mất trí nhớ gia đình Anh) 13\u003C\u002Fjats:p>\u003Cjats:p>4.1.4 Superoxide dismutase-1 (bệnh xơ cứng teo cơ một bên - ALS) 13\u003C\u002Fjats:p>\u003Cjats:p>4.1.5 Protein Prion (bệnh Creutzfeldt–Jakob, bệnh bò điên, v.v.) 14\u003C\u002Fjats:p>\u003Cjats:p>4.1.6 Huntingtin (bệnh Huntington) 14\u003C\u002Fjats:p>\u003Cjats:p>4.2 Các protein amyloidogenic không liên quan đến bệnh cũng hình thành protofibrils giống lỗ 15\u003C\u002Fjats:p>\u003Cjats:p>4.3 Các protein amyloid hình thành các chất kết tập không theo dạng sợi có đặc tính của kênh protein hoặc lỗ 15\u003C\u002Fjats:p>\u003Cjats:p>4.3.1 Kênh Aβ 15\u003C\u002Fjats:p>\u003Cjats:p>4.3.2 Lỗ α-Synuclein 16\u003C\u002Fjats:p>\u003Cjats:p>4.3.3 Kênh PrP 16\u003C\u002Fjats:p>\u003Cjats:p>4.3.4 Kênh Polyglutamine 17\u003C\u002Fjats:p>\u003Cjats:p>4.4 Tự nhiên sử dụng dây β để tạo độc tố tạo lỗ protein bằng cách liên kết các phân tử protein 17\u003C\u002Fjats:p>\u003Cjats:p>\u003Cjats:bold>5. Cơ chế độc tính gây ra bởi protofibrils trong các bệnh kết tập protein 19\u003C\u002Fjats:bold>\u003C\u002Fjats:p>\u003Cjats:p>5.1 Lỗ amyloid có thể giải thích sự liên quan đến tuổi và tính chọn lọc của các bệnh thoái hóa thần kinh 19\u003C\u002Fjats:p>\u003Cjats:p>5.2 Protofibrils có thể thúc đẩy sự tích lũy của chính nó bằng cách ức chế proteasome 20\u003C\u002Fjats:p>\u003Cjats:p>\u003Cjats:bold>6. Kiểm tra giả thuyết lỗ amyloid bằng cách cố thử chứng minh nó sai 21\u003C\u002Fjats:bold>\u003C\u002Fjats:p>\u003Cjats:p>\u003Cjats:bold>7. Lời cảm ơn 22\u003C\u002Fjats:bold>\u003C\u002Fjats:p>\u003Cjats:p>\u003Cjats:bold>8. Tài liệu tham khảo 22\u003C\u002Fjats:bold>\u003C\u002Fjats:p>\u003Cjats:p>Sự kết tụ protein có liên quan đến cơ chế bệnh sinh của hầu hết, nếu không muốn nói là tất cả, các bệnh thoái hóa thần kinh gắn với tuổi tác. Tuy nhiên, cơ chế mà bằng cách nào nó kích hoạt cái chết của tế bào thần kinh vẫn chưa được biết. Các nghiên cứu \u003Cjats:italic>in vitro\u003C\u002Fjats:italic> theo hướng làm giảm các yếu tố gợi ý rằng protofibril amyloid có thể là loài độc hại và nó có thể tự khuếch đại bằng cách ức chế sự phân giải protein phụ thuộc vào proteasome. Mặc dù mục tiêu gây bệnh của nó vẫn chưa được xác định, các đặc tính của protofibril gợi ý rằng các tế bào thần kinh có thể bị tiêu diệt bởi sự thấm màng mà không được kiểm soát, có thể do một loại protofibril được gọi là “lỗ amyloid\". Mục đích của bài đánh giá này là tóm tắt bằng chứng hỗ trợ hiện có và khuyến khích các nghiên cứu tiếp theo nhằm kiểm tra tính hợp lý của giả thuyết này.\u003C\u002Fjats:p>",{"EN":5051,"VI":5052},"Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?","Các bệnh amyloid có phải được gây ra bởi các protein kết tập bắt chước độc tố tạo lỗ trên vi khuẩn hay không?",{"VOID":5054},"16978447",{"VOID":5056},"10.1017\u002Fs0033583506004422",[126],[5059],"VI","https:\u002F\u002Fwww.cambridge.org\u002Fcore\u002Fproduct\u002Fidentifier\u002FS0033583506004422\u002Ftype\u002Fjournal_article",[5062,5083],{"id":5063,"sortIndex":131,"researcher":24,"roles":5064,"affiliations":5065,"properties":5076},"64089633-cdd8-4d42-a973-fa5a6987ff11",[],[5066],{"id":5067,"sortIndex":25,"affiliation":5068,"properties":24},"50afc453-ef0a-49f5-a7d5-b87a80169815",{"id":5069,"createTime":5070,"updateTime":5070,"relativeEntities":5071,"slug":5072,"properties":5073,"entityType":45,"verifyStatus":23,"verifyTime":24,"verifyNote":24,"syncStatus":23,"languages":24,"translateLanguages":24,"viewCount":25},"0f68d901-3487-47a0-8a6f-1a707df81f9e","2024-09-03T05:52:03.451+00:00",[],"Harvard-Center-for-Neurodegeneration-and-Repair-Center-for-Neurologic-Diseases-Brigham-and-Women-s-Hospital-and-Department-of-Neurology-Harvard-Medical-School-65-Landsdowne-St-Cambridge-MA-02139-USA",{"title":5074},{"EN":5075},"Harvard Center for Neurodegeneration and Repair, Center for Neurologic Diseases, Brigham and Women's Hospital and Department of Neurology, Harvard Medical School, 65 Landsdowne St, Cambridge, MA 02139, USA",{"openalex":5077,"orcid":5079,"title":5081},{"VOID":5078},"A5005020605",{"VOID":5080},"https:\u002F\u002Forcid.org\u002F0000-0001-6462-5024",{"EN":5082},"Peter T. 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