Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes最新文献

{"title":"Information for Contributors","authors":"","doi":"10.1016/S0304-4157(02)00017-5","DOIUrl":"https://doi.org/10.1016/S0304-4157(02)00017-5","url":null,"abstract":"","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1516 1","pages":"Pages ix-xiv"},"PeriodicalIF":0.0,"publicationDate":"2002-05-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(02)00017-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72277663","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Author Index 1972–2000","authors":"","doi":"10.1016/S0304-4157(02)00019-9","DOIUrl":"https://doi.org/10.1016/S0304-4157(02)00019-9","url":null,"abstract":"","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1516 1","pages":"Pages 3-22"},"PeriodicalIF":0.0,"publicationDate":"2002-05-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(02)00019-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136549848","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Subject Index 1972–2000","authors":"","doi":"10.1016/S0304-4157(02)00021-7","DOIUrl":"https://doi.org/10.1016/S0304-4157(02)00021-7","url":null,"abstract":"","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1516 1","pages":"Pages 25-298"},"PeriodicalIF":0.0,"publicationDate":"2002-05-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(02)00021-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136549849","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Maturation of HIV envelope glycoprotein precursors by cellular endoproteases","authors":"Maxime Moulard ,&nbsp;Etienne Decroly","doi":"10.1016/S0304-4157(00)00014-9","DOIUrl":"10.1016/S0304-4157(00)00014-9","url":null,"abstract":"<div><p><span><span>The entry of enveloped viruses into its host cells is a crucial step for the propagation of viral infection. The envelope glycoprotein<span> complex controls viral tropism and promotes the </span></span>membrane fusion process. The surface glycoproteins of enveloped viruses are synthesized as inactive precursors and sorted through the constitutive </span>secretory pathway<span><span><span><span> of the infected cells. To be infectious, most of the viruses require viral envelope glycoprotein maturation by host cell endoproteases. In spite of the strong variability of primary sequences observed within different viral envelope glycoproteins, the endoproteolytical cleavage occurs mainly in a highly conserved domain at the carboxy terminus of the basic consensus sequence (Arg-X-Lys/Arg-Arg↓). The same consensus sequence is recognized by the kexin/subtilisin-like </span>serine proteinases (so called convertases) in many cellular substrates such as prohormones, proprotein of receptors, </span>plasma proteins<span><span>, growth factors and bacterial toxins. Therefore, several groups of investigators have evaluated the implication of convertases in viral envelope glycoprotein cleavage. Using the </span>vaccinia virus<span> overexpression system, furin was first shown to mediate the proteolytic maturation of both human immunodeficiency virus (HIV-1) and influenza virus envelope glycoproteins. </span></span></span>In vitro studies<span><span> demonstrated that purified convertases directly and specifically cleave viral envelope glycoproteins. Although these studies suggested the participation of several enzymes belonging to the convertases family, recent data suggest that other protease families may also participate in the HIV envelope glycoprotein processing. Their role in the physiological maturation process is still hypothetical and the molecular mechanism of the cleavage is not well documented. Crystallization of the hemagglutinin precursor (HA0) of influenza virus allowed further understanding of the </span>molecular interaction<span> between viral precursors and the cellular endoproteases. Furthermore, relationships between differential pathogenicity of influenza strains and their susceptibility to cleavage are molecularly funded. Here we review the most recent data and recent insights demonstrating the crucial role played by this activation step in virus infectivity<span>. We discuss the cellular endoproteases that are implicated in HIV gp160 endoproteolytical maturation into gp120 and gp41.</span></span></span></span></p></div>","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1469 3","pages":"Pages 121-132"},"PeriodicalIF":0.0,"publicationDate":"2000-11-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(00)00014-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21890953","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structure of lipid bilayers","authors":"John F. Nagle ,&nbsp;Stephanie Tristram-Nagle","doi":"10.1016/S0304-4157(00)00016-2","DOIUrl":"10.1016/S0304-4157(00)00016-2","url":null,"abstract":"<div><p>The quantitative experimental uncertainty in the structure of fully hydrated, biologically relevant, fluid (<em>L</em>_α<span>) phase lipid bilayers has been too large to provide a firm base for applications or for comparison with simulations. Many structural methods are reviewed including modern liquid crystallography of lipid bilayers that deals with the fully developed undulation fluctuations that occur in the </span><em>L</em>_α<span> phase. These fluctuations degrade the higher order diffraction data in a way that, if unrecognized, leads to erroneous conclusions regarding bilayer structure. Diffraction measurements at high instrumental resolution provide a measure of these fluctuations. In addition to providing better structural determination, this opens a new window on interactions between bilayers, so the experimental determination of interbilayer interaction parameters is reviewed briefly. We introduce a new structural correction based on fluctuations that has not been included in any previous studies. Updated measurements, such as for the area compressibility modulus, are used to provide adjustments to many of the literature values of structural quantities. Since the gel (</span><em>L</em>_β′) phase is valuable as a stepping stone for obtaining fluid phase results, a brief review is given of the lower temperature phases. The uncertainty in structural results for lipid bilayers is being reduced and best current values are provided for bilayers of five lipids.</p></div>","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1469 3","pages":"Pages 159-195"},"PeriodicalIF":0.0,"publicationDate":"2000-11-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(00)00016-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21890956","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mutagenic study of the structure, function and biogenesis of the yeast plasma membrane H+-ATPase","authors":"Pierre Morsomme ,&nbsp;Carolyn W Slayman ,&nbsp;André Goffeau","doi":"10.1016/S0304-4157(00)00015-0","DOIUrl":"10.1016/S0304-4157(00)00015-0","url":null,"abstract":"","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1469 3","pages":"Pages 133-157"},"PeriodicalIF":0.0,"publicationDate":"2000-11-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(00)00015-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21890954","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Dynamics of the mammalian sperm plasma membrane in the process of fertilization","authors":"Frits M Flesch,&nbsp;Barend M Gadella","doi":"10.1016/S0304-4157(00)00018-6","DOIUrl":"10.1016/S0304-4157(00)00018-6","url":null,"abstract":"<div><p><span><span>Sexual reproduction requires the fusion of sperm cell and oocyte during fertilization to produce the diploid zygote. In mammals complex changes in the plasma membrane of the sperm cell are involved in this process. Sperm cells have unusual membranes compared to those of somatic cells. After leaving the testes, sperm cells cease plasma membrane lipid and </span>protein synthesis<span><span>, and vesicle mediated transport. Biophysical studies reveal that lipids and proteins are organized into lateral regions of the sperm head surface. A delicate reorientation and modification of plasma membrane molecules take place in the female tract when sperm cells are activated by so-called capacitation factors. These surface changes enable the sperm cell to bind to the extra cellular matrix of the egg (zona pellucida, ZP). The ZP primes the sperm cell to initiate the acrosome reaction, which is an exocytotic process that makes available the enzymatic machinery required for </span>sperm penetration through the ZP. After complete penetration the sperm cell meets the plasma membrane of the egg cell (oolemma). A specific set of molecules is involved in a disintegrin–integrin type of anchoring of the two </span></span>gametes which is completed by fusion of the two gamete plasma membranes. The fertilized egg is activated and zygote formation preludes the development of a new living organism. In this review we focus on the involvement of processes that occur at the sperm plasma membrane in the sequence of events that lead to successful fertilization. For this purpose, dynamics in adhesive and fusion properties, molecular composition and architecture of the sperm plasma membrane, as well as membrane derived signalling are reviewed.</p></div>","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1469 3","pages":"Pages 197-235"},"PeriodicalIF":0.0,"publicationDate":"2000-11-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(00)00018-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21890955","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The amoebapore superfamily","authors":"Yufeng Zhai,&nbsp;Milton H Saier Jr.","doi":"10.1016/S0304-4157(00)00003-4","DOIUrl":"10.1016/S0304-4157(00)00003-4","url":null,"abstract":"<div><p><span><span>Amoebapores, synthesized by human protozoan parasites, form ion channels in target cells and artificial lipid membranes<span>. The major pathogenic effect of these proteins is due to their cytolytic capability which results in target cell death. They comprise a coherent family and are homologous to other proteins and protein domains<span> found in eight families. These families include in addition to the amoebapores (1) the saposins, (2) the NK-lysins and granulysins, (3) the pulmonary surfactant proteins B, (4) the </span></span></span>acid sphingomyelinases<span><span>, (5) acyloxyacyl hydrolases and (6) the aspartic proteases. These amoebapore homologues have many properties in common including </span>membrane binding and stability. We note for the first time that a new protein, countin, from the cellular slime mold, </span></span><span><em>Dictyostelium discoideum</em></span><span>, comprises the eighth family within this superfamily. All currently sequenced members of these eight families are identified, and the structural, functional and phylogenetic properties of these proteins are discussed.</span></p></div>","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1469 2","pages":"Pages 87-99"},"PeriodicalIF":0.0,"publicationDate":"2000-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(00)00003-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21831183","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Intracellular lipid particles of eukaryotic cells","authors":"Dagmar Zweytick,&nbsp;Karin Athenstaedt,&nbsp;Günther Daum","doi":"10.1016/S0005-2736(00)00294-7","DOIUrl":"10.1016/S0005-2736(00)00294-7","url":null,"abstract":"<div><p><span>In this review article we describe characterization of intracellular lipid particles of three different eukaryotic species, namely mammalian cells, plants and yeast. Lipid particles of all types of cells share a general structure. A hydrophobic core of </span>neutral lipids<span><span> is surrounded by a membrane monolayer of phospholipids which contains a minor amount of proteins. Whereas lipid particles from mammalian cells and plants harbor specific classes of polypeptides, mainly perilipins and oleosins, respectively, yeast lipid particles contain a more complex set of enzymes which are involved in </span>lipid biosynthesis<span>. Function of lipid particles as storage compartment and metabolic organelle, and their interaction with other subcellular fractions are discussed. Furthermore, models for the biogenesis of lipid particles are presented and compared among the different species.</span></span></p></div>","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1469 2","pages":"Pages 101-120"},"PeriodicalIF":0.0,"publicationDate":"2000-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0005-2736(00)00294-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21831184","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Hydrophobins, the fungal coat unravelled","authors":"Han A.B. Wösten ,&nbsp;Marcel L. de Vocht","doi":"10.1016/S0304-4157(00)00002-2","DOIUrl":"10.1016/S0304-4157(00)00002-2","url":null,"abstract":"<div><p>Hydrophobins are among the most surface active molecules and self-assemble at any hydrophilic–hydrophobic interface into an amphipathic film. These small secreted proteins of about 100 amino acids can be used to make hydrophilic surfaces hydrophobic and hydrophobic surfaces hydrophilic. Although differences in the biophysical properties of hydrophobins have not yet been related to differences in primary structure<span> it has been established that the N-terminal part, at least partly, determines wettability of the hydrophilic side of the assemblage, while the eight conserved cysteine residues that form four disulphide bridges prevent self-assembly of the hydrophobin in the absence of a hydrophilic–hydrophobic interface. Three conformations of class I hydrophobins have been identified: the monomeric state, which is soluble in water, the α-helical state, which is the result of self-assembly at a hydrophobic solid, and the β-sheet state, which is formed during self-assembly at the water–air interface. Experimental evidence strongly indicates that the α-helical state is an intermediate and that the β-sheet state is the end form of assembly. The latter state has a typical ultrastructure of a mosaic of 10 nm wide rodlets, which have been shown to resemble the amyloid fibrils.</span></p></div>","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1469 2","pages":"Pages 79-86"},"PeriodicalIF":0.0,"publicationDate":"2000-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(00)00002-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21831182","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}