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Flexible viruses [[electronic resource] ] : structural disorder in viral proteins / / edited by Vladimir Uversky, Sonia Longhi
Flexible viruses [[electronic resource] ] : structural disorder in viral proteins / / edited by Vladimir Uversky, Sonia Longhi
Autore Uversky Vladimir N
Pubbl/distr/stampa Hoboken, N.J., : Wiley, c2012
Descrizione fisica 1 online resource (534 p.)
Disciplina 612/.015756
Altri autori (Persone) LonghiSonia
Collana Wiley series in protein and peptide science
Soggetto topico Viral proteins
ISBN 1-283-31596-3
9786613315960
1-118-13556-3
1-118-13557-1
1-118-13554-7
Classificazione SCI007000
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto FLEXIBLE VIRUSES; CONTENTS; Preface; Introduction to the Wiley Series on Protein and Peptide Science; Contributors; 1 Do Viral Proteins Possess Unique Features?; 2 Functional Role of Structural Disorder in Capsid Proteins; 3 Structural Disorder Within the Nucleoprotein and Phosphoprotein from Measles, Nipah, and Hendra Viruses; 4 Structural Disorder Within Sendai Virus Nucleoprotein and Phosphoprotein; 5 Structural Disorder in Proteins of the Rhabdoviridae Replication Complex; 6 Structural Disorder in Matrix Proteins of HIV-Related Viruses
7 Structural Disorder in Proteins From Influenza Virus8 Making Order in the Intrinsically Disordered Regions of HIV-1 Vif Protein; 9 Order from Disorder: Structure, Function, and Dynamics of the HIV-1 Transactivator of Transcription; 10 Intrinsically Disordered Domains of Sesbania Mosaic Virus Encoded Proteins; 11 Intrinsic Disorder in Genome-Linked Viral Proteins VPgs of Potyviruses; 12 Intrinsic Disorder in the Human Papillomavirus E7 Protein; 13 The Semliki Forest Virus Capsid Protease is Disordered and Yet Displays Catalytic Activity
14 Core-lations Between Intrinsic Disorder and Multifaceted Activities in Hepatitis C Virus and Related Viruses15 The NS5A Domain II of HCV: Conservation of Intrinsic Disorder in Several Genotypes; 16 Bacteriophage l N Protein Disorder-Order Transitions Upon Interactions with RNA or Proteins; 17 N-Terminal Extension Region of Hordeivirus Movement TGB1 Protein Consists of Two Domains with Different Content of Disordered Structure; Index
Record Nr. UNINA-9910141216203321
Uversky Vladimir N  
Hoboken, N.J., : Wiley, c2012
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Flexible viruses : structural disorder in viral proteins / / edited by Vladimir Uversky, Sonia Longhi
Flexible viruses : structural disorder in viral proteins / / edited by Vladimir Uversky, Sonia Longhi
Autore Uversky Vladimir N
Edizione [1st ed.]
Pubbl/distr/stampa Hoboken, N.J., : Wiley, c2012
Descrizione fisica 1 online resource (534 p.)
Disciplina 612/.015756
Altri autori (Persone) LonghiSonia
Collana Wiley series in protein and peptide science
Soggetto topico Viral proteins
ISBN 1-283-31596-3
9786613315960
1-118-13556-3
1-118-13557-1
1-118-13554-7
Classificazione SCI007000
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto FLEXIBLE VIRUSES; CONTENTS; Preface; Introduction to the Wiley Series on Protein and Peptide Science; Contributors; 1 Do Viral Proteins Possess Unique Features?; 2 Functional Role of Structural Disorder in Capsid Proteins; 3 Structural Disorder Within the Nucleoprotein and Phosphoprotein from Measles, Nipah, and Hendra Viruses; 4 Structural Disorder Within Sendai Virus Nucleoprotein and Phosphoprotein; 5 Structural Disorder in Proteins of the Rhabdoviridae Replication Complex; 6 Structural Disorder in Matrix Proteins of HIV-Related Viruses
7 Structural Disorder in Proteins From Influenza Virus8 Making Order in the Intrinsically Disordered Regions of HIV-1 Vif Protein; 9 Order from Disorder: Structure, Function, and Dynamics of the HIV-1 Transactivator of Transcription; 10 Intrinsically Disordered Domains of Sesbania Mosaic Virus Encoded Proteins; 11 Intrinsic Disorder in Genome-Linked Viral Proteins VPgs of Potyviruses; 12 Intrinsic Disorder in the Human Papillomavirus E7 Protein; 13 The Semliki Forest Virus Capsid Protease is Disordered and Yet Displays Catalytic Activity
14 Core-lations Between Intrinsic Disorder and Multifaceted Activities in Hepatitis C Virus and Related Viruses15 The NS5A Domain II of HCV: Conservation of Intrinsic Disorder in Several Genotypes; 16 Bacteriophage l N Protein Disorder-Order Transitions Upon Interactions with RNA or Proteins; 17 N-Terminal Extension Region of Hordeivirus Movement TGB1 Protein Consists of Two Domains with Different Content of Disordered Structure; Index
Record Nr. UNINA-9910809692803321
Uversky Vladimir N  
Hoboken, N.J., : Wiley, c2012
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Intrinsically Disordered Proteins / / by Vladimir N. Uversky
Intrinsically Disordered Proteins / / by Vladimir N. Uversky
Autore Uversky Vladimir N
Edizione [1st ed. 2014.]
Pubbl/distr/stampa Cham : , : Springer International Publishing : , : Imprint : Springer, , 2014
Descrizione fisica 1 online resource (73 p.)
Disciplina 572.633
Collana Protein Folding and Structure
Soggetto topico Proteins 
Medicinal chemistry
Biochemistry
Protein Structure
Medicinal Chemistry
Biochemistry, general
ISBN 3-319-08921-8
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Introducing the phenomenon of protein intrinsic disorder -- Peculiar amino acid sequences of soluble IDPs -- Natural abundance of IDPs/IDPRs -- Wavy evolution of intrinsic disorder: Reinventing the wheel -- Structural heterogeneity of IDPs: When almost everything is possible -- Typical functions of IDPs and IDPRs -- Binding promiscuity and multitude of the disorder-based binding modes -- IDPs/IDPRs in human diseases -- IDPs as potential drug targets -- Concluding remarks: Intrinsic disorder as a universal tool for solving protein mysteries and riddles.
Record Nr. UNINA-9910298327903321
Uversky Vladimir N  
Cham : , : Springer International Publishing : , : Imprint : Springer, , 2014
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui