Importance of MHV-CoV A59 nucleocapsid protein COOH-terminal negative charges. - Wikidata - wikimedia - TriplyDB

Importance of MHV-CoV A59 nucleocapsid protein COOH-terminal negative charges.

Importance of MHV-CoV A59 nucleocapsid protein COOH-terminal negative charges.

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Expression, crystallization and preliminary crystallographic study of mouse hepatitis virus (MHV) nucleocapsid protein C-terminal domain.Structures of the N- and C-terminal domains of MHV-A59 nucleocapsid protein corroborate a conserved RNA-protein binding mechanism in coronavirus

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Importance of MHV-CoV A59 nucleocapsid protein COOH-terminal negative charges.

http://www.wikidata.org/entity/Q37150129

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article científic

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article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on January 2006

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

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name

Importance of MHV-CoV A59 nucleocapsid protein COOH-terminal negative charges.

@en

Importance of MHV-CoV A59 nucleocapsid protein COOH-terminal negative charges.

@nl

type

label

Importance of MHV-CoV A59 nucleocapsid protein COOH-terminal negative charges.

@en

Importance of MHV-CoV A59 nucleocapsid protein COOH-terminal negative charges.

@nl

prefLabel

Importance of MHV-CoV A59 nucleocapsid protein COOH-terminal negative charges.

@en

Importance of MHV-CoV A59 nucleocapsid protein COOH-terminal negative charges.

@nl

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978-0-387-33012-9_22

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Advances in Experimental Medicine and Biology

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Importance of MHV-CoV A59 nucleocapsid protein COOH-terminal negative charges.

@en

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Andrew Blount

http://www.w3.org/2001/XMLSchema#string

Brenda G Hogue

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Sandhya Verma

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Valerie Bednar

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P2860

Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures

Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins.

Selective replication of coronavirus genomes that express nucleocapsid protein

Characterization of the coronavirus M protein and nucleocapsid interaction in infected cells.

Genetic evidence for a structural interaction between the carboxy termini of the membrane and nucleocapsid proteins of mouse hepatitis virus.

Systematic assembly of a full-length infectious cDNA of mouse hepatitis virus strain A59.

Identification of functionally important negatively charged residues in the carboxy end of mouse hepatitis coronavirus A59 nucleocapsid protein.

Specific interaction between coronavirus leader RNA and nucleocapsid protein

Activation of AP-1 signal transduction pathway by SARS coronavirus nucleocapsid protein.

The membrane M protein carboxy terminus binds to transmissible gastroenteritis coronavirus core and contributes to core stability.

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127-132

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scholarly article

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10.1007/978-0-387-33012-9_22

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581

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2006-01-01T00:00:00Z

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