Advantage of being a dimer for Serratia marcescens endonuclease

about

The binding process of a nonspecific enzyme with DNA.Homodimerisation-independent cleavage of dsRNA by a pestiviral nicking endoribonuclease.Endonuclease from Gram-Negative Bacteria Serratia marcescens Is as Effective as Pulmozyme in the Hydrolysis of DNA in Sputum.

P2860

Q35187681-FE647E60-6AF1-4368-945B-14850C241F04 Q54940015-899D7809-F0EC-4C1C-9A79-B3132B47A554 Q55354184-D271CD36-9C4C-46EC-9F3B-894F47DB44F6

P2860

Advantage of being a dimer for Serratia marcescens endonuclease

Item

http://www.wikidata.org/entity/Q37104807

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on January 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Advantage of being a dimer for Serratia marcescens endonuclease

@en

Advantage of being a dimer for Serratia marcescens endonuclease.

@nl

type

Item

label

Advantage of being a dimer for Serratia marcescens endonuclease

@en

Advantage of being a dimer for Serratia marcescens endonuclease.

@nl

prefLabel

Advantage of being a dimer for Serratia marcescens endonuclease

@en

Advantage of being a dimer for Serratia marcescens endonuclease.

@nl

P1476

Advantage of being a dimer for Serratia marcescens endonuclease

@en

P2093

B Montgomery Pettitt

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

Chuanying Chen

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

Kurt Krause

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

P2860

Electrostatics of nanosystems: application to microtubules and the ribosome

The active site of Serratia endonuclease contains a conserved magnesium-water cluster

Atomic structure of the Serratia marcescens endonuclease at 1.1 A resolution and the enzyme reaction mechanism

The crystal structure of the nuclease domain of colicin E7 suggests a mechanism for binding to double-stranded DNA by the H-N-H endonucleases

DNA binding and cleavage by the periplasmic nuclease Vvn: a novel structure with a known active site

DNA binding and degradation by the HNH protein ColE7

Structure of Bam HI endonuclease bound to DNA: partial folding and unfolding on DNA binding

All-atom empirical potential for molecular modeling and dynamics studies of proteins

VMD: visual molecular dynamics

Thermodynamic and kinetic analyses for understanding sequence-specific DNA recognition.

P304

511-521

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

P31

scholarly article

P356

10.1021/JP8057838

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

P407

English

P433

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

P478

113

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

P577

2009-01-01T00:00:00Z

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

P5875

23568658

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

P698

19053714

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

P932

2645866

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

Advantage of being a dimer for Serratia marcescens endonuclease

about

P2860

P2860

Advantage of being a dimer for Serratia marcescens endonuclease

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P932