The interaction of the antitoxin DM43 with a snake venom metalloproteinase analyzed by mass spectrometry and surface plasmon resonance.

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Natural Inhibitors of Snake Venom Metalloendopeptidases: History and Current Challenges Using mass spectrometry to explore the neglected glycan moieties of the antiophidic proteins DM43 and DM64.Natural Inhibitors of Snake Venom Metallopeptidases Antibody Cross-Reactivity in Antivenom Research

P2860

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P2860

The interaction of the antitoxin DM43 with a snake venom metalloproteinase analyzed by mass spectrometry and surface plasmon resonance.

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http://www.wikidata.org/entity/Q51540222

description

2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

@zh-cn

2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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2012年學術文章

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name

The interaction of the antitox ...... and surface plasmon resonance.

@en

The interaction of the antitox ...... and surface plasmon resonance.

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type

Item

label

The interaction of the antitox ...... and surface plasmon resonance.

@en

The interaction of the antitox ...... and surface plasmon resonance.

@nl

prefLabel

The interaction of the antitox ...... and surface plasmon resonance.

@en

The interaction of the antitox ...... and surface plasmon resonance.

@nl

P1476

The interaction of the antitox ...... and surface plasmon resonance.

@en

P2093

Ana G C Neves-Ferreira

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

Ana M Moura-da-Silva

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

Carlos Bloch

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

Gilberto B Domont

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

Isabelle Tanjoni

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

Peter Roepstorff

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

Rune Salbo

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

Thomas J D Jørgensen

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

P2860

Diversity of protein-protein interactions

The three-dimensional structure of bothropasin, the main hemorrhagic factor from Bothrops jararaca venom: insights for a new classification of snake venom metalloprotease subgroups

Principles of protein-protein interactions

E. coli expression of TIMP-4 and comparative kinetic studies with TIMP-1 and TIMP-2: insights into the interactions of TIMPs and matrix metalloproteinase 2 (gelatinase A)

Structural features of the reprolysin atrolysin C and tissue inhibitors of metalloproteinases (TIMPs) interaction.

Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity.

Structural and functional analyses of DM43, a snake venom metalloproteinase inhibitor from Didelphis marsupialis serum.

Probing the hydrophobic effect of noncovalent complexes by mass spectrometry.

Functional analysis of DM64, an antimyotoxic protein with immunoglobulin-like structure from Didelphis marsupialis serum.

Interpreting kinetic rate constants from optical biosensor data recorded on a decaying surface.

P304

567-573

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P31

scholarly article

P356

10.1002/JMS.2990

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P433

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

P478

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

P50

Richard H Valente

Carol V. Robinson

Guilherme D Brand

Elisabetta Boeri Erba

Jonas Perales

P577

2012-05-01T00:00:00Z

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P5875

224879161

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P698

22549991

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The interaction of the antitoxin DM43 with a snake venom metalloproteinase analyzed by mass spectrometry and surface plasmon resonance.

about

P2860

P2860

The interaction of the antitoxin DM43 with a snake venom metalloproteinase analyzed by mass spectrometry and surface plasmon resonance.

description

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P1433

P1476

P2093

P2860

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P2860

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P698