In-Silico Identification of SOD1 Exposed Dimer Interface which Binds a Novel Computationally Designed HTB1 Binding Protein in ALS SOD1 Mutants

Efrat Ben-Zeev; Niv Papo; Victor Banerje; Ofek Oren; Ran Taube; Stanislav Engel

In-Silico Identification of SOD1 Exposed Dimer Interface which Binds a Novel Computationally Designed HTB1 Binding Protein in ALS SOD1 Mutants

Efrat Ben-Zeev
, Niv Papo
, Victor Banerje
, Ofek Oren
, Ran Taube
, Stanislav Engel

Research output: Contribution to journal › Meeting Abstract

Abstract

Amyotrophic lateral sclerosis (ALS) is a devastating motor neuron disease resulting in paralysis and
death, usually within 3–5 years of diagnosis. Misfolding of Cu/Zn-superoxide dismutase (SOD1) is
emerging as a mechanism underlying motor neuron degeneration in individuals with amyotrophic lateral sclerosis (ALS) who carry a mutant SOD1 gene (ALS SOD).

Original language	English
Pages (from-to)	55-55
Number of pages	1
Journal	Protein Science
Volume	26
Issue number	S1
State	Published - Jul 2017

Cite this

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title = "In-Silico Identification of SOD1 Exposed Dimer Interface which Binds a Novel Computationally Designed HTB1 Binding Protein in ALS SOD1 Mutants",

abstract = "Amyotrophic lateral sclerosis (ALS) is a devastating motor neuron disease resulting in paralysis and death, usually within 3{\textendash}5 years of diagnosis. Misfolding of Cu/Zn-superoxide dismutase (SOD1) is emerging as a mechanism underlying motor neuron degeneration in individuals with amyotrophic lateral sclerosis (ALS) who carry a mutant SOD1 gene (ALS SOD).",

author = "Efrat Ben-Zeev and Niv Papo and Victor Banerje and Ofek Oren and Ran Taube and Stanislav Engel",

note = " Award Winners and Abstracts of the 31st Annual Symposium of The Protein Society, Montreal, Canada, July 24{\textendash}27, 2017",

year = "2017",

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language = "English",

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pages = "55--55",

journal = "Protein Science",

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T1 - In-Silico Identification of SOD1 Exposed Dimer Interface which Binds a Novel Computationally Designed HTB1 Binding Protein in ALS SOD1 Mutants

AU - Ben-Zeev, Efrat

AU - Papo, Niv

AU - Banerje, Victor

AU - Oren, Ofek

AU - Taube, Ran

AU - Engel, Stanislav

N1 - Award Winners and Abstracts of the 31st Annual Symposium of The Protein Society, Montreal, Canada, July 24–27, 2017

PY - 2017/7

Y1 - 2017/7

N2 - Amyotrophic lateral sclerosis (ALS) is a devastating motor neuron disease resulting in paralysis and death, usually within 3–5 years of diagnosis. Misfolding of Cu/Zn-superoxide dismutase (SOD1) is emerging as a mechanism underlying motor neuron degeneration in individuals with amyotrophic lateral sclerosis (ALS) who carry a mutant SOD1 gene (ALS SOD).

AB - Amyotrophic lateral sclerosis (ALS) is a devastating motor neuron disease resulting in paralysis and death, usually within 3–5 years of diagnosis. Misfolding of Cu/Zn-superoxide dismutase (SOD1) is emerging as a mechanism underlying motor neuron degeneration in individuals with amyotrophic lateral sclerosis (ALS) who carry a mutant SOD1 gene (ALS SOD).

M3 - Meeting Abstract

SN - 0961-8368

VL - 26

SP - 55

EP - 55

JO - Protein Science

JF - Protein Science

IS - S1

ER -

In-Silico Identification of SOD1 Exposed Dimer Interface which Binds a Novel Computationally Designed HTB1 Binding Protein in ALS SOD1 Mutants

Abstract

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