Modifying the vicinity of the isopeptide bond to reveal differential behavior of ubiquitin chains with interacting proteins: Organic chemistry applied to synthetic proteins

Najat Haj-Yahya; Mahmood Haj-Yahya; Carlos A. Castañeda; Liat Spasser; Hosahalli P. Hemantha; Muhammad Jbara; Marlin Penner; Aaron Ciechanover; David Fushman; Ashraf Brik

doi:10.1002/anie.201306118

Modifying the vicinity of the isopeptide bond to reveal differential behavior of ubiquitin chains with interacting proteins: Organic chemistry applied to synthetic proteins

Najat Haj-Yahya
, Mahmood Haj-Yahya
, Carlos A. Castañeda
, Liat Spasser
, Hosahalli P. Hemantha
, Muhammad Jbara
, Marlin Penner
, Aaron Ciechanover
, David Fushman
, Ashraf Brik

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

25 Scopus citations

Abstract

In every direction: Chemical protein synthesis allows the construction of 14 di-ubiquitin analogues modified in the vicinity of the isopeptide bond to examine their behavior with deubiquitinases and ubiquitin binding domains. The results set the ground for the generation of unique probes for studying the interactions of these chains with various ubiquitin-interacting proteins.

Original language	English
Pages (from-to)	11149-11153
Number of pages	5
Journal	Angewandte Chemie - International Edition
Volume	52
Issue number	42
DOIs	https://doi.org/10.1002/anie.201306118
State	Published - 11 Oct 2013

Keywords

deubiquitinases
peptide ligation
protein synthesis
ubiquitin chains
ubiquitination

ASJC Scopus subject areas

Catalysis
General Chemistry

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10.1002/anie.201306118

Cite this

Haj-Yahya, N., Haj-Yahya, M., Castañeda, C. A., Spasser, L., Hemantha, H. P., Jbara, M., Penner, M., Ciechanover, A., Fushman, D., & Brik, A. (2013). Modifying the vicinity of the isopeptide bond to reveal differential behavior of ubiquitin chains with interacting proteins: Organic chemistry applied to synthetic proteins. Angewandte Chemie - International Edition, 52(42), 11149-11153. https://doi.org/10.1002/anie.201306118

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abstract = "In every direction: Chemical protein synthesis allows the construction of 14 di-ubiquitin analogues modified in the vicinity of the isopeptide bond to examine their behavior with deubiquitinases and ubiquitin binding domains. The results set the ground for the generation of unique probes for studying the interactions of these chains with various ubiquitin-interacting proteins.",

keywords = "deubiquitinases, peptide ligation, protein synthesis, ubiquitin chains, ubiquitination",

author = "Najat Haj-Yahya and Mahmood Haj-Yahya and Casta{\~n}eda, \{Carlos A.\} and Liat Spasser and Hemantha, \{Hosahalli P.\} and Muhammad Jbara and Marlin Penner and Aaron Ciechanover and David Fushman and Ashraf Brik",

year = "2013",

month = oct,

day = "11",

doi = "10.1002/anie.201306118",

language = "English",

volume = "52",

pages = "11149--11153",

journal = "Angewandte Chemie - International Edition",

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Haj-Yahya, N, Haj-Yahya, M, Castañeda, CA, Spasser, L, Hemantha, HP, Jbara, M, Penner, M, Ciechanover, A, Fushman, D & Brik, A 2013, 'Modifying the vicinity of the isopeptide bond to reveal differential behavior of ubiquitin chains with interacting proteins: Organic chemistry applied to synthetic proteins', Angewandte Chemie - International Edition, vol. 52, no. 42, pp. 11149-11153. https://doi.org/10.1002/anie.201306118

Modifying the vicinity of the isopeptide bond to reveal differential behavior of ubiquitin chains with interacting proteins: Organic chemistry applied to synthetic proteins. / Haj-Yahya, Najat; Haj-Yahya, Mahmood; Castañeda, Carlos A. et al.
In: Angewandte Chemie - International Edition, Vol. 52, No. 42, 11.10.2013, p. 11149-11153.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Modifying the vicinity of the isopeptide bond to reveal differential behavior of ubiquitin chains with interacting proteins

T2 - Organic chemistry applied to synthetic proteins

AU - Haj-Yahya, Najat

AU - Haj-Yahya, Mahmood

AU - Castañeda, Carlos A.

AU - Spasser, Liat

AU - Hemantha, Hosahalli P.

AU - Jbara, Muhammad

AU - Penner, Marlin

AU - Ciechanover, Aaron

AU - Fushman, David

AU - Brik, Ashraf

PY - 2013/10/11

Y1 - 2013/10/11

N2 - In every direction: Chemical protein synthesis allows the construction of 14 di-ubiquitin analogues modified in the vicinity of the isopeptide bond to examine their behavior with deubiquitinases and ubiquitin binding domains. The results set the ground for the generation of unique probes for studying the interactions of these chains with various ubiquitin-interacting proteins.

AB - In every direction: Chemical protein synthesis allows the construction of 14 di-ubiquitin analogues modified in the vicinity of the isopeptide bond to examine their behavior with deubiquitinases and ubiquitin binding domains. The results set the ground for the generation of unique probes for studying the interactions of these chains with various ubiquitin-interacting proteins.

KW - deubiquitinases

KW - peptide ligation

KW - protein synthesis

KW - ubiquitin chains

KW - ubiquitination

UR - https://www.scopus.com/pages/publications/84885436866

U2 - 10.1002/anie.201306118

DO - 10.1002/anie.201306118

M3 - Article

C2 - 24006204

AN - SCOPUS:84885436866

SN - 1433-7851

VL - 52

SP - 11149

EP - 11153

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 42

ER -

Modifying the vicinity of the isopeptide bond to reveal differential behavior of ubiquitin chains with interacting proteins: Organic chemistry applied to synthetic proteins

Abstract

Keywords

ASJC Scopus subject areas

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