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Artikel ; Online: Recombinant Protein Expression in E. coli : A Historical Perspective.

Gileadi, Opher

Methods in molecular biology (Clifton, N.J.)

2017 Band 1586, Seite(n) 3–10

Abstract: This introductory chapter provides a brief historical survey of the key elements incorporated into commonly used E. coli-based expression systems. The highest impact in expression technology is associated with innovations that were based on extensively ... ...

Abstract	This introductory chapter provides a brief historical survey of the key elements incorporated into commonly used E. coli-based expression systems. The highest impact in expression technology is associated with innovations that were based on extensively studied biological systems, and where the tools were widely distributed in the academic community.
Sprache	Englisch
Erscheinungsdatum	2017
Erscheinungsland	United States
Dokumenttyp	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-6887-9_1
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: RecQ helicases in DNA repair and cancer targets.

Newman, Joseph A / Gileadi, Opher

Essays in biochemistry

2020 Band 64, Heft 5, Seite(n) 819–830

Abstract: Helicases are enzymes that use the energy derived from ATP hydrolysis to catalyze the unwinding of DNA or RNA. The RecQ family of helicases is conserved through evolution from prokaryotes to higher eukaryotes and plays important roles in various DNA ... ...

Abstract	Helicases are enzymes that use the energy derived from ATP hydrolysis to catalyze the unwinding of DNA or RNA. The RecQ family of helicases is conserved through evolution from prokaryotes to higher eukaryotes and plays important roles in various DNA repair pathways, contributing to the maintenance of genome integrity. Despite their roles as general tumor suppressors, there is now considerable interest in exploiting RecQ helicases as synthetic lethal targets for the development of new cancer therapeutics. In this review, we summarize the latest developments in the structural and mechanistic study of RecQ helicases and discuss their roles in various DNA repair pathways. Finally, we consider the potential to exploit RecQ helicases as therapeutic targets and review the recent progress towards the development of small molecules targeting RecQ helicases as cancer therapeutics.
Mesh-Begriff(e)	DNA Repair ; Genomic Instability ; Humans ; Neoplasms/genetics ; Neoplasms/therapy ; RecQ Helicases/metabolism
Chemische Substanzen	RecQ Helicases (EC 3.6.4.12)
Sprache	Englisch
Erscheinungsdatum	2020-10-23
Erscheinungsland	England
Dokumenttyp	Journal Article ; Review
ISSN	1744-1358 ; 0071-1365
ISSN (online)	1744-1358
ISSN	0071-1365
DOI	10.1042/EBC20200012
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Structures of soluble guanylate cyclase: implications for regulatory mechanisms and drug development.

Gileadi, Opher

Biochemical Society transactions

2014 Band 42, Heft 1, Seite(n) 108–113

Abstract: Activation of cGMP synthesis leads to vasodilation, and is an important mechanism in clinical treatment of angina, heart failure, and severe peripheral and pulmonary hypertension. The nitric oxide-responsive sGC (soluble guanylate cyclase) has been the ... ...

Abstract	Activation of cGMP synthesis leads to vasodilation, and is an important mechanism in clinical treatment of angina, heart failure, and severe peripheral and pulmonary hypertension. The nitric oxide-responsive sGC (soluble guanylate cyclase) has been the target of recent drug discovery efforts. The present review surveys recent data on the structure and regulation of sGC, and the prospects of new avenues for therapeutic intervention.
Mesh-Begriff(e)	Allosteric Regulation ; Animals ; Cardiovascular Diseases/drug therapy ; Catalytic Domain ; Drug Discovery ; Guanylate Cyclase/antagonists & inhibitors ; Guanylate Cyclase/chemistry ; Guanylate Cyclase/metabolism ; Humans ; Protein Structure, Secondary
Chemische Substanzen	Guanylate Cyclase (EC 4.6.1.2)
Sprache	Englisch
Erscheinungsdatum	2014-01-22
Erscheinungsland	England
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST20130228
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: Streamlining the production of proteins for structural biology.

Owens, Raymond J / Gileadi, Opher

Biophysical reviews

2019 , Seite(n) 533–534

Sprache	Englisch
Erscheinungsdatum	2019-06-27
Erscheinungsland	Germany
Dokumenttyp	Letter
ZDB-ID	2486483-3
ISSN	1867-2469 ; 1867-2450
ISSN (online)	1867-2469
ISSN	1867-2450
DOI	10.1007/s12551-019-00565-8
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Artikel ; Online: Regulation of inositol 5-phosphatase activity by the C2 domain of SHIP1 and SHIP2.

Bradshaw, William J / Kennedy, Emma C / Moreira, Tiago / Smith, Luke A / Chalk, Rod / Katis, Vittorio L / Benesch, Justin L P / Brennan, Paul E / Murphy, Emma J / Gileadi, Opher

Structure (London, England : 1993)

2024 Band 32, Heft 4, Seite(n) 453–466.e6

Abstract: SHIP1, an inositol 5-phosphatase, plays a central role in cellular signaling. As such, it has been implicated in many conditions. Exploiting SHIP1 as a drug target will require structural knowledge and the design of selective small molecules. We have ... ...

Abstract	SHIP1, an inositol 5-phosphatase, plays a central role in cellular signaling. As such, it has been implicated in many conditions. Exploiting SHIP1 as a drug target will require structural knowledge and the design of selective small molecules. We have determined apo, and magnesium and phosphate-bound structures of the phosphatase and C2 domains of SHIP1. The C2 domains of SHIP1 and the related SHIP2 modulate the activity of the phosphatase domain. To understand the mechanism, we performed activity assays, hydrogen-deuterium exchange mass spectrometry, and molecular dynamics on SHIP1 and SHIP2. Our findings demonstrate that the influence of the C2 domain is more pronounced for SHIP2 than SHIP1. We determined 91 structures of SHIP1 with fragments bound, with some near the interface between the two domains. We performed a mass spectrometry screen and determined four structures with covalent fragments. These structures could act as starting points for the development of potent, selective probes.
Mesh-Begriff(e)	C2 Domains ; Inositol Polyphosphate 5-Phosphatases/metabolism ; Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases/genetics ; Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases/metabolism ; Phosphoric Monoester Hydrolases/genetics ; Phosphoric Monoester Hydrolases/chemistry ; Phosphoric Monoester Hydrolases/metabolism ; Humans
Chemische Substanzen	Inositol Polyphosphate 5-Phosphatases (EC 3.1.3.56) ; INPP5D protein, human (EC 3.1.3.86) ; INPPL1 protein, human (EC 3.1.3.86) ; Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases (EC 3.1.3.86) ; Phosphoric Monoester Hydrolases (EC 3.1.3.2)
Sprache	Englisch
Erscheinungsdatum	2024-02-02
Erscheinungsland	United States
Dokumenttyp	Journal Article
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/j.str.2024.01.005
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Open drug discovery in Alzheimer's disease.

Axtman, Alison D / Brennan, Paul E / Frappier-Brinton, Tristan / Betarbet, Ranjita / Carter, Gregory W / Fu, Haian / Gileadi, Opher / Greenwood, Anna K / Leal, Karina / Longo, Frank M / Mangravite, Lara M / Edwards, Aled M / Levey, Allan I

Alzheimer's & dementia (New York, N. Y.)

2023 Band 9, Heft 2, Seite(n) e12394

Abstract: Alzheimer's disease (AD) drug discovery has focused on a set of highly studied therapeutic hypotheses, with limited success. The heterogeneous nature of AD processes suggests that a more diverse, systems-integrated strategy may identify new therapeutic ... ...

Abstract	Alzheimer's disease (AD) drug discovery has focused on a set of highly studied therapeutic hypotheses, with limited success. The heterogeneous nature of AD processes suggests that a more diverse, systems-integrated strategy may identify new therapeutic hypotheses. Although many target hypotheses have arisen from systems-level modeling of human disease, in practice and for many reasons, it has proven challenging to translate them into drug discovery pipelines. First, many hypotheses implicate protein targets and/or biological mechanisms that are under-studied, meaning there is a paucity of evidence to inform experimental strategies as well as high-quality reagents to perform them. Second, systems-level targets are predicted to act in concert, requiring adaptations in how we characterize new drug targets. Here we posit that the development and open distribution of high-quality experimental reagents and informatic outputs-termed target enabling packages (TEPs)-will catalyze rapid evaluation of emerging systems-integrated targets in AD by enabling parallel, independent, and unencumbered research.
Sprache	Englisch
Erscheinungsdatum	2023-05-17
Erscheinungsland	United States
Dokumenttyp	Journal Article
ZDB-ID	2832891-7
ISSN	2352-8737 ; 2352-8737
ISSN (online)	2352-8737
ISSN	2352-8737
DOI	10.1002/trc2.12394
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Screening and Production of Recombinant Human Proteins: Ligation-Independent Cloning.

Strain-Damerell, Claire / Mahajan, Pravin / Fernandez-Cid, Alejandra / Gileadi, Opher / Burgess-Brown, Nicola A

Methods in molecular biology (Clifton, N.J.)

2020 Band 2199, Seite(n) 23–43

Abstract: Structural genomics groups have identified the need to generate multiple truncated versions of each target to improve their success in producing a well-expressed, soluble, and stable protein and one that crystallizes and diffracts to a sufficient ... ...

Abstract	Structural genomics groups have identified the need to generate multiple truncated versions of each target to improve their success in producing a well-expressed, soluble, and stable protein and one that crystallizes and diffracts to a sufficient resolution for structural determination. At the Structural Genomics Consortium, we opted for the ligation-independent cloning (LIC) method which provides the throughput we desire to produce and screen many proteins in a parallel process. Here, we describe our LIC protocol for generating constructs in 96-well format and provide a choice of vectors suitable for expressing proteins in both E. coli and the baculovirus expression vector system (BEVS).
Mesh-Begriff(e)	Baculoviridae/genetics ; Cloning, Molecular ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression ; Genetic Vectors/genetics ; Humans ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/genetics
Chemische Substanzen	Recombinant Proteins
Sprache	Englisch
Erscheinungsdatum	2020-10-30
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-0892-0_3
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: A phosphate binding pocket is a key determinant of exo- versus endo-nucleolytic activity in the SNM1 nuclease family.

Baddock, Hannah T / Newman, Joseph A / Yosaatmadja, Yuliana / Bielinski, Marcin / Schofield, Christopher J / Gileadi, Opher / McHugh, Peter J

Nucleic acids research

2021 Band 49, Heft 16, Seite(n) 9294–9309

Abstract: The SNM1 nucleases which help maintain genome integrity are members of the metallo-β-lactamase (MBL) structural superfamily. Their conserved MBL-β-CASP-fold SNM1 core provides a molecular scaffold forming an active site which coordinates the metal ions ... ...

Abstract	The SNM1 nucleases which help maintain genome integrity are members of the metallo-β-lactamase (MBL) structural superfamily. Their conserved MBL-β-CASP-fold SNM1 core provides a molecular scaffold forming an active site which coordinates the metal ions required for catalysis. The features that determine SNM1 endo- versus exonuclease activity, and which control substrate selectivity and binding are poorly understood. We describe a structure of SNM1B/Apollo with two nucleotides bound to its active site, resembling the product state of its exonuclease reaction. The structure enables definition of key SNM1B residues that form contacts with DNA and identifies a 5' phosphate binding pocket, which we demonstrate is important in catalysis and which has a key role in determining endo- versus exonucleolytic activity across the SNM1 family. We probed the capacity of SNM1B to digest past sites of common endogenous DNA lesions and find that base modifications planar to the nucleobase can be accommodated due to the open architecture of the active site, but lesions axial to the plane of the nucleobase are not well tolerated due to constriction around the altered base. We propose that SNM1B/Apollo might employ its activity to help remove common oxidative lesions from telomeres.
Mesh-Begriff(e)	Binding Sites/genetics ; Catalysis ; Catalytic Domain/genetics ; DNA-Binding Proteins ; Endonucleases/chemistry ; Endonucleases/genetics ; Exodeoxyribonucleases/chemistry ; Exodeoxyribonucleases/genetics ; Exodeoxyribonucleases/ultrastructure ; Exonucleases/chemistry ; Exonucleases/genetics ; Humans ; Metals ; Phosphates/chemistry ; beta-Lactamases/chemistry ; beta-Lactamases/genetics
Chemische Substanzen	DNA-Binding Proteins ; Metals ; Phosphates ; DCLRE1B protein, human (EC 3.1.-) ; Endonucleases (EC 3.1.-) ; Exodeoxyribonucleases (EC 3.1.-) ; Exonucleases (EC 3.1.-) ; beta-Lactamases (EC 3.5.2.6)
Sprache	Englisch
Erscheinungsdatum	2021-08-13
Erscheinungsland	England
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkab692
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Characterization of covalent inhibitors that disrupt the interaction between the tandem SH2 domains of SYK and FCER1G phospho-ITAM.

PloS one

2024 Band 19, Heft 2, Seite(n) e0293548

Abstract: RNA sequencing and genetic data support spleen tyrosine kinase (SYK) and high affinity immunoglobulin epsilon receptor subunit gamma (FCER1G) as putative targets to be modulated for Alzheimer's disease (AD) therapy. FCER1G is a component of Fc receptor ... ...

Abstract	RNA sequencing and genetic data support spleen tyrosine kinase (SYK) and high affinity immunoglobulin epsilon receptor subunit gamma (FCER1G) as putative targets to be modulated for Alzheimer's disease (AD) therapy. FCER1G is a component of Fc receptor complexes that contain an immunoreceptor tyrosine-based activation motif (ITAM). SYK interacts with the Fc receptor by binding to doubly phosphorylated ITAM (p-ITAM) via its two tandem SH2 domains (SYK-tSH2). Interaction of the FCER1G p-ITAM with SYK-tSH2 enables SYK activation via phosphorylation. Since SYK activation is reported to exacerbate AD pathology, we hypothesized that disruption of this interaction would be beneficial for AD patients. Herein, we developed biochemical and biophysical assays to enable the discovery of small molecules that perturb the interaction between the FCER1G p-ITAM and SYK-tSH2. We identified two distinct chemotypes using a high-throughput screen (HTS) and orthogonally assessed their binding. Both chemotypes covalently modify SYK-tSH2 and inhibit its interaction with FCER1G p-ITAM, however, these compounds lack selectivity and this limits their utility as chemical tools.
Mesh-Begriff(e)	Humans ; src Homology Domains ; Protein-Tyrosine Kinases/metabolism ; Immunoreceptor Tyrosine-Based Activation Motif ; Intracellular Signaling Peptides and Proteins/metabolism ; Syk Kinase/metabolism ; Phosphorylation ; Receptors, Fc/metabolism ; Enzyme Precursors/metabolism
Chemische Substanzen	Protein-Tyrosine Kinases (EC 2.7.10.1) ; Intracellular Signaling Peptides and Proteins ; Syk Kinase (EC 2.7.10.2) ; Receptors, Fc ; Enzyme Precursors ; SYK protein, human (EC 2.7.10.2)
Sprache	Englisch
Erscheinungsdatum	2024-02-15
Erscheinungsland	United States
Dokumenttyp	Journal Article
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0293548
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: Development of FERM domain protein-protein interaction inhibitors for MSN and CD44 as a potential therapeutic strategy for Alzheimer's disease.

Du, Yuhong / Bradshaw, William J / Leisner, Tina M / Annor-Gyamfi, Joel K / Qian, Kun / Bashore, Frances M / Sikdar, Arunima / Nwogbo, Felix O / Ivanov, Andrey A / Frye, Stephen V / Gileadi, Opher / Brennan, Paul E / Levey, Allan I / Axtman, Alison D / Pearce, Kenneth H / Fu, Haian / Katis, Vittorio L

bioRxiv : the preprint server for biology

2023

Abstract: Recent genome-wide association studies have revealed genetic risk factors for Alzheimer's disease (AD) that are exclusively expressed in microglia within the brain. A proteomics approach identified moesin (MSN), a FERM (four-point-one ezrin radixin ... ...

Abstract	Recent genome-wide association studies have revealed genetic risk factors for Alzheimer's disease (AD) that are exclusively expressed in microglia within the brain. A proteomics approach identified moesin (MSN), a FERM (four-point-one ezrin radixin moesin) domain protein, and the receptor CD44 as hub proteins found within a co-expression module strongly linked to AD clinical and pathological traits as well as microglia. The FERM domain of MSN interacts with the phospholipid PIP
Sprache	Englisch
Erscheinungsdatum	2023-05-22
Erscheinungsland	United States
Dokumenttyp	Preprint
DOI	10.1101/2023.05.22.541727
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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