Evidence map›Paper›PMID 28966947›Full record

ArticleBio-protocol2017

Purifying Properly Folded Cysteine-rich, Zinc Finger Containing Recombinant Proteins for Structural Drug Targeting Studies: the CH1 Domain of p300 as a Case Example.

Yong Joon Kim, Stefan Kaluz, Anil Mehta, Emily Weinert, Shannon Rivera, Erwin G Van Meir

Open access · greenAbstract read
In one paragraph

Article in Bio-protocol, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.1field-weighted citation impact, top 54% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
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  3. TwoResearch square · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Yong Joon KimDepartment of Chemistry, Emory University, Atlanta, USA.
Stefan KaluzLaboratory of Molecular Neuro-Oncology, Departments of Neurosurgery and Hematology & Medical Oncology, School of Medicine and Winship Cancer Institute, Emory University, Atlanta, USA.
Anil MehtaDepartment of Chemistry, Emory University, Atlanta, USA.
Emily WeinertDepartment of Chemistry, Emory University, Atlanta, USA.
Shannon RiveraDepartment of Chemistry, Emory University, Atlanta, USA.
Erwin G Van MeirLaboratory of Molecular Neuro-Oncology, Departments of Neurosurgery and Hematology & Medical Oncology, School of Medicine and Winship Cancer Institute, Emory University, Atlanta, USA.
Emory University · US

Funding

Winship Cancer Institute Cancer Center Support GrantP30CA138292 · NCI · EMORY UNIVERSITY · PI Suresh S Ramalingam · 2009 to 2026
$47.5M
THERAPEUTIC MODULATION OF ANGIOGENESIS IN HUMAN GLIOMASR01CA086335 · NCI · EMORY UNIVERSITY · PI VAN MEIR, ERWIN G. · 2000 to 2011
$3.9M
Targeting Glioblastoma Using Novel Small Molecule HIF-1 Pathway InhibitorsR01CA116804 · NCI · EMORY UNIVERSITY · PI VAN MEIR, ERWIN G. · 2007 to 2011
$2.5M
Defining mechanisms of extracellular communication for cancer therapyR01CA163722 · NCI · EMORY UNIVERSITY · PI VAN MEIR, ERWIN G. · 2013 to 2017
$1.7M
Mechanisms of Action for KCN1 in the Control of Uveal Melanoma MetastasisR01CA176001 · NCI · EMORY UNIVERSITY · PI GROSSNIKLAUS, HANS E., VAN MEIR, ERWIN G. · 2014 to 2018
$1.7M
Discovery of chemical probes for uveal melanomaR01CA180805 · NCI · EMORY UNIVERSITY · PI GROSSNIKLAUS, HANS E., VAN MEIR, ERWIN G. · 2013 to 2015
$1.6M
NCI NIH HHS P30 CA138292NCI NIH HHS R01 CA086335NCI NIH HHS R01 CA116804NCI NIH HHS R01 CA163722NCI NIH HHS R01 CA176001NCI NIH HHS R01 CA180805
6 · The paper itself

Abstract

The transcription factor Hypoxia-Inducible Factor (HIF) complexes with the coactivator p300, activating the hypoxia response pathway and allowing tumors to grow. The CH1 and CAD domains of each respective protein form the interface between p300 and HIF. Small molecule compounds are in development that target and inhibit HIF/p300 complex formation, with the goal of reducing tumor growth. High resolution NMR spectroscopy is necessary to study ligand interaction with p300-CH1, and purifying high quantities of properly folded p300-CH1 is needed for pursuing structural and biophysical studies. p300-CH1 has 3 zinc fingers and 9 cysteine residues, posing challenges associated with reagent compatibility and protein oxidation. A protocol has been developed to overcome such issues by incorporating zinc during expression and streamlining the purification time, resulting in a high yield of optimally folded protein (120 mg per 4 L expression media) that is suitable for structural NMR studies. The structural integrity of the final recombinant p300-CH1 has been verified to be optimal using onedimensional

Indexed as

CBPCH1CysteineHIFHypoxiap300Recombinant protein purificationZinc finger

Identifiers

PMID28966947
PMCPMC5621770
OpenAlexW2752456589

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.