Evidence map›Paper›PMID 22918579›Full record

ReviewSub-cellular biochemistry2012

The origin recognition complex: a biochemical and structural view.

Huilin Li, Bruce Stillman

Abstract readReview
In one paragraph

Review in Sub-cellular biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

33 citing papers in PubMed, 49 citations in OpenAlex.

  1. Compact Origins and Where to Find Them: ORC's Guide to Genome-Wide Licensing.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  2. Oncofetal IGF2BP3-mediated control of microRNA structural diversity in the malignancy of early-stage lung adenocarcinoma.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Review
  4. Origin recognition complex harbors an intrinsic nucleosome remodeling activity.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Open biology · 2020
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Cryo-EM structure of Mcm2-7 double hexamer on DNA suggests a lagging-strand DNA extrusion model.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Cryo-EM of dynamic protein complexes in eukaryotic DNA replication.Protein science : a publication of the Protein Society · 2017
    Review
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

2 authors at 2 institutions in 1 country.

Huilin LiDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY, 11794, USA, hli@bnl.gov.
Bruce Stillman
Brookhaven National Laboratory · USCold Spring Harbor Laboratory · US

Funding

VIRAL TRANSACTIVATIONP01CA013106 · NCI · COLD SPRING HARBOR LABORATORY · PI Camila dos Santos · 1985 to 2026
$116.8M
REGULATION OF DNA REPLICATIONR01GM045436 · NIGMS · COLD SPRING HARBOR LABORATORY · PI STILLMAN, BRUCE W. · 1991 to 2025
$15.8M
Structural mechanism of DNA replicationR35GM131754 · NIGMS · VAN ANDEL RESEARCH INSTITUTE · PI Huilin Li · 2019 to 2026
$6.0M
The Structural Basis of Eukaryotic Replication Origin Licensing by Cryo-EMR01GM074985 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI LI, HUILIN · 2006 to 2010
$1.7M
CCD Camera for Cryo-EMS10RR025415 · NCRR · STATE UNIVERSITY NEW YORK STONY BROOK · PI LI, HUILIN · 2009 to 2009
$244k
NCI NIH HHS CA013106NCI NIH HHS P01 CA013106NCRR NIH HHS S10 RR025415NIGMS NIH HHS GM045436NIGMS NIH HHS GM74985NIGMS NIH HHS R01 GM045436NIGMS NIH HHS R01 GM074985NIGMS NIH HHS R35 GM131754
6 · The paper itself

Abstract

The origin recognition complex (ORC) was first discovered in the baker's yeast in 1992. Identification of ORC opened up a path for subsequent molecular level investigations on how eukaryotic cells initiate and control genome duplication each cell cycle. Twenty years after the first biochemical isolation, ORC is now taking on a three-dimensional shape, although a very blurry shape at the moment, thanks to the recent electron microscopy and image reconstruction efforts. In this chapter, we outline the current biochemical knowledge about ORC from several eukaryotic systems, with emphasis on the most recent structural and biochemical studies. Despite many species-specific properties, an emerging consensus is that ORC is an ATP-dependent machine that recruits other key proteins to form pre-replicative complexes (pre-RCs) at many origins of DNA replication, enabling the subsequent initiation of DNA replication in S phase.

Indexed as

Adenosine TriphosphateOrigin Recognition ComplexAnimalsGenome, HumanHumansS PhaseAdenosine TriphosphateOrigin Recognition Complex

Identifiers

PMID22918579
PMCPMC3779782
OpenAlexW1733946133

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.