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Scientists reveal how cells “back up” DNA replication to survive severe damage

Researchers found that DNA helicase HELQ promotes replication fork reversal to protect cells from toxic DNA crosslinks. This process enables stalled replication forks to reverse and stabilize, minimizing mutations and cell death. The study identifies HELQ as a critical regulator of genome integrity under replication stress.

SourceInstitute for Basic Science·JournalNucleic Acids Research·TypeExperimental study·DateMay 7, 2026
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Scientists see the first steps of DNA unwinding

For the first time, scientists have witnessed the moment DNA begins to unravel, revealing a necessary molecular event for DNA replication. This direct observation sheds light on the fundamental mechanisms that allow cells to faithfully duplicate their genetic material.

SourceKing Abdullah University of Science & Technology (KAUST)·JournalNature·TypeExperimental study·DateMar 19, 2025
Apple Watch Series 11 (GPS, 46mm)

Apple Watch Series 11 (GPS, 46mm) tracks health metrics and safety alerts during long observing sessions, fieldwork, and remote expeditions.

Protein involved in balancing DNA replication and restarting found

A team of researchers has identified the USP50 protein's role in regulating DNA replication by deciding which enzymes to use during critical processes. The study found that USP50 helps cells balance nuclease and helicase activity, preventing replication defects when it is absent.

SourceUniversity of Birmingham·JournalNature Communications·DateOct 14, 2024

DDX41: A key nuclear player in maintaining genomic stability

Researchers have characterized the functional significance of DDX41 in molecular processes underlying cancer. The study reveals that DDX41 serves crucial functions in transcriptional processes, RNA splicing, and genomic integrity maintenance, which may hold significance in treating hematopoietic malignancies.

SourceKumamoto University·JournalLeukemia·TypeExperimental study·DateNov 17, 2022

Rice models moving ‘washers’ that help DNA replicate

Researchers have modelled a key mechanism by which DNA replicates, revealing details about how helicases wrangle DNA during replication. The simulations showed each step of translocation can travel more than 12 nucleotides along the backbone, pinpointing interactions involved in long-distance movement.

SourceRice University·JournalProceedings of the National Academy of Sciences·TypeComputational simulation/modeling·DateAug 9, 2022
Apple MacBook Pro 14-inch (M4 Pro)

Apple MacBook Pro 14-inch (M4 Pro) powers local ML workloads, large datasets, and multi-display analysis for field and lab teams.

Role identified for key gene in developmental disability syndrome

Duke researchers identify DDX3X gene as crucial for neuron formation and brain development, with dosage-dependent defects leading to developmental disabilities. The study sheds light on the molecular mechanisms underlying DDX3X syndrome and related disorders, potentially paving the way for therapies.

SourceDuke University·JournaleLife·TypeExperimental study·DateJun 28, 2022

Aging-US | WRNing for the right DNA repair pathway choice

A recent study published in Aging-US reveals the crucial role of WRN in making choices between classical and alternative non-homologous end joining (NHEJ) DNA repair pathways. The research provides new insights into progeroid syndromes, such as Werner syndrome, and their connection to aging.

SourceImpact Journals LLC·JournalAging-US·TypeExperimental study·DateJun 16, 2022

New microscopy method offers 3D tracking of 100 single molecules at once

Researchers at Arizona State University have developed a new microscopy method that can track 100 single molecules simultaneously in three dimensions. The technique uses surface plasmon resonance (SPR) technology to precisely image molecular binding events and study their dynamic activities in real time.

SourceArizona State University·JournalACS Sensors·TypeExperimental study·DateNov 18, 2021

The precise function of the RNA helicases in ribosome synthesis

Researchers used a yeast model to understand the dynamics of early-stage ribosomal subunit assembly, discovering snR190 functions as an RNA chaperone. The study also identified Dbp7 as the enzyme responsible for dissociating snR190 from ribosomal RNA precursors.

SourceUniversity of Seville·JournalNature Communications·DateNov 3, 2021

Tool encoded in coronaviruses provides a potential target for COVID-19

Researchers identify nsp13 as a key helicase enzyme in coronaviruses, which could be targeted for COVID-19 treatment and prevention. The study found that nsp13 is a relatively weak helicase requiring assistance to function, providing a potential first line of defense against future coronavirus outbreaks.

SourceBiophysical Society·DateFeb 23, 2021
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In one direction or the other: That is how DNA is unwound

A study published in PNAS reveals that DNA helicases unwind the double strand more easily in one direction than the other, with the speed of unwinding depending on the sequence composition of the bases. This discovery has implications for understanding gene expression and the regulation of cellular activities.

SourceScuola Internazionale Superiore di Studi Avanzati·JournalProceedings of the National Academy of Sciences·DateOct 30, 2019

Tip sheet: Recent research on how DNA is read and copied

Scientists at Johns Hopkins University have unraveled how the DNA machinery fits together, revealing a paradigm shift in understanding genetic illness. The discovery of how nucleosomes change shape to bind with an enzyme could unveil new treatment opportunities for childhood leukemia.

SourceJohns Hopkins Medicine·JournalCell·DateMay 22, 2019
Sony Alpha a7 IV (Body Only)

Sony Alpha a7 IV (Body Only) delivers reliable low-light performance and rugged build for astrophotography, lab documentation, and field expeditions.

Study finds that enzymes 'partner up' to accelerate cancer, aging diseases

Researchers at Indiana University have identified two enzymes that combine to speed up telomere growth, potentially leading to new ways to treat cancer and premature aging disorders. The study sheds light on the role of helicases in telomere maintenance and may lead to the development of new therapies.

SourceIndiana University·JournalJournal of Biological Chemistry·DateSep 25, 2018

Cryo-EM imaging suggests how the double helix separates during replication

Researchers have gained insight into how the double helix unwinds in the earliest stages of DNA replication. The new cryo-EM images show that the twin helicase enzymes load head to head, forming a complex that positions one strand for extrusion and another as the leading strand.

SourceCold Spring Harbor Laboratory·JournalProceedings of the National Academy of Sciences·DateOct 23, 2017

Cryo-EM reveals ignition mechanism for DNA replication

Scientists at Van Andel Research Institute and collaborators have shed new light on the critical step of DNA replication, revealing a spring-loaded mechanism that positions DNA strands toward two side-way gates. This discovery offers fresh insights into a fundamental process of life and driver of many different diseases, including cancer.

SourceVan Andel Research Institute·JournalProceedings of the National Academy of Sciences·DateOct 23, 2017
GoPro HERO13 Black

GoPro HERO13 Black records stabilized 5.3K video for instrument deployments, field notes, and outreach, even in harsh weather and underwater conditions.

Scientists reveal open-ringed structure of Cdt1-Mcm2-7 complex

The study reveals a left-handed coil structure of the Mcm2-7 hexamer and Cdt1-MCM heptamer, shedding light on DNA unwinding mechanisms. The open-coil structure has profound implications for understanding DNA replication initiation and elongation.

SourceHong Kong University of Science and Technology·JournalNature Structural & Molecular Biology·DateMar 17, 2017

ORC as Loader of the Rings

Researchers have mapped the critical steps of DNA replication, revealing how a ring-shaped protein called origin recognition complex (ORC) initiates the process by slipping into a groove on DNA and initiating a cascade of microscopic interactions. The study provides new insights into an immensely complex system that is constantly ongoi...

SourceVan Andel Research Institute·JournalNature Structural & Molecular Biology·DateFeb 21, 2017

New study reveals the structure of DNA helicase at the replication fork

A new study reveals the structure of DNA helicase at the replication fork, reversing a long-held assumption about its orientation. The findings provide a crucial piece in understanding how life propagates and may lead to new treatments for diseases such as cancers and anemias.

SourceVan Andel Research Institute·JournalProceedings of the National Academy of Sciences·DateJan 16, 2017

Squeezing life from DNA's double helix

Researchers have solved the mystery of DNA replication by identifying a ring of proteins that binds to origin DNA, causing it to melt and initiate replication. This discovery could lead to understanding genetic duplication and potentially blocking viral pathogens and cancer cells.

SourceUniversity of Southern California·DateDec 12, 2016
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Nikon Monarch 5 8x42 Binoculars deliver bright, sharp views for wildlife surveys, eclipse chases, and quick star-field scans at dark sites.

Cracking the mystery of Zika virus replication

Researchers from Tianjin University and Nankai University have unraveled the puzzle of how Zika virus replicates. They discovered a tunnel in the enzyme that holds viral RNA, allowing it to unwind its genetic material. This breakthrough could lead to the development of antiretroviral drugs against this spreading disease.

SourceSpringer·JournalProtein & Cell·DateJul 26, 2016

Eukaryote process of programmed fork arrest determined

Cells use programmed fork arrest to halt DNA replication at terminator sites, controlling life span and preserving genome stability. The process involves proteins working together to calibrate fork movement, preventing constant machinery operation.

SourceMedical University of South Carolina·JournalProceedings of the National Academy of Sciences·DateJun 14, 2016

Researchers solve the structure of the Zika virus helicase

Scientists have successfully obtained a high-resolution image of the Zika virus helicase, a key target for antiviral development. The structural information will help researchers design and develop effective small-molecule inhibitors to stop viral replication and prevent disease.

SourceSpringer·JournalProtein & Cell·DateMay 20, 2016

Scientists propose 'pumpjack' mechanism for splitting and copying DNA

Researchers proposed a new mechanism for DNA replication called the 'pumpjack' mechanism, which involves a molecular machine with two distinct conformations that rock back and forth to split the DNA double helix. This linear translocation mechanism appears different from previously thought mechanisms in more primitive organisms.

SourceDOE/Brookhaven National Laboratory·JournalNature Structural & Molecular Biology·DateFeb 8, 2016
Celestron NexStar 8SE Computerized Telescope

Celestron NexStar 8SE Computerized Telescope combines portable Schmidt-Cassegrain optics with GoTo pointing for outreach nights and field campaigns.

First complete pictures of cells' DNA-copying machinery

Researchers have produced the first-ever images of the protein complex that unwinds, splits, and copies double-stranded DNA, revealing a counterintuitive architecture. The helicase coordinates with polymerases to duplicate each strand, suggesting potential molecular quality control and developmental biology implications.

SourceDOE/Brookhaven National Laboratory·JournalNature Structural & Molecular Biology·DateNov 2, 2015

Study reveals the architecture of the molecular machine that copies DNA

A team of researchers has revealed the molecular architecture of the replisome, a complex responsible for unwinding and replicating DNA in eukaryotic organisms. The findings show that the replisome has a unique structure, with one polymerase sitting above the helicase, challenging decades-old textbook drawings.

SourceRockefeller University·JournalNature Structural & Molecular Biology·DateNov 2, 2015

FSU researcher identifies protein with promise for cancer therapy

Researchers at Florida State University have identified a protein called Treslin that shows promise in stopping the unregulated division of cancer cells. Treslin stimulates the activation of helicase, a key enzyme involved in DNA replication, and assembles it for cell division.

SourceFlorida State University·JournalProceedings of the National Academy of Sciences·DateAug 24, 2015

New lab technique reveals structure and function of proteins critical in DNA repair

Scientists at the University of Illinois have developed a new lab technique that simultaneously observes protein structure and function in DNA repair. The technique, combining fluorescence microscopy and optical trapping, provides definitive answers to long-debated questions and opens up new avenues for biological engineering.

SourceUniversity of Illinois Grainger College of Engineering·JournalScience·DateApr 17, 2015

Key moment mapped in assembly of DNA-splitting molecular machine

Researchers pinpoint key moments in the beginning of DNA replication, including structural details about the enzyme that unwinds the DNA double helix. The study's findings offer insights into how the enzyme becomes reactivated to begin its work splitting the DNA.

SourceDOE/Brookhaven National Laboratory·JournalGenes & Development·DateOct 15, 2014
SAMSUNG T9 Portable SSD 2TB

SAMSUNG T9 Portable SSD 2TB transfers large imagery and model outputs quickly between field laptops, lab workstations, and secure archives.

Molecular gate that could keep cancer cells locked up

A team of researchers has identified a unique molecular mechanism involved in DNA duplication during cell division, revealing how a key enzyme governs DNA through a gated system. The study suggests a route for stopping cell division in diseases like cancer by controlling the entry point of the helicase onto DNA.

SourceMedical Research Council (MRC) Laboratory of Medical Sciences·JournalGenes & Development·DateJul 31, 2014

Key step in molecular 'dance' that duplicates DNA deciphered

Researchers have captured a key step in the molecular 'dance' necessary for cell division by imaging the enzyme that unwinds DNA double helices. The study reveals how this enzyme recruits and interacts with the origin recognition complex, enhancing understanding of essential biological processes.

SourceDOE/Brookhaven National Laboratory·JournalNature Structural & Molecular Biology·DateJul 14, 2013

Random walks on DNA

Researchers have discovered a new mechanism of DNA helicase that utilizes thermal motion to move long distances along DNA, providing an energy-efficient way to unwind double-stranded DNA

SourceUniversity of Bristol·JournalScience·DateApr 19, 2013
CalDigit TS4 Thunderbolt 4 Dock

CalDigit TS4 Thunderbolt 4 Dock simplifies serious desks with 18 ports for high-speed storage, monitors, and instruments across Mac and PC setups.

Celebrating the golden anniversary of a remarkable science agency

The National Institute of General Medical Sciences (NIGMS) is honoring its 50th anniversary with a symposium showcasing research advancements in disease diagnosis, treatment, and prevention. NIGMS has funded over 74 Nobel laureates and supports research training programs to foster the next generation of scientists.

SourceAmerican Chemical Society·DateAug 20, 2012
Garmin GPSMAP 67i with inReach

Garmin GPSMAP 67i with inReach provides rugged GNSS navigation, satellite messaging, and SOS for backcountry geology and climate field teams.

Ends of chromosomes protected by stacked, coiled DNA caps

Researchers at the University of Pennsylvania School of Medicine have discovered how telomere caps, made up of G-quadruplexes, protect chromosomes from unraveling. This discovery has implications for studying human aging, Werner syndrome, and Bloom syndrome.

SourceUniversity of Pennsylvania School of Medicine·JournalNature Structural & Molecular Biology·DateApr 20, 2011

Scripps Research scientists identify key interaction in hepatitis C virus

Researchers found that the core protein interacts with non-structural helicase protein, playing a critical role in viral replication. This new understanding supports a potential new therapeutic target for hepatitis C drug development and may prevent production of infectious viral particles.

SourceScripps Research Institute·JournalJournal of General Virology·DateDec 28, 2010

Researchers advance understanding of enzyme that regulates DNA

Researchers have revealed the mechanisms of the DNA-regulating enzyme PcrA, which controls recombination by removing recombination proteins from the DNA. By combining structure-specific binding and motor function, PcrA reels in DNA and kicks off recombination proteins.

SourceUniversity of Illinois at Urbana-Champaign, News Bureau·JournalCell·DateAug 20, 2010
Davis Instruments Vantage Pro2 Weather Station

Davis Instruments Vantage Pro2 Weather Station offers research-grade local weather data for networked stations, campuses, and community observatories.

Atomic-level snapshot catches protein motor in action

Researchers have uncovered the critical action shapshot of an enzyme known as the Rho transcription termination factor, a remarkable class of ring-shaped protein motors. The study reveals a rotary engine-like mechanism that enables the motor to selectively terminate transcription at discrete points along the genome.

SourceDOE/Lawrence Berkeley National Laboratory·JournalCell·DateNov 24, 2009

UC San Diego biologists discover a motor protein that rewinds DNA

Researchers identify HARP, the first motor protein that rewinds defective DNA, preventing gene expression and potentially treating Schimke immuno-osseous dysplasia. The discovery expands our understanding of molecular mechanisms underlying this devastating genetic disorder.

SourceUniversity of California - San Diego·JournalScience·DateOct 30, 2008

The structure of XPD sheds light on cancer and aging

Researchers have solved the XPD protein structure, revealing how small changes in its architecture can cause different diseases. The findings provide novel insight into the processes of aging and cancer.

SourceDOE/Lawrence Berkeley National Laboratory·JournalCell·DateMay 29, 2008

Researchers probe a DNA repair enzyme

The researchers studied the archaeal version of Rad3, a unique helicase involved in DNA repair. The findings revealed that the integrity of an iron-sulfur cluster is crucial for proper function of the enzyme.

SourceUniversity of Illinois at Urbana-Champaign, News Bureau·JournalJournal of Biological Chemistry·DateFeb 18, 2008
Aranet4 Home CO2 Monitor

Aranet4 Home CO2 Monitor tracks ventilation quality in labs, classrooms, and conference rooms with long battery life and clear e-ink readouts.

Hepatitis C helicase unwinds DNA in a spring-loaded, 3-step process

Researchers have shed new light on how the Hepatitis C helicase plays its role in duplicating genes by tracking the gradual separation of nucleotide pairs. The study found that the helicase unwinds DNA in discrete jumps, requiring three ATP molecules for each reaction.

SourceUniversity of Illinois at Urbana-Champaign, News Bureau·JournalScience·DateJul 26, 2007

CU researchers solve mystery of how DNA strands separate

Cornell researchers have solved a fundamental question about DNA strand separation by demonstrating the active role of an enzyme called helicase. The study found that helicase exerts a force onto the fork and separates the two strands, contradicting earlier passive unwinding mechanisms.

SourceCornell University·JournalCell·DateJul 2, 2007
Sky-Watcher EQ6-R Pro Equatorial Mount

Sky-Watcher EQ6-R Pro Equatorial Mount provides precise tracking capacity for deep-sky imaging rigs during long astrophotography sessions.

Yale scientists visualize details of how hepatitis C unwinds RNA

Researchers at Yale University have made significant breakthroughs in understanding the helicase function of the hepatitis C virus. By visualizing the behavior of the viral enzyme NS3, scientists discovered that it moves with a discontinuous stepping motion that alternates rapid translocation with pausing.

SourceYale University·JournalNature·DateJul 23, 2004

Findings redefine mechanism of action of RNA helicase enzymes

Researchers from Case Western Reserve University School of Medicine have discovered that RNA helicases can displace proteins from single-stranded RNA and change shape without unwinding duplexes. This finding redefines the mechanism of action of RNA helicases, providing new insights into their roles in various biological processes.

SourceCase Western Reserve University·JournalScience·DateMay 5, 2004
Anker Laptop Power Bank 25,000mAh (Triple 100W USB-C)

Anker Laptop Power Bank 25,000mAh (Triple 100W USB-C) keeps Macs, tablets, and meters powered during extended observing runs and remote surveys.

DNA unzipping found to take at least two proteins, not one alone

New research has solved a long-standing mystery about DNA unzipping, revealing that it requires at least two proteins working together. The study found that if one protein falls away, the process stops and DNA reverts to its zipped state unless another protein joins in.

SourceUniversity of Illinois at Urbana-Champaign, News Bureau·JournalNature·DateOct 9, 2002

Peering at a machine that pries DNA apart

Harvard researchers have created the first atomic-resolution image of a donut-shaped enzyme that unwinds the DNA double helix for replication. The structure reveals how six individual polypeptide lobes arrange themselves to look like a ring of bread buns, providing new insights into the molecular motor's mechanism.

SourceHarvard Medical School·JournalCell·DateOct 15, 1999
Kestrel 3000 Pocket Weather Meter

Kestrel 3000 Pocket Weather Meter measures wind, temperature, and humidity in real time for site assessments, aviation checks, and safety briefings.

Scientists Show Proteins Function Individually As Part Of DNA Repair

Researchers at UNC-CH discovered DNA helicase II can act individually in DNA repair, similar to fixing a car. This finding brings scientists closer to correcting defective biological processes and treating diseases like Werner's and Bloom's syndromes.

SourceUniversity of North Carolina at Chapel Hill·JournalJournal of Biological Chemistry·DateApr 29, 1999