ReviewProtein science : a publication of the Protein Society2001
A structural basis for processivity.
Review in Protein science : a publication of the Protein Society, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
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.
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.
Who cites it
88 citing papers in PubMed.
- XPA confers ability of endonucleases to act processively and to incise damaged nucleosomal DNA.Experimental biology and medicine (Maywood, N.J.) · 2026Review
- Article
- Processive ring-opening metathesis polymerization of low ring strain cycloalkenes via molecularly confined catalyst.Nature communications · 2025Article
- Structural insight into the substrate binding of the AMT complex via an inhibitor-trapped state.Protein science : a publication of the Protein Society · 2025Article
- Chitin Translocation Is Functionally Coupled with Synthesis in Chitin Synthase.International journal of molecular sciences · 2024Article
- Catalytic Upcycling of Polyolefins.Chemical reviews · 2024Review
- Fidelity Characterization of Highly Pathogenic Porcine Reproductive and Respiratory Syndrome Virus and NADC30-like Strain.Viruses · 2024Article
- Decomposing bulk signals to reveal hidden information in processive enzyme reactions: A case study in mRNA translation.PLoS computational biology · 2024Article
- Unveiling the Catalytic Mechanism of a Processive Metalloaminopeptidase.Biochemistry · 2023Article
- An anti-biofilm cyclic peptide targets a secreted aminopeptidase from P. aeruginosa.Nature chemical biology · 2023Article
- Molecular mechanisms of processive glycoside hydrolases underline catalytic pragmatism.Biochemical Society transactions · 2023Article
- An Accessible Method to Improve the Stability and Reusability of Porcine Pancreatic α-Amylase via Immobilization in Gellan-Based Hydrogel Particles Obtained by Ionic Cross-Linking with MgMolecules (Basel, Switzerland) · 2023Article
- Vitamin K-Dependent Protein Activation: Normal Gamma-Glutamyl Carboxylation and Disruption in Disease.International journal of molecular sciences · 2022Review
- Synergic action of an inserted carbohydrate-binding module in a glycoside hydrolase family 5 endoglucanase.Acta crystallographica. Section D, Structural biology · 2022Article
- Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex.Science advances · 2021Article
- Structures of two novel crystal forms of Aspergillus oryzae alpha amylase (taka-amylase).Journal of bioscience and bioengineering · 2021Article
- Article
- Semiprocessive Hyperglycosylation of Adhesin by Bacterial ProteinACS chemical biology · 2021Article
- Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer.Nature communications · 2020Article
- Structural insights into CpG-specific DNA methylation by human DNA methyltransferase 3B.Nucleic acids research · 2020Article
28 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
The structures of a number of processive enzymes have been determined recently. These proteins remain attached to their polymeric substrates and may perform thousands of rounds of catalysis before dissociating. Based on the degree of enclosure of the substrate, the structures fall into two broad categories. In one group, the substrate is partially enclosed, while in the other class, enclosure is complete. In the latter case, enclosure is achieved by way of an asymmetric structure for some enzymes while others use a symmetrical toroid. In those cases where the protein completely encloses its polymeric substrate, the two are topologically linked and an immediate explanation for processivity is provided. In cases where there is only partial enclosure, the structural basis for processivity is less obvious. There are, for example, pairs of proteins that have quite similar structures but differ substantially in their processivity. It does appear, however, that the enzymes that are processive tend to be those that more completely enclose their substrates. In general terms, proteins that do not use topological restraint appear to achieve processivity by using a large interaction surface. This allows the enzyme to bind with moderate affinity at a multitude of adjacent sites distributed along its polymeric substrate. At the same time, the use of a large interaction surface minimizes the possibility that the enzyme might bind at a small number of sites with much higher affinity, which would interfere with sliding. Proteins that can both slide along a polymeric substrate, and, as well, recognize highly specific sites (e.g., some site-specific DNA-binding proteins) appear to undergo a conformational change between the cognate and noncognate-binding modes.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.