On the public citation graph

Small cause, large effect: Structural characterization of cutinases from Thermobifida cellulosilytica

0 signed · 124 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/biot.201000391openalex-snapshot
Engineered Thermobifida fusca cutinase with increased activity on polyester substrates
inferredcites →https://doi.org/10.1002/biot.201400620openalex-snapshot
Ca 2+ and Mg 2+ binding site engineering increases the degradation of polyethylene terephthalate films by polyester hydrolases from Thermobifida fusca
inferredcites →https://doi.org/10.1002/biot.201500074openalex-snapshot
Biocatalyzed approach for the surface functionalization of poly(L‐lactic acid) films using hydrolytic enzymes
inferredcites →https://doi.org/10.1002/bit.24930openalex-snapshot
Surface engineering of a cutinase from Thermobifida cellulosilytica for improved polyester hydrolysis
inferredcites →https://doi.org/10.1002/bit.25941openalex-snapshot
Engineered bacterial polyester hydrolases efficiently degrade polyethylene terephthalate due to relieved product inhibition
inferredcites →https://doi.org/10.1002/jcc.10349openalex-snapshot
A point‐charge force field for molecular mechanics simulations of proteins based on condensed‐phase quantum mechanical calculations
inferredcites →https://doi.org/10.1002/jctb.1994openalex-snapshot
Lipase‐catalyzed synthesis of polylactic acid: an overview of the experimental aspects
inferredcites →https://doi.org/10.1002/pi.5087openalex-snapshot
Renewable building blocks for sustainable polyesters: new biotechnological routes for greener plastics
inferredcites →https://doi.org/10.1002/prot.10104openalex-snapshot
Increasing the precision of comparative models with YASARA NOVA—a self‐parameterizing force field
inferredcites →https://doi.org/10.1002/prot.24955openalex-snapshot
Toward rational thermostabilization of Aspergillus oryzae cutinase: Insights into catalytic and structural stability
inferredcites →https://doi.org/10.1007/s00253-011-3781-6openalex-snapshot
Biochemical and genetic analysis of a cutinase-type polyesterase from a thermophilic Thermobifida alba AHK119
inferredcites →https://doi.org/10.1007/s00253-014-5672-0openalex-snapshot
Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca
inferredcites →https://doi.org/10.1007/s00253-014-6272-8openalex-snapshot
Structural basis for the Ca2+-enhanced thermostability and activity of PET-degrading cutinase-like enzyme from Saccharomonospora viridis AHK190
inferredcites →https://doi.org/10.1007/s10692-010-9213-zopenalex-snapshot
Overview of Poly(lactic acid) (PLA) Fibre
inferredcites →https://doi.org/10.1007/s10692-010-9226-7openalex-snapshot
Overview of Poly(lactic acid) (PLA) fibre
inferredcites →https://doi.org/10.1016/j.biortech.2016.07.106openalex-snapshot
Ultrasound-enhanced enzymatic hydrolysis of poly(ethylene terephthalate)
inferredcites →https://doi.org/10.1016/j.colsurfb.2003.08.005openalex-snapshot
Enzymatic hydrolysis by cutinase of PEG-co PLA copolymers spread monolayers
inferredcites →https://doi.org/10.1016/j.jbiotec.2006.12.028openalex-snapshot
Tailoring cutinase activity towards polyethylene terephthalate and polyamide 6,6 fibers
inferredcites →https://doi.org/10.1016/j.polymdegradstab.2016.02.025openalex-snapshot
Improving enzymatic polyurethane hydrolysis by tuning enzyme sorption
inferredcites →https://doi.org/10.1016/j.procbio.2016.10.014openalex-snapshot
Enzyme-catalyzed functionalization of poly(L-lactic acid) for drug delivery applications
inferredcites →https://doi.org/10.1016/j.reactfunctpolym.2012.12.007openalex-snapshot
Bioactive albumin functionalized polylactic acid membranes for improved biocompatibility
inferredcites →https://doi.org/10.1016/j.tibtech.2015.12.009openalex-snapshot
The Closure of the Cycle: Enzymatic Synthesis and Functionalization of Bio-Based Polyesters
inferredcites →https://doi.org/10.1016/s0969-2126(98)00052-5openalex-snapshot
Structure of a microbial homologue of mammalian platelet-activating factor acetylhydrolases: Streptomyces exfoliatus lipase at 1.9 å resolution
inferredcites →https://doi.org/10.1021/bm400140uopenalex-snapshot
Fusion of Binding Domains to Thermobifida cellulosilytica Cutinase to Tune Sorption Characteristics and Enhancing PET Hydrolysis
inferredcites →https://doi.org/10.1021/ci500118sopenalex-snapshot
Docking Covalent Inhibitors: A Parameter Free Approach To Pose Prediction and Scoring
inferredcites →https://doi.org/10.1021/ma200949popenalex-snapshot
Enzymatic Surface Hydrolysis of PET: Effect of Structural Diversity on Kinetic Properties of Cutinases from Thermobifida
inferredcites →https://doi.org/10.1038/nmeth.2648openalex-snapshot
Improved low-resolution crystallographic refinement with Phenix and Rosetta
inferredcites →https://doi.org/10.1039/c6gc03150aopenalex-snapshot
Superhydrophobic functionalization of cutinase activated poly(lactic acid) surfaces
inferredcites →https://doi.org/10.1107/s0907444903029640openalex-snapshot
Novel buffer systems for macromolecular crystallization
inferredcites →https://doi.org/10.1107/s0907444909047374openalex-snapshot
Integration, scaling, space-group assignment and post-refinement
inferredcites →https://doi.org/10.1107/s0907444909052925openalex-snapshot
PHENIX : a comprehensive Python-based system for macromolecular structure solution
inferredcites →https://doi.org/10.1107/s0907444910007493openalex-snapshot
Features and development of Coot
inferredcites →https://doi.org/10.1107/s0907444910048675openalex-snapshot
iMOSFLM: a new graphical interface for diffraction-image processing withMOSFLM
inferredcites →https://doi.org/10.1128/aem.04111-14openalex-snapshot
Enhanced Cutinase-Catalyzed Hydrolysis of Polyethylene Terephthalate by Covalent Fusion to Hydrophobins
inferredcites →https://doi.org/10.1177/0040517512458345openalex-snapshot
Modification of polylactic acid fabric by two lipolytic enzyme hydrolysis
inferredcites →https://doi.org/10.2174/1389203003381405openalex-snapshot
Alpha Beta-Hydrolase Fold Enzymes Structures, Functions and Mechanisms
inferredcites →https://doi.org/10.3390/polym4010617openalex-snapshot
A New Esterase from Thermobifida halotolerans Hydrolyses Polyethylene Terephthalate (PET) and Polylactic Acid (PLA)

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4887387openalex-extracted
Discovery and Structure-Guided Engineering a Novel Mhetase for Efficient Enhanced Pet Biodegradation
inferred← citeshttps://doi.org/10.1002/bit.27984openalex-snapshot
Structure‐function analysis of two closely related cutinases from Thermobifida cellulosilytica
inferred← citeshttps://doi.org/10.1002/chem.202403879openalex-snapshot
Selective Hydrolysis by Engineered Cutinases: Characterization of Aliphatic‐Aromatic Homo and Co‐Polyesters by LC and LC–MS Methods
inferred← citeshttps://doi.org/10.1002/cjce.25717openalex-snapshot
Biorecycling of polylactide: From enzymatic depolymerization to biotransformation of released products
inferred← citeshttps://doi.org/10.1002/cssc.202100740openalex-snapshot
Emerging Strategies in Polyethylene Terephthalate Hydrolase Research for Biorecycling
inferred← citeshttps://doi.org/10.1002/cssc.202101062openalex-snapshot
Low Carbon Footprint Recycling of Post‐Consumer PET Plastic with a Metagenomic Polyester Hydrolase
inferred← citeshttps://doi.org/10.1002/cssc.202500944openalex-snapshot
Cutinases for Biocatalytic Polycarbonate Hydrolysis: Empowering Circular Economy
inferred← citeshttps://doi.org/10.1002/jctb.6745openalex-snapshot
Insights into polyester plastic biodegradation by carboxyl ester hydrolases
inferred← citeshttps://doi.org/10.1002/prot.26325openalex-snapshot
Plastics degradation by hydrolytic enzymes: The plastics‐active enzymes database— PAZy
inferred← citeshttps://doi.org/10.1002/prot.26785openalex-snapshot
Similar but Distinct—Biochemical Characterization of the Staphylococcus aureus Serine Hydrolases FphH and FphI
inferred← citeshttps://doi.org/10.1007/978-3-031-74874-5_2openalex-snapshot
Enzymatic Degradation of Synthetic Plastics: New Insights
inferred← citeshttps://doi.org/10.1007/s00253-018-8850-7openalex-snapshot
Surface engineering of polyester-degrading enzymes to improve efficiency and tune specificity
inferred← citeshttps://doi.org/10.1007/s00253-018-9374-xopenalex-snapshot
Enzymatic hydrolysis of PET: functional roles of three Ca2+ ions bound to a cutinase-like enzyme, Cut190*, and its engineering for improved activity
inferred← citeshttps://doi.org/10.1007/s00253-019-09717-yopenalex-snapshot
Current knowledge on enzymatic PET degradation and its possible application to waste stream management and other fields
inferred← citeshttps://doi.org/10.1007/s00253-024-13212-4openalex-snapshot
Enzymatic degradation of polylactic acid (PLA)
inferred← citeshttps://doi.org/10.1007/s10311-024-01714-6openalex-snapshot
Natural and engineered enzymes for polyester degradation: a review
inferred← citeshttps://doi.org/10.1007/s10529-023-03418-3openalex-snapshot
The structural and molecular mechanisms of type II PETases: a mini review
inferred← citeshttps://doi.org/10.1007/s12010-025-05308-yopenalex-snapshot
Comparison of Polyethylene Terephthalate (PET) Degrading Cutinases from Bacteria and Fungi: Structural Characterization and Molecular Docking Analysis
inferred← citeshttps://doi.org/10.1016/bs.mie.2020.12.031openalex-snapshot
Cutinases from thermophilic bacteria (actinomycetes): From identification to functional and structural characterization
inferred← citeshttps://doi.org/10.1016/j.aac.2023.12.001openalex-snapshot
Structural insights of poly(butylene adipate-co-terephthalate) depolymerases
inferred← citeshttps://doi.org/10.1016/j.bioorg.2026.110537openalex-snapshot
Engineering a thermostable MHET-active esterase through active-site compaction for efficient dual-enzyme PET depolymerization
inferred← citeshttps://doi.org/10.1016/j.biortech.2020.124609openalex-snapshot
Decolorization of molasses alcohol wastewater by thermophilic hydrolase with practical application value
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2020.107520openalex-snapshot
Enzymes revolutionize the bioproduction of value-added compounds: From enzyme discovery to special applications
inferred← citeshttps://doi.org/10.1016/j.cec.2024.100077openalex-snapshot
Biotechnological approaches: Degradation and valorization of waste plastic to promote the circular economy
inferred← citeshttps://doi.org/10.1016/j.csbj.2021.01.019openalex-snapshot
An extracellular lipase from Amycolatopsis mediterannei is a cutinase with plastic degrading activity
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2022.110004openalex-snapshot
Enhancement of PET biodegradation by anchor peptide-cutinase fusion protein
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2026.110955openalex-snapshot
Beyond model substrates: Reevaluating enzymes claimed to hydrolyze zearalenone
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2023.127656openalex-snapshot
Engineered Geobacillus lipolytic enzymes – Attractive polyesterases that degrade polycaprolactones and simultaneously produce esters
inferred← citeshttps://doi.org/10.1016/j.jhazmat.2022.129941openalex-snapshot
The plastisphere microbiome in alpine soils alters the microbial genetic potential for plastic degradation and biogeochemical cycling
inferred← citeshttps://doi.org/10.1016/j.mcat.2025.115392openalex-snapshot
Advances in enzymatic degradation of microplastics: Mechanisms, optimization strategies, and future directions
inferred← citeshttps://doi.org/10.1016/j.mcat.2026.116074openalex-snapshot
Identification and catalytic characterization of a thermostable PET-hydrolyzing enzyme from Lactobacillus johnsonii
inferred← citeshttps://doi.org/10.1016/j.nbt.2025.03.007openalex-snapshot
Screening assay for polyester hydrolyzing microorganisms using fluorescence-labeled poly(butylene adipate)
inferred← citeshttps://doi.org/10.1016/j.procbio.2017.11.021openalex-snapshot
Characterization of a cutinase from Myceliophthora thermophila and its application in polyester hydrolysis and deinking process
inferred← citeshttps://doi.org/10.1016/j.procbio.2023.10.020openalex-snapshot
Production of recombinant cutinases and their potential applications in polymer hydrolysis: The current status
inferred← citeshttps://doi.org/10.1016/j.scitotenv.2024.174978openalex-snapshot
Unveiling potential PET degrading eukaryotes through in silico bioprospecting of PETases
inferred← citeshttps://doi.org/10.1016/j.tibtech.2021.02.008openalex-snapshot
Enzyme discovery and engineering for sustainable plastic recycling
inferred← citeshttps://doi.org/10.1016/j.wasman.2025.01.040openalex-snapshot
Enzymes offer a promising avenue for enhancing the competitiveness of biodegradable plastics in environmental restoration and the circular economy
inferred← citeshttps://doi.org/10.1021/acs.chemrev.2c00644openalex-snapshot
Enzymes’ Power for Plastics Degradation
inferred← citeshttps://doi.org/10.1021/acs.jcim.5c03051openalex-snapshot
Molecular Dynamics Insights into the Biodegradation of Synthetic Polymers by Moniliophthora roreri Cutinases
inferred← citeshttps://doi.org/10.1021/acs.jpcb.1c05901openalex-snapshot
Rate-Perturbing Single Amino Acid Mutation for Hydrolases: A Statistical Profiling
inferred← citeshttps://doi.org/10.1021/acsabm.4c01628openalex-snapshot
Enzyme-Embedded Biodegradable Plastic for Sustainable Applications: Advances, Challenges, and Perspectives
inferred← citeshttps://doi.org/10.1021/acscatal.3c02142openalex-snapshot
Directed Evolution of Material Binding Peptide for Polylactic Acid-specific Degradation in Mixed Plastic Wastes
inferred← citeshttps://doi.org/10.1021/acsestengg.4c00253openalex-snapshot
Prochiral Selectivity in Enzymatic Polyethylene Terephthalate Depolymerization Revealed by Computational Modeling
inferred← citeshttps://doi.org/10.1021/acsmaterialslett.6c00172openalex-snapshot
Enzymatic Nylon Deconstruction: Enzyme Discovery, Engineering, and Opportunities
inferred← citeshttps://doi.org/10.1021/acssuschemeng.0c01638openalex-snapshot
Current State and Perspectives Related to the Polyethylene Terephthalate Hydrolases Available for Biorecycling
inferred← citeshttps://doi.org/10.1021/acssuschemeng.2c01961openalex-snapshot
Particle Size Reduction of Poly(ethylene terephthalate) Increases the Rate of Enzymatic Depolymerization But Does Not Increase the Overall Conversion Extent
inferred← citeshttps://doi.org/10.1021/acssuschemeng.4c00060openalex-snapshot
Discovery and Surface Charge Engineering of Fungal Cutinases for Enhanced Activity on Poly(ethylene terephthalate)
inferred← citeshttps://doi.org/10.1021/bk-2018-1310.ch005openalex-snapshot
Structural and Mutational Analysis of Polyethylene Terephthalate–Hydrolyzing Enzyme, Cut190, Based on Three-Dimensional Docking Structure with Model Compounds of Polyethylene Terephthalate
inferred← citeshttps://doi.org/10.1021/bk-2020-1373.ch004openalex-snapshot
Crystal Structures of Polyethylene Terephthalate-Degrading Enzyme Cut190 in Substrate-Bound States Reveal the Enzymatic Reaction Cycle Accelerated by Calcium Ion
inferred← citeshttps://doi.org/10.1021/jacsau.4c00718openalex-snapshot
From Bulk to Binding: Decoding the Entry of PET into Hydrolase Binding Pockets
inferred← citeshttps://doi.org/10.1038/s41467-023-37415-xopenalex-snapshot
Structure and function of the metagenomic plastic-degrading polyester hydrolase PHL7 bound to its product
inferred← citeshttps://doi.org/10.1038/s41467-023-40233-wopenalex-snapshot
Discovery and rational engineering of PET hydrolase with both mesophilic and thermophilic PET hydrolase properties
inferred← citeshttps://doi.org/10.1038/s41564-023-01529-1openalex-snapshot
Sustainable production and degradation of plastics using microbes
inferred← citeshttps://doi.org/10.1038/s41598-024-84718-0openalex-snapshot
Evaluating cutinase from Fusarium oxysporum as a biocatalyst for the degradation of nine synthetic polymer
inferred← citeshttps://doi.org/10.1039/c7gc02905eopenalex-snapshot
Enzymatic surface hydrolysis of poly(ethylene furanoate) thin films of various crystallinities
inferred← citeshttps://doi.org/10.1039/c9ra07519dopenalex-snapshot
Switched reaction specificity in polyesterases towards amide bond hydrolysis by enzyme engineering
inferred← citeshttps://doi.org/10.1039/d4ra00844hopenalex-snapshot
Recent advances in microbial and enzymatic engineering for the biodegradation of micro- and nanoplastics
inferred← citeshttps://doi.org/10.1039/d5em00563aopenalex-snapshot
Enzymes involved in the manipulation of polyethylene degradation: oxidative attack by invertebrates, microorganisms and algae on microplastics
inferred← citeshttps://doi.org/10.1080/10643389.2026.2708126openalex-snapshot
Enzymatic degradation performance of biopolymers: A systematic comparative review and meta-analysis of literature
inferred← citeshttps://doi.org/10.1111/1751-7915.14479openalex-snapshot
Identification and expression of MarCE, a marine carboxylesterase with synthetic ester‐degrading activity
inferred← citeshttps://doi.org/10.1111/febs.14781openalex-snapshot
Structural insights into the unique polylactate‐degrading mechanism of Thermobifida alba cutinase
inferred← citeshttps://doi.org/10.1128/aem.01842-21openalex-snapshot
Antarctic Polyester Hydrolases Degrade Aliphatic and Aromatic Polyesters at Moderate Temperatures
inferred← citeshttps://doi.org/10.1134/s0003683824020091openalex-snapshot
Substrate Inhibition of the Highly Efficient PET Hydrolase
inferred← citeshttps://doi.org/10.1186/s40643-020-00324-8openalex-snapshot
Structure-guided engineering of a Thermobifida fusca cutinase for enhanced hydrolysis on natural polyester substrate
inferred← citeshttps://doi.org/10.1186/s44316-024-00011-0openalex-snapshot
Recent trends in microbial and enzymatic plastic degradation: a solution for plastic pollution predicaments
inferred← citeshttps://doi.org/10.13560/j.cnki.biotech.bull.1985.2020-0336openalex-snapshot
Research Advance in Polyethylene Terephthalate Hydrolytic Enzymes
inferred← citeshttps://doi.org/10.15255/kui.2022.076openalex-snapshot
Discovery of Plastics-degrading Enzymes
inferred← citeshttps://doi.org/10.2139/ssrn.6096241openalex-snapshot
Engineering a compact-pocket MHETase to relieve product inhibition and enable near-complete enzymatic depolymerization of PET
inferred← citeshttps://doi.org/10.2174/0929866530666230509141807openalex-snapshot
Attack Site Density of a Highly-efficient PET Hydrolases
inferred← citeshttps://doi.org/10.31399/asm.hb.v11b.a0006866openalex-snapshot
Microbial Degradation of Plastics
inferred← citeshttps://doi.org/10.3389/fmicb.2019.02187openalex-snapshot
In silico Screening and Heterologous Expression of a Polyethylene Terephthalate Hydrolase (PETase)-Like Enzyme (SM14est) With Polycaprolactone (PCL)-Degrading Activity, From the Marine Sponge-Derived Strain Streptomyces sp. SM14
inferred← citeshttps://doi.org/10.3389/fmicb.2020.00114openalex-snapshot
A Novel Polyester Hydrolase From the Marine Bacterium Pseudomonas aestusnigri – Structural and Functional Insights
inferred← citeshttps://doi.org/10.3389/fmicb.2021.777727openalex-snapshot
Potential Use of Microbial Enzymes for the Conversion of Plastic Waste Into Value-Added Products: A Viable Solution
inferred← citeshttps://doi.org/10.3389/fmicb.2025.1599470openalex-snapshot
Efficient biodegradation and upcycling of polyethylene terephthalate mediated by cell-factories
inferred← citeshttps://doi.org/10.3390/catal11020206openalex-snapshot
The Current State of Research on PET Hydrolyzing Enzymes Available for Biorecycling
inferred← citeshttps://doi.org/10.3390/catal11070784openalex-snapshot
Criteria for Engineering Cutinases: Bioinformatics Analysis of Catalophores
inferred← citeshttps://doi.org/10.3390/catal14060379openalex-snapshot
Selection of Putative Polyester Hydrolases from the Metagenome of Los Humeros Geothermal Field by Means of In Silico Probes
inferred← citeshttps://doi.org/10.3390/catal7110318openalex-snapshot
Enzymatic Degradation of Poly(ethylene 2,5-furanoate) Powders and Amorphous Films
inferred← citeshttps://doi.org/10.3390/catal8120612openalex-snapshot
A Middle-Aged Enzyme Still in Its Prime: Recent Advances in the Field of Cutinases
inferred← citeshttps://doi.org/10.3390/ijms222011257openalex-snapshot
Perspectives on the Role of Enzymatic Biocatalysis for the Degradation of Plastic PET
inferred← citeshttps://doi.org/10.3390/ijms25158120openalex-snapshot
Biochemical Characterisation of Sis: A Distinct Thermophilic PETase with Enhanced NanoPET Substrate Hydrolysis and Thermal Stability
inferred← citeshttps://doi.org/10.4014/jmb.2208.08048openalex-snapshot
Recent Advances in the Chemobiological Upcycling of Polyethylene Terephthalate (PET) into Value-Added Chemicals
inferred← citeshttps://doi.org/10.4236/abb.2018.95015openalex-snapshot
Expression, Purification and Crystallization of Thermostable Mutant of Cutinase Est1 from Thermobifida alba
inferred← citeshttps://doi.org/10.4236/abb.2018.98025openalex-snapshot
Erratum to “Expression, Purification and Crystallization of Thermostable Mutant of Cutinase Est1 from Thermobifida alba.” [Advances in Bioscience and Biotechnology 9 (2018), 215-223]
inferred← citeshttps://doi.org/10.4236/ojapps.2026.165106openalex-snapshot
Enzymatic Biorecycling of Polyethylene Terephthalate (PET): Mechanisms, Microbial Resources, and Protein Engineering Strategies
inferred← citeshttps://doi.org/10.57634/rcr5069openalex-snapshot
Catalytic degradation of microplastics
inferred← citeshttps://doi.org/10.64898/2026.06.02.729468openalex-snapshot
PETase Kubu enables near-complete enzymatic depolymerization of commercial PLA/PBAT blend mulch film
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.