1. Riedl, R, 1979, Order in living organisms: A Systems Analysis of Evolution: London, Wiley.

BibTeX
@book{riedl1979order1,
    author = "Riedl, R",
    title = "Order in living organisms",
    year = "1979",
    publisher = "A Systems Analysis of Evolution: London, Wiley",
    note = "talkorigins\_source = {true}; raw\_reference = {Riedl, R., 1979, Order in living organisms: A Systems Analysis of Evolution: London, Wiley.}"
}

2. 1980, Order in living organisms: Comparative Biochemistry and Physiology Part A: Physiology: v. 66, no. 3: p. 550-551.

BibTeX
@article{crossref1980order,
    title = "Order in living organisms",
    year = "1980",
    journal = "Comparative Biochemistry and Physiology Part A: Physiology",
    url = "https://doi.org/10.1016/0300-9629(80)90215-7",
    doi = "10.1016/0300-9629(80)90215-7",
    number = "3",
    pages = "550-551",
    volume = "66"
}

3. Harper, Charles W. and Riedl, Rupert, 1980, Order in Living Organisms: A Systems Analysis of Evolution.: Systematic Zoology: v. 29, no. 1: p. 104.

BibTeX
@article{harper1980order,
    author = "Harper, Charles W. and Riedl, Rupert",
    title = "Order in Living Organisms: A Systems Analysis of Evolution.",
    year = "1980",
    journal = "Systematic Zoology",
    url = "https://doi.org/10.2307/2412636",
    doi = "10.2307/2412636",
    number = "1",
    pages = "104",
    volume = "29"
}

4. Paranjpe, Dhanashree A and Sharma, Vijay Kumar, 2005, Evolution of temporal order in living organisms: Journal of Circadian Rhythms: v. 3, no. 0: p. 7.

BibTeX
@article{paranjpe2005evolution,
    author = "Paranjpe, Dhanashree A and Sharma, Vijay Kumar",
    title = "Evolution of temporal order in living organisms",
    year = "2005",
    journal = "Journal of Circadian Rhythms",
    url = "https://doi.org/10.1186/1740-3391-3-7",
    doi = "10.1186/1740-3391-3-7",
    number = "0",
    pages = "7",
    volume = "3"
}

5. Owen, Dylan M. and Magenau, Astrid and Majumdar, Arindam and Gaus, Katharina, 2010, Imaging Membrane Lipid Order in Whole, Living Vertebrate Organisms: Biophysical Journal: v. 99, no. 1: p. L7-L9.

BibTeX
@article{owen2010imaging,
    author = "Owen, Dylan M. and Magenau, Astrid and Majumdar, Arindam and Gaus, Katharina",
    title = "Imaging Membrane Lipid Order in Whole, Living Vertebrate Organisms",
    year = "2010",
    journal = "Biophysical Journal",
    url = "https://doi.org/10.1016/j.bpj.2010.04.022",
    doi = "10.1016/j.bpj.2010.04.022",
    number = "1",
    pages = "L7-L9",
    volume = "99"
}

6. Kneuer, Lukas and Wurst, René and Lapp, Christian Jonas and Lê, Nhật Quang and Kobza, Leah and Menzel, Milena and Klein, Edina Marlen and Philipp, Laura-Alina and Paquete, Catarina M and Gescher, Johannes, 2026, Living electronics: Coupling S. oneidensis MtrC-SpyTag cells to SpyCatcher-functionalized electrodes for direct electron transfer.: Biosensors & bioelectronics.

Abstract

This work set out to establish an easily applicable system to improve a broad range of bioelectronic devices using the SpyTag-SpyCatcher crosslinking system together with one of the model organisms for extracellular electron transport, Shewanella oneidensis. Therefore, the surface-displayed c-type cytochrome MtrC was equipped with an accessible SpyTag and coupled to SpyCatcher-functionalized surfaces. A transposon screen followed by nanopore sequencing was conducted in order to identify integration positions which facilitate MtrC functionality while the SpyTag is surface accessible. Three integration positions (W314, Y417, T603) were chosen for further characterization. Expression of the MtrC-SpyTag constructs in a S. oneidensis strain lacking all outer membrane cytochromes restored the ability to reduce an extracellular electron acceptor. Two of the three strains reached reduction rates at the wildtype MtrC level proving that the integrated SpyTag does not hamper extracellular electron transfer. In vivo, all three constructs showed significantly better binding properties to SpyCatcher functionalized magnetic beads than the wildtype MtrC control. The two most promising candidates were coupled to conductive, magnetic gold nanoparticles and directed towards a screen-printed electrode showcasing how MtrC-SpyTag expression can improve bioelectronic devices. A significantly higher charge transfer compared to the wildtype control was reached in linear sweep voltammetry and chronoamperometry experiments. Moreover, a shift towards direct electron transfer was observed which reduces the problem of redox shuttle washout in flowthrough systems. Direct binding of the cells to SpyCatcher functionalized electrodes enabled robust current production even after thorough washing of the electrodes while control cells failed to produce current under these conditions. The versatile SpyCatcher toolbox can be used together with the here reported strains to eliminate bottlenecks in bioelectronics like poor biofilm formation or the production of an insulating extracellular polymer matrix.

BibTeX
@article{doi101016jbios2026118682,
    author = "Kneuer, Lukas and Wurst, René and Lapp, Christian Jonas and Lê, Nhật Quang and Kobza, Leah and Menzel, Milena and Klein, Edina Marlen and Philipp, Laura-Alina and Paquete, Catarina M and Gescher, Johannes",
    title = "Living electronics: Coupling S. oneidensis MtrC-SpyTag cells to SpyCatcher-functionalized electrodes for direct electron transfer.",
    year = "2026",
    journal = "Biosensors \& bioelectronics",
    abstract = "This work set out to establish an easily applicable system to improve a broad range of bioelectronic devices using the SpyTag-SpyCatcher crosslinking system together with one of the model organisms for extracellular electron transport, Shewanella oneidensis. Therefore, the surface-displayed c-type cytochrome MtrC was equipped with an accessible SpyTag and coupled to SpyCatcher-functionalized surfaces. A transposon screen followed by nanopore sequencing was conducted in order to identify integration positions which facilitate MtrC functionality while the SpyTag is surface accessible. Three integration positions (W314, Y417, T603) were chosen for further characterization. Expression of the MtrC-SpyTag constructs in a S. oneidensis strain lacking all outer membrane cytochromes restored the ability to reduce an extracellular electron acceptor. Two of the three strains reached reduction rates at the wildtype MtrC level proving that the integrated SpyTag does not hamper extracellular electron transfer. In vivo, all three constructs showed significantly better binding properties to SpyCatcher functionalized magnetic beads than the wildtype MtrC control. The two most promising candidates were coupled to conductive, magnetic gold nanoparticles and directed towards a screen-printed electrode showcasing how MtrC-SpyTag expression can improve bioelectronic devices. A significantly higher charge transfer compared to the wildtype control was reached in linear sweep voltammetry and chronoamperometry experiments. Moreover, a shift towards direct electron transfer was observed which reduces the problem of redox shuttle washout in flowthrough systems. Direct binding of the cells to SpyCatcher functionalized electrodes enabled robust current production even after thorough washing of the electrodes while control cells failed to produce current under these conditions. The versatile SpyCatcher toolbox can be used together with the here reported strains to eliminate bottlenecks in bioelectronics like poor biofilm formation or the production of an insulating extracellular polymer matrix.",
    url = "https://pubmed.ncbi.nlm.nih.gov/42025054/",
    doi = "10.1016/j.bios.2026.118682",
    pmid = "42025054"
}

7. Yamanashi, Yuki and Kanai, Motomu, 2026, Catalytic strategies for post-translational modifications regulating protein higher-order structure and properties.: Chemical Society reviews.

Abstract

Proteins, the major functional components of living organisms, undergo post-translational modifications (PTMs) that expand their structural and functional diversity. Recent advances in PTM profiling and functional analysis have revealed that many PTMs act as reversible modulators of protein behavior, operating with residue- and domain-level precision to reshape higher-order structures. Both biotic and abiotic catalyses are emerging means of deciphering and controlling PTMs. In this Tutorial Review, we outline how PTMs influence protein architecture across multiple structural scales and survey catalytic strategies that enable their analysis and manipulation.

BibTeX
@article{doi101039d6cs00107f,
    author = "Yamanashi, Yuki and Kanai, Motomu",
    title = "Catalytic strategies for post-translational modifications regulating protein higher-order structure and properties.",
    year = "2026",
    journal = "Chemical Society reviews",
    abstract = "Proteins, the major functional components of living organisms, undergo post-translational modifications (PTMs) that expand their structural and functional diversity. Recent advances in PTM profiling and functional analysis have revealed that many PTMs act as reversible modulators of protein behavior, operating with residue- and domain-level precision to reshape higher-order structures. Both biotic and abiotic catalyses are emerging means of deciphering and controlling PTMs. In this Tutorial Review, we outline how PTMs influence protein architecture across multiple structural scales and survey catalytic strategies that enable their analysis and manipulation.",
    url = "https://pubmed.ncbi.nlm.nih.gov/41910043/",
    doi = "10.1039/d6cs00107f",
    pmid = "41910043"
}