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Journal articles on the topic 'Proteins cross-link'

Author: Grafiati

Published: 3 June 2025

Last updated: 31 July 2025

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1

Bode, Tom, Kai Höltje, Sara Leal-Marin, Marc Müller, and Birgit Glasmacher. "Evaluation and Implementation of Biocompatible Methods for the Cross-linking of Plasma Proteins." Current Directions in Biomedical Engineering 7, no. 2 (2021): 187–90. http://dx.doi.org/10.1515/cdbme-2021-2048.

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Abstract Autologous plasma proteins can be used to fabricate patient specific cardiovascular implants but need to be cross-linked to increase their mechanical strength and reduce water solubility. Glutaraldehyde is the state-of-the-art solution but its reaction products have been shown to be cytotoxic and pro-inflammatory. In this work, it has been shown, that cross-linking of plasma proteins with biocompatible alternatives to glutaraldehyde is possible. This was achieved by identifying four candidate substances (thrombin, transglutaminase, genipin, EDC) from current literature and investigati

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2

Fife, R. S., B. Caterson, and S. L. Myers. "Identification of link proteins in canine synovial cell cultures and canine articular cartilage." Journal of Cell Biology 100, no. 4 (1985): 1050–55. http://dx.doi.org/10.1083/jcb.100.4.1050.

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Link proteins are glycoproteins in cartilage that are involved in the stabilization of aggregates of proteoglycans and hyaluronic acid. We have identified link proteins in synovial cell cultures form normal canine synovium using sodium dodecyl sulfate-polyacrylamide gel electrophoresis, immunofluorescence, and immunolocation with specific antibodies by electrophoretic transfer. We have also found evidence for the synthesis of link proteins in these cultures by fluorography of radiolabeled synovial cell extracts. We have identified a 70,000 mol-wt protein in canine synovial cell culture extract

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3

Migliorini, Elisa, Dhruv Thakar, Jens Kühnle, et al. "Cytokines and growth factors cross-link heparan sulfate." Open Biology 5, no. 8 (2015): 150046. http://dx.doi.org/10.1098/rsob.150046.

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The glycosaminoglycan heparan sulfate (HS), present at the surface of most cells and ubiquitous in extracellular matrix, binds many soluble extracellular signalling molecules such as chemokines and growth factors, and regulates their transport and effector functions. It is, however, unknown whether upon binding HS these proteins can affect the long-range structure of HS. To test this idea, we interrogated a supramolecular model system, in which HS chains grafted to streptavidin-functionalized oligoethylene glycol monolayers or supported lipid bilayers mimic the HS-rich pericellular or extracel

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Zhang, Pan, Deepa Sridharan, Michael Acosta та Muriel Lambert. "FANCD2 Localizes to Cross-Linked Induced Nuclear Foci That Are Distinct From Those to Which αaII Spectrin and the Cross-Link Repair Protein, XPF, Co-Localize, Indicating An Involvement of These Proteins in Different Steps of the DNA Interstrand Cross-Link Repair Process." Blood 114, № 22 (2009): 3196. http://dx.doi.org/10.1182/blood.v114.22.3196.3196.

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Abstract Abstract 3196 Poster Board III-133 The hereditary bone marrow failure disorder, Fanconi anemia (FA), is characterized by a markedly increased incidence of acute myelogenous leukemia, diverse congenital abnormalities and a defect in ability to repair DNA interstrand cross-links. We have previously shown that in FA cells there is a deficiency in the structural protein nonerythroid a spectrin (aSpII), which is involved in repair of DNA interstrand cross-links and binds to cross-linked DNA. aSpII co-localizes in nuclear foci with FANCA and the cross-link repair protein, XPF, after normal

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5

Staknis, D., and R. Reed. "Direct interactions between pre-mRNA and six U2 small nuclear ribonucleoproteins during spliceosome assembly." Molecular and Cellular Biology 14, no. 5 (1994): 2994–3005. http://dx.doi.org/10.1128/mcb.14.5.2994-3005.1994.

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Highly purified mammalian spliceosomal complex B contains more than 30 specific protein components. We have carried out UV cross-linking studies to determine which of these components directly contacts pre-mRNA in purified prespliceosomal and spliceosomal complexes. We show that heterogeneous nuclear ribonucleoproteins cross-link in the nonspecific complex H but not in the B complex. U2AF65, which binds to the 3' splice site, is the only splicing factor that cross-links in purified prespliceosomal complex E. U2AF65 and the U1 small nuclear ribonucleoprotein particle (snRNP) are subsequently de

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6

Staknis, D., and R. Reed. "Direct interactions between pre-mRNA and six U2 small nuclear ribonucleoproteins during spliceosome assembly." Molecular and Cellular Biology 14, no. 5 (1994): 2994–3005. http://dx.doi.org/10.1128/mcb.14.5.2994.

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Highly purified mammalian spliceosomal complex B contains more than 30 specific protein components. We have carried out UV cross-linking studies to determine which of these components directly contacts pre-mRNA in purified prespliceosomal and spliceosomal complexes. We show that heterogeneous nuclear ribonucleoproteins cross-link in the nonspecific complex H but not in the B complex. U2AF65, which binds to the 3' splice site, is the only splicing factor that cross-links in purified prespliceosomal complex E. U2AF65 and the U1 small nuclear ribonucleoprotein particle (snRNP) are subsequently de

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7

ALI, Sohail T., John R. COGGINS, and Howard T. JACOBS. "The study of cell-death proteins in the outer mitochondrial membrane by chemical cross-linking." Biochemical Journal 325, no. 2 (1997): 321–24. http://dx.doi.org/10.1042/bj3250321.

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Chemical cross-linking was used to study the interactions of the anti-cell-death protein Bcl2 with other proteins in the outer mitochondrial membrane. Cross-linking of mitochondrial surface proteins produced a large Bcl2-containing complex (> 200 kDa), and a Bcl2-derived peptide was shown to cross-link specifically with a mitochondrial protein identified by immunoblotting as Raf-1 kinase.

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8

Kaddar, Tagrid, and Madeleine Carreau. "Fanconi Anemia Proteins and Their Interacting Partners: A Molecular Puzzle." Anemia 2012 (2012): 1–11. http://dx.doi.org/10.1155/2012/425814.

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In recent years, Fanconi anemia (FA) has been the subject of intense investigations, primarily in the DNA repair research field. Many discoveries have led to the notion of a canonical pathway, termed the FA pathway, where all FA proteins function sequentially in different protein complexes to repair DNA cross-link damages. Although a detailed architecture of this DNA cross-link repair pathway is emerging, the question of how a defective DNA cross-link repair process translates into the disease phenotype is unresolved. Other areas of research including oxidative metabolism, cell cycle progressi

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9

Neubacher, Saskia, Jordy M. Saya, Alessia Amore, and Tom N. Grossmann. "In Situ Cyclization of Proteins (INCYPRO): Cross-Link Derivatization Modulates Protein Stability." Journal of Organic Chemistry 85, no. 3 (2019): 1476–83. http://dx.doi.org/10.1021/acs.joc.9b02490.

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10

Figueroa-Espinoza, M. C., M. H. Morel, A. Surget, et al. "Attempt to cross-link feruloylated arabinoxylans and proteins with a fungal laccase." Food Hydrocolloids 13, no. 1 (1999): 65–71. http://dx.doi.org/10.1016/s0268-005x(98)00072-1.

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11

Narai-Kanayama, Asako, Tomoko Hanaishi, and Keiichi Aso. "Mechanistic investigation of capability of enzymatically synthesized polycysteine to cross-link proteins." Biochemistry and Biophysics Reports 7 (September 2016): 338–46. http://dx.doi.org/10.1016/j.bbrep.2016.07.013.

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12

Susic, D. "Cross-link breakers as a new therapeutic approach to cardiovascular disease." Biochemical Society Transactions 35, no. 5 (2007): 853–56. http://dx.doi.org/10.1042/bst0350853.

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Fibrillar proteins, such as collagens type I and III, and elastin are components of the extracellular matrix. They form an intricate widespread network that provides a basis for maintaining the physical structure of the heart and vessels and also play an important role in determining cardiovascular function. Physiologically, collagen and elastin fibres are enzymatically cross-linked to form matrix. In addition to these enzymatically formed cross-links, collagen fibres may be linked non-enzymatically, most notably by formation of AGEs (advanced glycation end-products). AGEs are formed by a reac

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13

Kluger, Ronald, Krisztina Paal, and J. Gordon Adamson. "An ether-linked tetrafunctional acylating reagent and its cross-linking reactions with hemoglobin." Canadian Journal of Chemistry 77, no. 2 (1999): 271–79. http://dx.doi.org/10.1139/v98-236.

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A new type of tetrafunctional reagent for cross-linking proteins has been prepared and used to modify human hemoglobin A. DPEE (1,2-bis{2-[3,5-bis(3,5-dibromosalicyloxycarbonyl) phenoxy]ethoxy}ethane)) has two separate pairs of reacting sites connected by a flexible tetraether chain. DPEE is capable of connecting a cross-link within a protein to another cross-link, either within the same protein molecule or between molecules. DPEE was readily prepared by esterification of a tetraether-linked bisphthalate (prepared by coupling of 1,2-bis(2-iodoethoxy)ethane and 5-hydroxyisophthalic acid). DPEE

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14

Yan, Dao-Jing, Hong Yuan, Wei Li, et al. "How a novel tyrosine–heme cross-link fine-tunes the structure and functions of heme proteins: a direct comparitive study of L29H/F43Y myoglobin." Dalton Transactions 44, no. 43 (2015): 18815–22. http://dx.doi.org/10.1039/c5dt03040d.

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15

Christoforo, Courtney, Haley Haws, and Andrew Smith. "Tough Slug Glue: How Transition Metal Binding Proteins Cross‐link an Unusual Bioadhesive." FASEB Journal 34, S1 (2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.04325.

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16

Slavin, Moriya, Tamar Tayri-Wilk, Hala Milhem, and Nir Kalisman. "Open Search Strategy for Inferring the Masses of Cross-Link Adducts on Proteins." Analytical Chemistry 92, no. 24 (2020): 15899–907. http://dx.doi.org/10.1021/acs.analchem.0c03292.

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17

Solivio, Morwena J., Dessalegn B. Nemera, Larry Sallans, and Edward J. Merino. "Biologically Relevant Oxidants Cause Bound Proteins To Readily Oxidatively Cross-Link at Guanine." Chemical Research in Toxicology 25, no. 2 (2012): 326–36. http://dx.doi.org/10.1021/tx200376e.

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18

Akhand, Anwarul A., Masashi Kato, Haruhiko Suzuki, et al. "Carbonyl compounds cross-link cellular proteins and activate protein-tyrosine kinase p60c-Src." Journal of Cellular Biochemistry 72, no. 1 (1999): 1–7. http://dx.doi.org/10.1002/(sici)1097-4644(19990101)72:1<1::aid-jcb1>3.0.co;2-y.

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19

Sparrow, L. G., C. P. Robinson, A. Kirkpatrick, D. E. Rivett, and J. J. Gorman. "CNBR-induced formation of tryptathionine in proteins." Protein & Peptide Letters 4, no. 4 (1997): 271–76. http://dx.doi.org/10.2174/092986650404221017125245.

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Abstract: Cleavage of peptide bonds at methionine using cyanogen bromide under acid conditions is widely used in structural studies of proteins. Here we report a novel reaction in which a cross-link, tryptathionine, involving tryptophan and cysteine, may be introduced into certain proteins through the action of cyanogen bromide under acidic conditions. The reaction has been demonstrated both with free cysteine and with cysteine-containing peptides.

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20

Pujari, Suresh S., Yi Zhang, Shaofei Ji, Mark D. Distefano, and Natalia Y. Tretyakova. "Site-specific cross-linking of proteins to DNA via a new bioorthogonal approach employing oxime ligation." Chemical Communications 54, no. 49 (2018): 6296–99. http://dx.doi.org/10.1039/c8cc01300d.

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21

Slavin, Moriya, Joanna Zamel, Keren Zohar, et al. "Targeted in situ cross-linking mass spectrometry and integrative modeling reveal the architectures of three proteins from SARS-CoV-2." Proceedings of the National Academy of Sciences 118, no. 34 (2021): e2103554118. http://dx.doi.org/10.1073/pnas.2103554118.

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Atomic structures of several proteins from the coronavirus family are still partial or unavailable. A possible reason for this gap is the instability of these proteins outside of the cellular context, thereby prompting the use of in-cell approaches. In situ cross-linking and mass spectrometry (in situ CLMS) can provide information on the structures of such proteins as they occur in the intact cell. Here, we applied targeted in situ CLMS to structurally probe Nsp1, Nsp2, and nucleocapsid (N) proteins from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and obtained cross-link sets

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22

Bhagwat, Nikhil, Anna L. Olsen, Anderson T. Wang, et al. "XPF-ERCC1 Participates in the Fanconi Anemia Pathway of Cross-Link Repair." Molecular and Cellular Biology 29, no. 24 (2009): 6427–37. http://dx.doi.org/10.1128/mcb.00086-09.

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ABSTRACT Interstrand cross-links (ICLs) prevent DNA strand separation and, therefore, transcription and replication, making them extremely cytotoxic. The precise mechanism by which ICLs are removed from mammalian genomes largely remains elusive. Genetic evidence implicates ATR, the Fanconi anemia proteins, proteins required for homologous recombination, translesion synthesis, and at least two endonucleases, MUS81-EME1 and XPF-ERCC1. ICLs cause replication-dependent DNA double-strand breaks (DSBs), and MUS81-EME1 facilitates DSB formation. The subsequent repair of these DSBs occurs via homologo

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23

Tellinghuisen, Timothy L., and Richard J. Kuhn. "Nucleic Acid-Dependent Cross-Linking of the Nucleocapsid Protein of Sindbis Virus." Journal of Virology 74, no. 9 (2000): 4302–9. http://dx.doi.org/10.1128/jvi.74.9.4302-4309.2000.

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ABSTRACT The assembly of the alphavirus nucleocapsid core is a multistep event requiring the association of the nucleocapsid protein with nucleic acid and the subsequent oligomerization of capsid proteins into an assembled core particle. Although the mechanism of assembly has been investigated extensively both in vivo and in vitro, no intermediates in the core assembly pathway have been identified. Through the use of both truncated and mutant Sindbis virus nucleocapsid proteins and a variety of cross-linking reagents, a possible nucleic acid-protein assembly intermediate has been detected. The

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24

Dierkes, Lindsay E., Craig L. Peebles, Brian A. Firek, Roger W. Hendrix, and Robert L. Duda. "Mutational Analysis of a Conserved Glutamic Acid Required for Self-Catalyzed Cross-Linking of Bacteriophage HK97 Capsids." Journal of Virology 83, no. 5 (2008): 2088–98. http://dx.doi.org/10.1128/jvi.02000-08.

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ABSTRACT The capsid of bacteriophage HK97 is stabilized by ∼400 covalent cross-links between subunits which form without any action by external enzymes or cofactors. Cross-linking only occurs in fully assembled particles after large-scale structural changes bring together side chains from three subunits at each cross-linking site. Isopeptide cross-links form between asparagine and lysine side chains on two subunits. The carboxylate of glutamic acid 363 (E363) from a third subunit is found ∼2.4 Å from the isopeptide bond in the partly hydrophobic pocket that contains the cross-link. It was pre

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Friedrich, Michael G., Zhen Wang, Kevin L. Schey, and Roger J. W. Truscott. "Mechanism of protein cleavage at asparagine leading to protein–protein cross-links." Biochemical Journal 476, no. 24 (2019): 3817–34. http://dx.doi.org/10.1042/bcj20190743.

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Long-lived proteins (LLPs) are present in numerous tissues within the human body. With age, they deteriorate, often leading to the formation of irreversible modifications such as peptide bond cleavage and covalent cross-linking. Currently understanding of the mechanism of formation of these cross-links is limited. As part of an ongoing study, proteomics was used to characterise sites of novel covalent cross-linking in the human lens. In this process, Lys residues were found cross-linked to C-terminal aspartates that had been present in the original protein as Asn residues. Cross-links were ide

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Schäfer, Christian, Christian Zacherl, Karl-Heinz Engel, Sybille Neidhart, and Reinhold Carle. "Comparative study of gelation and cross-link formation during enzymatic texturisation of leguminous proteins." Innovative Food Science & Emerging Technologies 8, no. 2 (2007): 269–78. http://dx.doi.org/10.1016/j.ifset.2007.01.005.

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27

Lin, Lo-Wei, Michael S. Denison, and Robert H. Rice. "Woodsmoke Extracts Cross-Link Proteins and Induce Cornified Envelope Formation without Stimulating Keratinocyte Terminal Differentiation." Toxicological Sciences 183, no. 1 (2021): 128–38. http://dx.doi.org/10.1093/toxsci/kfab071.

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Abstract Air pollution poses a serious risk to human health. To help understand the contribution of smoke from wood burning to the harmfulness of air pollution toward the skin, we studied the effects of liquid smoke, aqueous extracts of wood smoke condensate, a commercially available food flavor additive, in cultured keratinocytes. We report that liquid smoke can react with and cross-link keratinocyte cellular proteins, leading to abnormal cross-linked envelope formation. Instead of inducing genes ordinarily involved in terminal differentiation, liquid smoke induced expression of genes associa

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Masdar, Huriatul. "The Link Of Epstein Barr Virus Infection And Rheumatoid Arthritis Immunopathogenesis." Jurnal Ilmu Kedokteran 4, no. 2 (2017): 79. http://dx.doi.org/10.26891/jik.v4i2.2010.79-88.

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The cause of Rheumatoid Arthritis (RA) remains unknown. Environmental factors as well as genetic factors have beenlinked to pathogenesis of RA, in particular Epstein Barr Virus (EBV) infection. Since clinical onset of RA is long timeafter primary viral exposure, it is still difficult to demonstrate the direct link of EBV infection with RA pathogenesis.However, the high levels of antibodies against several EBV proteins detected in RA patient sera, the molecular mimicryof EBV proteins with RA susceptible alleles, cross reactive of several antibodies against EBV with proteins in RAsynovium, the h

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Summerscales, Joanna, and John F. Dawson. "Probing Dictyostelium severin structure and function by cross linking to actin." Biochemistry and Cell Biology 82, no. 2 (2004): 343–50. http://dx.doi.org/10.1139/o04-002.

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DS151 is the first 151 amino acids of the Dictyostelium discoidium protein severin, which shares high sequence similarity with segment 1 of the actin-severing protein gelsolin. DS151 is able to mediate the depolymerization of F-actin in a calcium-dependent fashion, much like segment 1 of gelsolin. A structural model of DS151 was obtained by comparative modeling studies with segment 1 of gelsolin. This model was tested by studies of chemical cross linking between DS151 and bound actin, suggesting that Cys residues on DS151 are cross linked with Lys residues of actin. The model suggests that Cys

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Cai, Shang, Lesley N. Weaver, Stephanie C. Ems-McClung, and Claire E. Walczak. "Kinesin-14 Family Proteins HSET/XCTK2 Control Spindle Length by Cross-Linking and Sliding Microtubules." Molecular Biology of the Cell 20, no. 5 (2009): 1348–59. http://dx.doi.org/10.1091/mbc.e08-09-0971.

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Kinesin-14 family proteins are minus-end directed motors that cross-link microtubules and play key roles during spindle assembly. We showed previously that the Xenopus Kinesin-14 XCTK2 is regulated by Ran via the association of a bipartite NLS in the tail of XCTK2 with importin α/β, which regulates its ability to cross-link microtubules during spindle formation. Here we show that mutation of the nuclear localization signal (NLS) of human Kinesin-14 HSET caused an accumulation of HSET in the cytoplasm, which resulted in strong microtubule bundling. HSET overexpression in HeLa cells resulted in

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Tellinghuisen, Timothy L., Rushika Perera, and Richard J. Kuhn. "In Vitro Assembly of Sindbis Virus Core-Like Particles from Cross-Linked Dimers of Truncated and Mutant Capsid Proteins." Journal of Virology 75, no. 6 (2001): 2810–17. http://dx.doi.org/10.1128/jvi.75.6.2810-2817.2001.

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ABSTRACT A nucleic acid-bound capsid protein dimer was previously identified using a Sindbis virus in vitro nucleocapsid assembly system and cross-linking reagents. Cross-link mapping, in combination with a model of the nucleocapsid core, suggested that this dimer contained one monomer from each of two adjacent capsomeres. This intercapsomere dimer is believed to be the initial intermediate in the nucleocapsid core assembly mechanism. This paper presents the purification of cross-linked dimers of a truncated capsid protein and the partial purification of cross-linked dimers of a full-length as

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Karić, Amina, and Mohamed Ragab Abdel Gawwad. "In silico interactome analysis of cross-link repair proteins (RPA32b and RPA2) in Arabidopsis thaliana." Bioengineering Studies 2, no. 1 (2021): 19–30. http://dx.doi.org/10.37868/bes.v2i1.id180.

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DNA molecule is found in every cell in a living organism and function as an instruction manual for growth, development, as well as any other processes that happen. As the cell divide, it needs to copy its DNA. During the copying, an error can occur, which can lead to a disease. However, there are different error repair mechanisms that are searching for an error, and repairing it. This study focused on 2 proteins involved in DNA repair mechanism, RPA32B and RPA2 from Arabidopsis thaliana. Throughout multiple in silico approached, multiple sequence alignment, phylogenetic tree construction, 3D v

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Zhang, D., and M. Rosbash. "Identification of eight proteins that cross-link to pre-mRNA in the yeast commitment complex." Genes & Development 13, no. 5 (1999): 581–92. http://dx.doi.org/10.1101/gad.13.5.581.

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Cheng, Rongzhu, Qi Feng, Ognyan K. Argirov, and Beryl J. Ortwerth. "Structure Elucidation of a Novel Yellow Chromophore from Human Lens Protein." Journal of Biological Chemistry 279, no. 44 (2004): 45441–49. http://dx.doi.org/10.1074/jbc.m405664200.

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We report here the isolation of a novel acid-labile yellow chromophore from the enzymatic digest of human lens proteins and the identification of its chemical structure by liquid chromatography-mass spectrometry, liquid chromatography-tandem mass spectrometry, and1H,13C, and two-dimensional NMR. This new chromophore exhibited a UV absorbance maximum at 343 nm and fluorescence at 410 nm when excited at 343 nm. Analysis of the purified compound by reversed-phase HPLC with in-line electrospray ionization mass spectrometry revealed a molecular mass of 370 Da. One- and two-dimensional NMR analyses

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Ross, Daniel E., Shane S. Ruebush, Susan L. Brantley, et al. "Characterization of Protein-Protein Interactions Involved in Iron Reduction by Shewanella oneidensis MR-1." Applied and Environmental Microbiology 73, no. 18 (2007): 5797–808. http://dx.doi.org/10.1128/aem.00146-07.

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ABSTRACT The interaction of proteins implicated in dissimilatory metal reduction by Shewanella oneidensis MR-1 (outer membrane [OM] proteins OmcA, MtrB, and MtrC; OM-associated protein MtrA; periplasmic protein CctA; and cytoplasmic membrane protein CymA) were characterized by protein purification, analytical ultracentrifugation, and cross-linking methods. Five of these proteins are heme proteins, OmcA (83 kDa), MtrC (75 kDa), MtrA (32 kDa), CctA (19 kDa), and CymA (21 kDa), and can be visualized after sodium dodecyl sulfate-polyacrylamide gel electrophoresis by heme staining. We show for the

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Chaubet, Loïc, Abdullah R. Chaudhary, Hossein K. Heris, Allen J. Ehrlicher, and Adam G. Hendricks. "Dynamic actin cross-linking governs the cytoplasm’s transition to fluid-like behavior." Molecular Biology of the Cell 31, no. 16 (2020): 1744–52. http://dx.doi.org/10.1091/mbc.e19-09-0504.

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Cells constantly adapt their mechanics in response to mechanical and biochemical cues to migrate, divide, and organize into tissues. We developed new methods to probe the viscoelasticity of the cytoplasm and found that the binding kinetics of proteins that cross-link actin filaments control the transition from an elastic to a fluid-like network.

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Aamodt, E. J., and J. G. Culotti. "Microtubules and microtubule-associated proteins from the nematode Caenorhabditis elegans: periodic cross-links connect microtubules in vitro." Journal of Cell Biology 103, no. 1 (1986): 23–31. http://dx.doi.org/10.1083/jcb.103.1.23.

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The nematode Caenorhabditis elegans should be an excellent model system in which to study the role of microtubules in mitosis, embryogenesis, morphogenesis, and nerve function. It may be studied by the use of biochemical, genetic, molecular biological, and cell biological approaches. We have purified microtubules and microtubule-associated proteins (MAPs) from C. elegans by the use of the anti-tumor drug taxol (Vallee, R. B., 1982, J. Cell Biol., 92:435-44). Approximately 0.2 mg of microtubules and 0.03 mg of MAPs were isolated from each gram of C. elegans. The C. elegans microtubules were sma

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Lederer, Markus O., and Holger P. Bühler. "Cross-linking of proteins by maillard processes—characterization and detection of a lysine-arginine cross-link derived from d-glucose." Bioorganic & Medicinal Chemistry 7, no. 6 (1999): 1081–88. http://dx.doi.org/10.1016/s0968-0896(99)00040-1.

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Yang, Pok Kwan, Coralie Hoareau, Carine Froment, Bernard Monsarrat, Yves Henry, and Guillaume Chanfreau. "Cotranscriptional Recruitment of the Pseudouridylsynthetase Cbf5p and of the RNA Binding Protein Naf1p during H/ACA snoRNP Assembly." Molecular and Cellular Biology 25, no. 8 (2005): 3295–304. http://dx.doi.org/10.1128/mcb.25.8.3295-3304.2005.

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ABSTRACT H/ACA small nucleolar ribonucleoprotein particles (snoRNPs) are essential for the maturation and pseudouridylation of the precursor of rRNAs and other stable RNAs. Although the RNA and protein components of these RNPs have been identified, the mechanisms by which they are assembled in vivo are poorly understood. Here we show that the RNA binding protein Naf1p, which is required for H/ACA snoRNPs stability, associates with RNA polymerase II-associated proteins Spt16p, Tfg1p, and Sub1p and with H/ACA snoRNP proteins. Chromatin immunoprecipitation experiments show that Naf1p and the pseu

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Strauß, Tobias, Saskia Schattner, Stefan Hoth, and Wilhelm J. Walter. "The Arabidopsis thaliana Kinesin-5 AtKRP125b Is a Processive, Microtubule-Sliding Motor Protein with Putative Plant-Specific Functions." International Journal of Molecular Sciences 22, no. 21 (2021): 11361. http://dx.doi.org/10.3390/ijms222111361.

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The formation and maintenance of the mitotic spindle during cell division requires several microtubule-interacting motor proteins. Members of the kinesin-5 family play an essential role in the bipolar organization of the spindle. These highly conserved, homotetrameric proteins cross-link anti-parallel microtubules and slide them apart to elongate the spindle during the equal separation of chromosomes. Whereas vertebrate kinesin-5 proteins are well studied, knowledge about the biochemical properties and the function of plant kinesin-5 proteins is still limited. Here, we characterized the proper

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Kluger, Ronald. "2001 Lemieux Award Lecture Organic chemistry and hemoglobin: Benefits from controlled alteration." Canadian Journal of Chemistry 80, no. 3 (2002): 217–21. http://dx.doi.org/10.1139/v01-200.

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Hemoglobin carries oxygen in circulation within red cells but does not function outside the cells because it fails not only to release oxygen but also dissociates into dimers that make up the tetrameric protein. Bifunctional anionic acylating agents that contain a structurally rigid bridge introduce cross-links that stabilize hemoglobin and alter its oxygen affinity so that it could be used to carry oxygen outside cells. Nitric oxide binds to hemoglobin and in circulation this causes undesirable increases in blood pressure. It had been reported that higher weight collections of hemoglobin do n

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Dietl, Andreas, Wouter J. Maalcke, Christina Ferousi, Mike S. M. Jetten, Boran Kartal, and Thomas R. M. Barends. "A 60-heme reductase complex from an anammox bacterium shows an extended electron transfer pathway." Acta Crystallographica Section D Structural Biology 75, no. 3 (2019): 333–41. http://dx.doi.org/10.1107/s2059798318017473.

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The hydroxylamine oxidoreductase/hydrazine dehydrogenase (HAO/HDH) protein family constitutes an important group of octaheme cytochromes c (OCCs). The majority of these proteins form homotrimers, with their subunits being covalently attached to each other via a rare cross-link between the catalytic heme moiety and a conserved tyrosine residue in an adjacent subunit. This covalent cross-link has been proposed to modulate the active-site heme towards oxidative catalysis by distorting the heme plane. In this study, the crystal structure of a stable complex of an HAO homologue (KsHAOr) with its di

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Martina, LOI Laura QUINTIERI Francesca FANELLI Vania C. LIUZZI Miriam HAIDUKOWSKI Antonio F. LOGRIECO Giuseppina MULÈ. "Rimozione della aflatossina M1 e potenziali applicativi di una laccasi da Pleurotus eryngii per la sicurezza del latte." Scienza e Tecnica Lattiero-Casearia 67, no. 1-2 (2017): 23–32. https://doi.org/10.5281/zenodo.822778.

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Aflatoxin M1 removal and potential applications of a laccase enzyme from Pleurotus eryngii for milk safety - Aflatoxin M1 (AFM1), is the main catabolite deriving from the hydroxylation of aflatoxin B1 (AFB1), found in the milk of animals fed with AFB1 contaminated feeds. The International Agency for the Research on Cancer (IARC) has classified it in group 2B, thus possibly carcinogenic for humans. Their maximum limit in raw milk, heat-treated milk and milk for the manufacture of milk-based products, has been set by the Regulation (EC) 1881 of 2006 to 50ng/kg. AFM1 resists to the most common tr

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Liu, Zhi-Ren, Bruno Sargueil, and Christopher W. J. Smith. "Detection of a Novel ATP-Dependent Cross-Linked Protein at the 5′ Splice Site-U1 Small Nuclear RNA Duplex by Methylene Blue-Mediated Photo-Cross-Linking." Molecular and Cellular Biology 18, no. 12 (1998): 6910–20. http://dx.doi.org/10.1128/mcb.18.12.6910.

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ABSTRACT Assembly of spliceosomes involves a number of sequential steps in which small nuclear ribonucleoprotein particles (snRNPs) and some non-snRNP proteins recognize the splice site sequences and undergo various conformational rearrangements. A number of important intermolecular RNA-RNA duplexes are formed transiently during the process of splice site recognition. Various steps in the assembly pathway are dependent upon ATP hydrolysis, either for protein phosphorylation or for the activity of helicases, which may modulate the RNA structures. Major efforts have been made to identify protein

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Volkmann, Niels, David DeRosier, Paul Matsudaira, and Dorit Hanein. "An Atomic Model of Actin Filaments Cross-Linked by Fimbrin and Its Implications for Bundle Assembly and Function." Journal of Cell Biology 153, no. 5 (2001): 947–56. http://dx.doi.org/10.1083/jcb.153.5.947.

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Actin bundles have profound effects on cellular shape, division, adhesion, motility, and signaling. Fimbrin belongs to a large family of actin-bundling proteins and is involved in the formation of tightly ordered cross-linked bundles in the brush border microvilli and in the stereocilia of inner ear hair cells. Polymorphism in these three-dimensional (3D) bundles has prevented the detailed structural characterization required for in-depth understanding of their morphogenesis and function. Here, we describe the structural characterization of two-dimensional arrays of actin cross-linked with hum

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Campbell, E. J., S. A. MacKinlay, and T. H. MacRae. "Cross-linking of microtubules by microtubule-associated proteins (MAPs) from the brine shrimp, Artemia." Journal of Cell Science 93, no. 1 (1989): 29–39. http://dx.doi.org/10.1242/jcs.93.1.29.

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Microtubules induced with taxol to assemble in cell-free extracts of the brine shrimp, Artemia, are cross-linked by microtubule-associated proteins (MAPs). When the MAPs, extracted from taxol-stabilized microtubules with 1 M-NaCl are co-assembled with purified Artemia or mammalian neural tubulin, reconstitution of cross-linking between microtubules occurs. The most prominent non-tubulin protein associated with reconstituted cross-linked microtubules has a molecular weight of 49,000 but we cannot yet exclude the possibility that other proteins may be responsible for the cross-linking. Cross-lin

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Perkins, S. J., A. S. Nealis, D. G. Dunham, T. E. Hardingham, and I. H. Muir. "Neutron and X-ray solution-scattering studies of the ternary complex between proteoglycan-binding region, link protein and hyaluronan." Biochemical Journal 285, no. 1 (1992): 263–68. http://dx.doi.org/10.1042/bj2850263.

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Proteoglycan aggregates of cartilage are stabilized by the formation of a ternary complex between the G1 domain at the N-terminus of the proteoglycan monomer (aggrecan), link protein and hyaluronan polysaccharide. Both the G1 domain and link protein contain similar three-domain structures formed from an immunoglobulin fold and two proteoglycan tandem repeats, the arrangement of which had been investigated by neutron and synchrotron X-ray scattering [Perkins, Nealis, Dunham, Hardingham & Muir (1991) Biochemistry 30, 10708-10716]. Here, solution scattering was used to investigate the ternary

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Lambert, Muriel W., Laura W. McMahon та Deepa M. Sridharan. "α II Spectrin Interacts with Specific Proteins in the Nucleus: Relevance to Fanconi Anemia." Blood 106, № 11 (2005): 184. http://dx.doi.org/10.1182/blood.v106.11.184.184.

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Abstract Fanconi anemia (FA) is a genetic disorder characterized by bone marrow failure, a predisposition to cancer, congenital abnormalities and a cellular hypersensitivity to DNA interstrand cross-linking agents. We have previously shown that in FA cells there is a deficiency in the structural protein nonerythroid spectrin (α SpII∑*) and that this deficiency correlates with a defect in ability to repair DNA interstrand cross-links. In order to get a better understanding of the exact role that α IISp∑* plays in the repair of cross-links and the repair defect in FA, whether it may have additio

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Cain, Peter, Iris Holdermann, Irmgard Sinning, Arthur E. Johnson, and Colin Robinson. "Binding of chloroplast signal recognition particle to a thylakoid membrane protein substrate in aqueous solution and delineation of the cpSRP43–substrate interaction domain." Biochemical Journal 437, no. 1 (2011): 149–55. http://dx.doi.org/10.1042/bj20110270.

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A cpSRP [chloroplast SRP (signal recognition particle)] comprising cpSRP54 and cpSRP43 subunits mediates the insertion of light-harvesting proteins into the thylakoid membrane. We dissected its interaction with a full-length membrane protein substrate in aqueous solution by insertion of site-specific photo-activatable cross-linkers into in vitro-synthesized Lhcb1 (major light-harvesting chlorophyll-binding protein of photosystem II). We show that Lhcb1 residues 166–176 cross-link specifically to the cpSRP43 subunit. Some cross-link positions within Lhcb1 are in the ‘L18’ peptide required for t

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Thomson, Timothy M., and Marta Guerra-Rebollo. "Ubiquitin and SUMO signalling in DNA repair." Biochemical Society Transactions 38, no. 1 (2010): 116–31. http://dx.doi.org/10.1042/bst0380116.

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The repair of lesions and gaps in DNA follows different pathways, each mediated by specific proteins and complexes. Post-translational modifications in many of these proteins govern their activities and interactions, ultimately determining whether a particular pathway is followed. Prominent among these modifications are the addition of phosphate or ubiquitin (and ubiquitin-like) moieties that confer new binding surfaces and conformational states on the modified proteins. The present review summarizes some of consequences of ubiquitin and ubiquitin-like modifications and interactions that regul

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