Publications
327 results found
Zhang XD, Moréra S, Bates PA, et al., 1998, Structure of an XRCC1 BRCT domain:: a new protein-protein interaction module, EMBO JOURNAL, Vol: 17, Pages: 6404-6411, ISSN: 0261-4189
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- Citations: 208
Hodges M, Tissot C, Freemont PS, 1998, Protein regulation: Tag wrestling with relatives of ubiquitin, CURRENT BIOLOGY, Vol: 8, Pages: R749-R752, ISSN: 0960-9822
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- Citations: 32
Saurin AJ, Shiels C, Williamson J, et al., 1998, The human polycomb group complex associates with pericentromeric heterochromatin to form a novel nuclear domain, Journal of Cell Biology, Vol: 142, Pages: 887-898, ISSN: 0021-9525
The Polycomb group (PcG) complex is a chromatin-associated multiprotein complex, involved in the stable repression of homeotic gene activity in Drosophila. Recently, a mammalian PcG complex has been identified with several PcG proteins implicated in the regulation of Hox gene expression. Although the mammalian PcG complex appears analogous to the complex in Drosophila, the molecular mechanisms and functions for the mammalian PcG complex remain unknown. Here we describe a detailed characterization of the human PcG complex in terms of cellular localization and chromosomal association. By using antibodies that specifically recognize three human PcG proteins— RING1, BMI1, and hPc2—we demonstrate in a number of human cell lines that the PcG complex forms a unique discrete nuclear structure that we term PcG bodies. PcG bodies are prominent novel nuclear structures with the larger PcG foci generally localized near the centromeres, as visualized with a kinetochore antibody marker. In both normal fetal and adult fibroblasts, PcG bodies are not randomly dispersed, but appear clustered into defined areas within the nucleus. We show in three different human cell lines that the PcG complex can tightly associate with large pericentromeric heterochromatin regions (1q12) on chromosome 1, and with related pericentromeric sequences on different chromosomes, providing evidence for a mammalian PcG–heterochromatin association. Furthermore, these heterochromatin-bound PcG complexes remain stably associated throughout mitosis, thereby allowing the potential inheritance of the PcG complex through successive cell divisions. We discuss these results in terms of the known function of the PcG complex as a transcriptional repression complex.
Hodges M, Tissot C, Howe K, et al., 1998, Structure, organization, and dynamics of promyelocytic leukemia protein nuclear bodies, AMERICAN JOURNAL OF HUMAN GENETICS, Vol: 63, Pages: 297-304, ISSN: 0002-9297
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- Citations: 142
Everett RD, Freemont P, Saitoh H, et al., 1998, The disruption of ND10 during herpes simplex virus infection correlates with the Vmw11O- and proteasome-dependent loss of several PML isoforms, JOURNAL OF VIROLOGY, Vol: 72, Pages: 6581-6591, ISSN: 0022-538X
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- Citations: 344
Lally JM, Newman RH, Knowles PP, et al., 1998, Crystallization of an intact GST-estrogen receptor hormone binding domain fusion protein, ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, Vol: 54, Pages: 423-426, ISSN: 0907-4449
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- Citations: 8
Cao TY, Duprez E, Borden KLB, et al., 1998, Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML, JOURNAL OF CELL SCIENCE, Vol: 111, Pages: 1319-1329, ISSN: 0021-9533
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- Citations: 76
Rabouille C, Kondo H, Newman R, et al., 1998, Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro, CELL, Vol: 92, Pages: 603-610, ISSN: 0092-8674
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- Citations: 219
Howe K, Williamson J, Boddy N, et al., 1998, The ubiquitin-homology gene <i>PIC1</i>:: Characterization of mouse (<i>Pic1</i>) and human (<i>UBL1</i>) genes and pseudogenes, GENOMICS, Vol: 47, Pages: 92-100, ISSN: 0888-7543
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- Citations: 23
Saha V, Young BD, Freemont PS, 1998, Translocations, fusion genes, and acute leukemia., J Cell Biochem Suppl, Vol: 30-31, Pages: 264-276, ISSN: 0733-1959
Genes involved in chromosomal translocations, associated with the formation of fusion proteins in leukemia, are modular in nature and regulatory in function. It is likely that they are involved in the initiation and maintenance of normal hematopoiesis. A conceptual model is proposed by which disruption of these different genes leads to the development of acute leukemia. Central to this model is the functional interaction between the mammalian trithorax and polycomb group protein complexes. Many of the genes identified in leukemia-associated translocations are likely upstream regulators, co-participators or downstream targets of these complexes. In the natural state, these proteins interact with each other to form multimeric higher-order structures, which sequentially regulate the development of the normal hematopoietic state, either through HOX gene expression or other less defined pathways. The novel interaction domains acquired by the chimaeric fusion products subvert normal cellular control mechanisms, which result in both a failure of cell maturation and activation of anti-apoptotic pathways. The mechanisms by which these translocation products are able to affect these processes are thought to lie at the level of chromatin-mediated transcriptional activation and/or repression. The stimuli for proliferation and development of clinically overt disease may require subsequent mutations in more than one oncogene or tumor suppressor gene, or both. A more comprehensive catalogue of mutation events in malignant cells is therefore required to understand the key regulatory networks that serve to maintain multipotentiality and in particular the modifications which initiate and coordinate commitment in differentiating hematopoietic cells. We propose a model in which common pathways for leukemogenesis lie along the cell cycle control of chromatin structure in terms of transcriptional activation or repression. A clearer understanding of this cascade will provide opportunities
Saha V, Young BD, Freemont PS, 1998, Translocations, fusion genes, and acute leukemia, JOURNAL OF CELLULAR BIOCHEMISTRY, Pages: 264-+, ISSN: 0730-2312
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- Citations: 17
Grimwade D, Gorman P, Duprez E, et al., 1997, Characterization of cryptic rearrangements and variant translocations in acute promyelocytic leukemia, BLOOD, Vol: 90, Pages: 4876-4885, ISSN: 0006-4971
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- Citations: 118
Gorman MA, Morera S, Rothwell DG, et al., 1997, The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites, EMBO JOURNAL, Vol: 16, Pages: 6548-6558, ISSN: 0261-4189
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- Citations: 278
Dokurno P, Lally JM, Bates PA, et al., 1997, Crystallization of an antitumour antibody SM3 complexed with a peptide epitope, ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, Vol: 53, Pages: 780-781, ISSN: 2059-7983
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- Citations: 1
Boddy MN, Duprez E, Borden KLB, et al., 1997, Surface residue mutations of the PML RING finger domain alter the formation of nuclear matrix-associated PML bodies, JOURNAL OF CELL SCIENCE, Vol: 110, Pages: 2197-2205, ISSN: 0021-9533
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- Citations: 37
Kondo H, Rabouille C, Newman R, et al., 1997, p47 is a cofactor for p97-mediated membrane fusion, NATURE, Vol: 388, Pages: 75-78, ISSN: 0028-0836
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- Citations: 357
Dokurno P, Lally JM, Bates PA, et al., 1997, Crystallization of the Fab fragment of the tumour-specific antibody PR1A3, ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, Vol: 53, Pages: 472-473, ISSN: 0907-4449
Cao TY, Borden KLB, Freemont PS, et al., 1997, Involvement of the rfp tripartite motif in protein-protein interactions and subcellular distribution, JOURNAL OF CELL SCIENCE, Vol: 110, Pages: 1563-1571, ISSN: 0021-9533
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- Citations: 97
Satijn DPE, Gunster MJ, vanderVlag J, et al., 1997, RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor, MOLECULAR AND CELLULAR BIOLOGY, Vol: 17, Pages: 4105-4113, ISSN: 0270-7306
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- Citations: 163
Newman RH, Freemont PS, 1997, Electron microscopy of thin protein crystals from vapour diffusion 'hanging drops' provides structural information at intermediate resolution, NATO Advanced Study Institute on Electron Crystallography, Publisher: SPRINGER, Pages: 405-406, ISSN: 0168-132X
Rothwell DG, Barzilay G, Gorman M, et al., 1997, The structure and functions of the HAP1/Ref-1 protein, ONCOLOGY RESEARCH, Vol: 9, Pages: 275-280, ISSN: 0965-0407
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- Citations: 36
Vrielink A, Freemont PS, 1996, Chapter 5 Protein-nucleic acid recognition and interactions, Principles of Medical Biology, Vol: 5, Pages: 85-115, ISSN: 1569-2582
The application of protein crystallography and two-dimensional NMR to study proteins which interact with DNA has provided detailed information about protein-DNA recognition and specificity. Numerous structural motifs have evolved to allow a diverse variety of interactions between proteins and DNA. These include motifs such as the helix-turn-helix, zinc finger, basic region leucine zipper, and ribbon-helix-helix, some of which are found in both prokaryotes and eukaryotes. DNA recognition is usually achieved through specific protein amino acid-DNA base pair interactions which can be mediated via water molecules, in either the major or minor grooves of the DNA. However, interactions between protein side chains and the phosphodiester backbone is a common feature of non-sequence-specific protein-DNA recognition. The flexibility and existence of DNA in a number of different conformations contributes significantly to the overall process of protein-DNA recognition. The enormous variety of protein structures and motifs which can interact with DNA probably reflects the diversity of biological function which requires the formation of protein-DNA complexes. © 1996 Elsevier B.V. All rights reserved.
Saurin A, Borden K, Boddy M, et al., 1996, Does this have a familiar RING? (vol 21, pg 208, 1996), TRENDS IN BIOCHEMICAL SCIENCES, Vol: 21, Pages: 453-453, ISSN: 0968-0004
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- Citations: 4
Newman RH, Freemont PS, 1996, Use of planar lipid monolayers for 2D crystallisation of proteins and simple analysis of specific lipid-peptide interactions, 7th International Conference on Organized Molecular Films (LB7), Publisher: ELSEVIER SCIENCE SA LAUSANNE, Pages: 18-23, ISSN: 0040-6090
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- Citations: 1
Boddy MN, Howe K, Etkin LD, et al., 1996, PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia, ONCOGENE, Vol: 13, Pages: 971-982, ISSN: 0950-9232
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- Citations: 324
Borden KLB, Freemont PS, 1996, The RING finger domain: A recent example of a sequence-structure family, CURRENT OPINION IN STRUCTURAL BIOLOGY, Vol: 6, Pages: 395-401, ISSN: 0959-440X
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- Citations: 405
Saurin AJ, Borden KLB, Boddy MN, et al., 1996, Does this have a familiar RING?, TRENDS IN BIOCHEMICAL SCIENCES, Vol: 21, Pages: 208-214, ISSN: 0968-0004
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- Citations: 596
Newman RH, Whitehead P, Lally J, et al., 1996, 20S human proteasomes bind with a specific orientation to lipid monolayers in vitro, BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, Vol: 1281, Pages: 111-116, ISSN: 0005-2736
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- Citations: 13
Borden KLB, Lally JM, Martin SR, et al., 1996, In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 93, Pages: 1601-1606, ISSN: 0027-8424
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- Citations: 96
Otto WR, Rao JD, Cox HM, et al., 1996, Effects of pancreatic spasmolytic polypeptide (PSP) on epithelial cell function, EUROPEAN JOURNAL OF BIOCHEMISTRY, Vol: 235, Pages: 64-72, ISSN: 0014-2956
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- Citations: 37
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