Chunlin Lu

Summary

Affiliation: Duke University Medical Center
Country: USA

Publications

  1. pmc In vitro assembly and GTP hydrolysis by bacterial tubulins BtubA and BtubB
    Christopher A Sontag
    Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA
    J Cell Biol 169:233-8. 2005
  2. pmc Irisin and FNDC5 in retrospect: An exercise hormone or a transmembrane receptor?
    Harold P Erickson
    Departments of Cell Biology and Biochemistry Duke University Medical Center Durham, NC USA
    Adipocyte 2:289-93. 2013
  3. pmc BtubA-BtubB heterodimer is an essential intermediate in protofilament assembly
    Christopher A Sontag
    Department of Cell Biology, Duke University Medical Center, Durham, North Carolina, United States of America
    PLoS ONE 4:e7253. 2009
  4. pmc The coiled coils of cohesin are conserved in animals, but not in yeast
    Glenn E White
    Department of Biological and Environmental Sciences, Longwood University, Farmville, Virginia, United Kingdom
    PLoS ONE 4:e4674. 2009
  5. pmc Bacterial actin homolog ParM: arguments for an apolar, antiparallel double helix
    Harold P Erickson
    Departments of Cell Biology, Biochemistry, and Biomedical Engineering, Duke University, Durham, NC 27710 3709, USA
    J Mol Biol 422:461-3. 2012
  6. pmc Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy
    Harold P Erickson
    Department of Cell Biology, Duke University Medical Center, Durham, NC 27710 3709 USA
    Biol Proced Online 11:32-51. 2009
  7. pmc Modeling the physics of FtsZ assembly and force generation
    Harold P Erickson
    Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA
    Proc Natl Acad Sci U S A 106:9238-43. 2009
  8. pmc Site-specific mutations of FtsZ--effects on GTPase and in vitro assembly
    C Lu
    Dept of Cell Biology, 3709 Duke Univ, Med, Cntr, Durham, NC 27710, USA
    BMC Microbiol 1:7. 2001
  9. ncbi request reprint The FtsZ protofilament and attachment of ZipA--structural constraints on the FtsZ power stroke
    H P Erickson
    Department of Cell Biology, Box 3709, Research Drive, Duke University Medical Center, Durham, North Carolina 27710, USA
    Curr Opin Cell Biol 13:55-60. 2001
  10. ncbi request reprint Stretching fibronectin
    Harold P Erickson
    Department of Cell Biology, Box 3079, Duke University Medical Center, Durham, NC 27710, USA
    J Muscle Res Cell Motil 23:575-80. 2002

Research Grants

  1. EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINS
    HAROLD ERICKSON; Fiscal Year: 2006
  2. Structure and Assembly Dynamics of FtsZ
    HAROLD ERICKSON; Fiscal Year: 2007
  3. EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINS
    HAROLD ERICKSON; Fiscal Year: 2007
  4. EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINS
    HAROLD ERICKSON; Fiscal Year: 2009
  5. Structure and Assembly Dynamics of FtsZ
    HAROLD ERICKSON; Fiscal Year: 2009
  6. EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINS
    Harold P Erickson; Fiscal Year: 2010
  7. Structure and Assembly Dynamics of FtsZ
    Harold P Erickson; Fiscal Year: 2010
  8. Structure and Assembly Dynamics of FtsZ
    HAROLD ERICKSON; Fiscal Year: 2009
  9. Structure and Assembly Dynamics of FtsZ
    HAROLD ERICKSON; Fiscal Year: 2009
  10. Structure and Assembly Dynamics of FtsZ
    HAROLD ERICKSON; Fiscal Year: 2006

Collaborators

Detail Information

Publications49

  1. pmc In vitro assembly and GTP hydrolysis by bacterial tubulins BtubA and BtubB
    Christopher A Sontag
    Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA
    J Cell Biol 169:233-8. 2005
    ..37 per min when mixed 1:1 with BtubA. A critical concentration of 0.4-1.0 microM was indicated by light scattering experiments and extrapolation of GTPase versus concentration, thus suggesting a cooperative assembly mechanism...
  2. pmc Irisin and FNDC5 in retrospect: An exercise hormone or a transmembrane receptor?
    Harold P Erickson
    Departments of Cell Biology and Biochemistry Duke University Medical Center Durham, NC USA
    Adipocyte 2:289-93. 2013
    ..The original discovery proposing that FNDC5 may be a transmembrane receptor may deserve a new look...
  3. pmc BtubA-BtubB heterodimer is an essential intermediate in protofilament assembly
    Christopher A Sontag
    Department of Cell Biology, Duke University Medical Center, Durham, North Carolina, United States of America
    PLoS ONE 4:e7253. 2009
    ..A 1:1 mixture of the two proteins assembles into tubulin-like protofilaments, which further aggregate into pairs and bundles. The proteins also form a BtubA/B heterodimer, which appears to be a repeating subunit in the protofilament...
  4. pmc The coiled coils of cohesin are conserved in animals, but not in yeast
    Glenn E White
    Department of Biological and Environmental Sciences, Longwood University, Farmville, Virginia, United Kingdom
    PLoS ONE 4:e4674. 2009
    ..5%. These coiled coils are among the most highly conserved mammalian proteins, suggesting that they make extensive contacts over their entire surface...
  5. pmc Bacterial actin homolog ParM: arguments for an apolar, antiparallel double helix
    Harold P Erickson
    Departments of Cell Biology, Biochemistry, and Biomedical Engineering, Duke University, Durham, NC 27710 3709, USA
    J Mol Biol 422:461-3. 2012
    ..I present arguments here that ParM may be an apolar filament, in which the two helical strands are antiparallel...
  6. pmc Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy
    Harold P Erickson
    Department of Cell Biology, Duke University Medical Center, Durham, NC 27710 3709 USA
    Biol Proced Online 11:32-51. 2009
    ..A combination of hydrodynamics and electron microscopy is especially powerful...
  7. pmc Modeling the physics of FtsZ assembly and force generation
    Harold P Erickson
    Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA
    Proc Natl Acad Sci U S A 106:9238-43. 2009
    ..Finally, I address recent models that try to explain how protofilaments 1-subunit-thick show a cooperative assembly...
  8. pmc Site-specific mutations of FtsZ--effects on GTPase and in vitro assembly
    C Lu
    Dept of Cell Biology, 3709 Duke Univ, Med, Cntr, Durham, NC 27710, USA
    BMC Microbiol 1:7. 2001
    ..We have constructed 16 site-directed mutants of E. coli ftsZ, and tested them for GTP hydrolysis and assembly in vitro, and for their ability to complement the temperature sensitive ftsZ84 mutation in E. coli...
  9. ncbi request reprint The FtsZ protofilament and attachment of ZipA--structural constraints on the FtsZ power stroke
    H P Erickson
    Department of Cell Biology, Box 3709, Research Drive, Duke University Medical Center, Durham, North Carolina 27710, USA
    Curr Opin Cell Biol 13:55-60. 2001
    ..A model is proposed here for how membrane-bound ZipA can reach around the FtsZ protofilament to bind the carboxy-terminal peptide, which faces away from the membrane...
  10. ncbi request reprint Stretching fibronectin
    Harold P Erickson
    Department of Cell Biology, Box 3079, Duke University Medical Center, Durham, NC 27710, USA
    J Muscle Res Cell Motil 23:575-80. 2002
    ..The second proposes that molecules in fibrils are already extended, and stretching is produced by force-induced unfolding of FN type III domains. Experimental observations that may help distinguish these two possibilities are discussed...
  11. pmc FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one
    Harold P Erickson
    Department of Cell Biology, Box 3709, Duke University Medical Center, Durham, NC 27710, USA
    Microbiol Mol Biol Rev 74:504-28. 2010
    ..Recent efforts to develop antibacterial drugs that target FtsZ are reviewed. Finally, we discuss evidence of how FtsZ generates a constriction force: by protofilament bending into a curved conformation...
  12. pmc Evolution of the cytoskeleton
    Harold P Erickson
    Department of Cell Biology, Duke University Medical Center, Durham, NC 27710 3709, USA
    Bioessays 29:668-77. 2007
    ..The highly conserved amino acids are not those forming the subunit core or protofilament interface, but those involved in binding and hydrolysis of GTP...
  13. ncbi request reprint Atomic structures of tubulin and FtsZ
    H P Erickson
    Dept of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA
    Trends Cell Biol 8:133-7. 1998
    ..This article discusses these findings and the molecular mechanisms that can now be addressed with the atomic structures...
  14. ncbi request reprint FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima--quantitation, GTP hydrolysis, and assembly
    C Lu
    Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA
    Cell Motil Cytoskeleton 40:71-86. 1998
    ..Using this standard and quantitative Western blotting, we determined that the average E. coli cell has 15,000 molecules of FtsZ, at a concentration of 400 microg/ml. This is just above the plateau for full GTPase activity in vitro...
  15. ncbi request reprint Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?
    L Romberg
    Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA
    J Biol Chem 276:11743-53. 2001
    ..It predicts that unlike microtubules, FtsZ protofilaments consist of GTP-bound FtsZ subunits that hydrolyze their nucleotide only slowly and are connected by high affinity longitudinal bonds with a nanomolar K(D)...
  16. pmc Cell adhesion molecule L1 in folded (horseshoe) and extended conformations
    G Schurmann
    Duke University Medical Center, Department of Cell Biology, Durham, North Carolina 27710 3709, USA
    Mol Biol Cell 12:1765-73. 2001
    ..Our study resolves conflicting interpretations from previous electron microscopy studies of L1...
  17. pmc The symmetrical structure of structural maintenance of chromosomes (SMC) and MukB proteins: long, antiparallel coiled coils, folded at a flexible hinge
    T E Melby
    Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710 3011, USA
    J Cell Biol 142:1595-604. 1998
    ..The bifunctional symmetry and a possible scissoring action at the hinge should provide unique biomechanical properties to the SMC proteins...
  18. ncbi request reprint Oligomeric structure and tissue distribution of ficolins from mouse, pig and human
    T Ohashi
    Department of Cell Biology, Duke University Medical Center, Durham, North Carolina, 27710, USA
    Arch Biochem Biophys 360:223-32. 1998
    ..One ficolin gene in all species is expressed in liver and is the primary source of plasma ficolin. Expression of this gene in other tissues, and expression of the second ficolin gene, appears to vary in different species...
  19. ncbi request reprint Ultrastructural and biochemical properties of the 120-kDa form of chick kinectin
    J Kumar
    Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA
    J Biol Chem 273:31738-43. 1998
    ..Immunoprecipitation with a 160-kDa kinectin-specific antibody brought down the 120-kDa kinectin. Thus, we suggest that kinectin is an extended parallel coiled-coil dimer, often a heterodimer...
  20. ncbi request reprint Drosophila stretchin-MLCK is a novel member of the Titin/Myosin light chain kinase family
    M B Champagne
    Department of Cell Biology, Duke University Medical Center, Durham, NC, 27710 0001, USA
    J Mol Biol 300:759-77. 2000
    ....
  21. ncbi request reprint Structural analysis of a human glial variant laminin
    E K LeMosy
    Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA
    Exp Cell Res 227:80-8. 1996
    ..Together our results implicate human U251 MG glial laminin as a previously uncharacterized laminin isoform with strong adhesive activity for fibroblasts and glial cells...
  22. ncbi request reprint Structure of the Rad50 x Mre11 DNA repair complex from Saccharomyces cerevisiae by electron microscopy
    D E Anderson
    Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710 3709, USA
    J Biol Chem 276:37027-33. 2001
    ..We also demonstrate that Mre11 binds as a dimer between the catalytic domains of Rad50, bringing the nuclease activities of Mre11 in close proximity to the ATPase and DNA binding activities of Rad50...
  23. pmc Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain
    Tomoo Ohashi
    Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710 3709, USA
    J Bacteriol 184:4313-5. 2002
    ..We estimated a persistence length of 0.66 nm, which is similar to the persistence lengths of other unfolded and unstructured polypeptides...
  24. pmc FtsZ from divergent foreign bacteria can function for cell division in Escherichia coli
    Masaki Osawa
    Department Cell Biology, Box 3709, Duke University Medical Center, Durham, NC 27710, USA
    J Bacteriol 188:7132-40. 2006
    ..The C-terminal peptide of FtsZ, which binds FtsA, provides the link between FtsZ assembly and peptidoglycan remodeling...
  25. pmc Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching
    Jesse Stricker
    Department of Cell Biology, Duke University Medical Center, Box 3709, Durham, NC 27710, USA
    Proc Natl Acad Sci U S A 99:3171-5. 2002
    ..This finding implies that assembly dynamics are determined primarily by GTP hydrolysis. Despite the greatly reduced assembly dynamics, the ftsZ84 cells divide with a normal cell-cycle time...
  26. pmc An experimental study of GFP-based FRET, with application to intrinsically unstructured proteins
    Tomoo Ohashi
    Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA
    Protein Sci 16:1429-38. 2007
    ..We conclude that GFP-based FRET can be useful for studying intrinsically unstructured proteins, and we present a range of calibrated protein inserts to experimentally determine the distances that can be studied...
  27. pmc Assembly dynamics of Mycobacterium tuberculosis FtsZ
    Yaodong Chen
    Department of Cell Biology, Duke University, Medical Center, Durham, North Carolina 27710, USA
    J Biol Chem 282:27736-43. 2007
    ..7 was 42 s for MtbFtsZ compared with 5.5 s for EcFtsZ. Photobleaching studies in vivo showed a range of turnover half-times with an average of 25 s for MtbFtsZ as compared with 9 s for EcFtsZ...
  28. pmc In vitro assembly studies of FtsZ/tubulin-like proteins (TubZ) from Bacillus plasmids: evidence for a capping mechanism
    Yaodong Chen
    Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA
    J Biol Chem 283:8102-9. 2008
    ..This suggests that the TubZ polymers have a capping mechanism that may be related to the GTP cap that produces dynamic instability of microtubules...
  29. ncbi request reprint Domain unfolding plays a role in superfibronectin formation
    Tomoo Ohashi
    Department of Cell Biology, Duke University, Medical Center, Durham, North Carolina 27710, USA
    J Biol Chem 280:39143-51. 2005
    ..The model is consistent with our observation that the kinetics of aggregation are first order, with a reaction time of 500-700 s. Similar mechanisms may contribute to the assembly of the native FN matrix...
  30. ncbi request reprint Understanding the elasticity of fibronectin fibrils: unfolding strengths of FN-III and GFP domains measured by single molecule force spectroscopy
    Nehal I Abu-Lail
    Center for Biologically Inspired Materials and Material Systems, Duke University, Durham, NC 27708, USA
    Matrix Biol 25:175-84. 2006
    ..Our results thus favor an alternative model, which invokes a conformational change from a compact to an extended conformation, as the basis for FN fibril elasticity...
  31. ncbi request reprint Probing the domain structure of FtsZ by random truncation and insertion of GFP
    Masaki Osawa
    Dept of Cell Biology, 3709 Duke University Medical Center, Durham, NC 27710, USA
    Microbiology 151:4033-43. 2005
    ..Directional assembly could occur by either a treadmilling or a dynamic instability mechanism...
  32. pmc Force measurements of the alpha5beta1 integrin-fibronectin interaction
    Feiya Li
    Department of Physiology and Biophysics, University of Miami School of Medicine, Miami, Florida 33136, USA
    Biophys J 84:1252-62. 2003
    ..These results suggest that integrin activation involved a cooperative interaction with both the RGD and synergy sites...
  33. pmc In vivo characterization of Escherichia coli ftsZ mutants: effects on Z-ring structure and function
    Jesse Stricker
    Department of Cell Biology, Duke University Medical Center, Durham, North Carolina, USA
    J Bacteriol 185:4796-805. 2003
    ....
  34. ncbi request reprint The disulfide bonding pattern in ficolin multimers
    Tomoo Ohashi
    Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA
    J Biol Chem 279:6534-9. 2004
    ..We present a model in which symmetric Cys24-Cys24 disulfide bonds between trimers are the basis for multimerization. The model may also be relevant to collectin multimers...
  35. ncbi request reprint The role of the specificity-determining loop of the integrin beta subunit I-like domain in autonomous expression, association with the alpha subunit, and ligand binding
    Junichi Takagi
    The Center for Blood Research and Department of Pathology, Harvard Medical School, 200 Longwood Avenue, Boston, Massachusetts 02115, USA
    Biochemistry 41:4339-47. 2002
    ....
  36. pmc Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins
    David E Anderson
    Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA
    J Bacteriol 186:5775-81. 2004
    ..In B. subtilis, only 30 to 35% of the FtsZ protein was in the Z ring, from which we conclude that a Z ring only 2 or 3 protofilaments thick can function for cell division...
  37. pmc A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus
    Yaodong Chen
    Department of Cell Biology, Duke University Medical Center, Durham, North Carolina, USA
    Biophys J 88:505-14. 2005
    ..Fragmentation was absent in the model, another characteristic of cooperative assembly. We are left with an enigma: how can the FtsZ protofilament, which appears to be one-subunit thick, assemble with apparent cooperativity?..
  38. ncbi request reprint Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants
    Tomoo Ohashi
    Department of Cell Biology, Duke University Medical Center, NC27710, USA
    J Cell Sci 115:1221-9. 2002
    ..When the cell culture was treated with cytochalasin to disrupt the actin cytoskeleton, some fibrils contracted substantially, suggesting that the segment attached primarily to the cell surface is stretched...
  39. pmc Mutants of FtsZ targeting the protofilament interface: effects on cell division and GTPase activity
    Sambra D Redick
    Department of Cell Biology, Duke University, 3709 Duke University Medical Center, Durham, NC 27710, USA
    J Bacteriol 187:2727-36. 2005
    ..This is inconsistent with the present model of the protofilament, as a simple stack of subunits one on top of the other, and may require a new structural model...
  40. ncbi request reprint Localization of a cryptic binding site for tenascin on fibronectin
    Kenneth C Ingham
    Department of Biochemistry, American Red Cross Holland Laboratory, Rockville, MD 20896, USA
    J Biol Chem 279:28132-5. 2004
    ..The binding site on fibronectin appears to be cryptic in the whole molecule in solution but is exposed on the proteolytic fragments and probably when fibronectin is in the extended conformation...
  41. ncbi request reprint Apparent cooperative assembly of the bacterial cell division protein FtsZ demonstrated by isothermal titration calorimetry
    Michael R Caplan
    Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA
    J Biol Chem 278:13784-8. 2003
    ..The ITC data are highly suggestive of a cooperative assembly, although this is difficult to reconcile with the 1-subunit-thick protofilaments observed by electron microscopy...
  42. ncbi request reprint Trimers of the fibronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation
    Fran├žoise Coussen
    Department of Cell Biology, Box 3709, Duke University Medical Center, Durham, NC 27710, USA
    J Cell Sci 115:2581-90. 2002
    ..Beads containing monomer or dimer showed only brief binding and diffusive movements. We conclude that clusters of three integrin-binding ligands are necessary and sufficient for coupling to and translocating with the actin cytoskeleton...
  43. pmc The RGD motif in fibronectin is essential for development but dispensable for fibril assembly
    Seiichiro Takahashi
    Max Planck Institute of Biochemistry, Department of Molecular Medicine, 82152 Martinsried, Germany
    J Cell Biol 178:167-78. 2007
    ..Our findings demonstrate that FN contains a novel motif for integrin binding and fibril formation whose activity is controlled by amino acid modification...
  44. pmc Designing an extracellular matrix protein with enhanced mechanical stability
    Sean P Ng
    Cambridge University Chemical Laboratory, Medical Research Council Centre for Protein Engineering, Lensfield Road, Cambridge CB2 1EW, United Kingdom
    Proc Natl Acad Sci U S A 104:9633-7. 2007
    ..Thus, we have specifically designed a protein with increased mechanical stability. Our results demonstrate that core engineering can be used to change the mechanical strength of proteins while retaining functional surface interactions...
  45. pmc Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer
    Yaodong Chen
    Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA
    J Biol Chem 280:22549-54. 2005
    ..The mechanism may be related to the dynamic instability of microtubules...
  46. pmc Reconstitution of contractile FtsZ rings in liposomes
    Masaki Osawa
    Department of Cell Biology, Duke University Medical Center, Durham, NC 27710 3709, USA
    Science 320:792-4. 2008
    ..Brighter Z rings produced visible constrictions in the liposome, suggesting that FtsZ itself can assemble the Z ring and generate a force. No other proteins were needed for assembly and force generation...
  47. ncbi request reprint Sequence divergence of coiled coils--structural rods, myosin filament packing, and the extraordinary conservation of cohesins
    Glenn E White
    School of Pharmacy, Wingate University, Wingate, NC 28174, USA
    J Struct Biol 154:111-21. 2006
    ..Finally, analysis of the heptad repeat shows that the a and d positions are more constrained in spacer rods, and the bcefg positions more constrained in skeletal muscle myosin...

Research Grants27

  1. EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINS
    HAROLD ERICKSON; Fiscal Year: 2006
    ..After our initial applications and testing in FN, these sensors should be widely applicable to determine the tension in other ECM and cytoskeletal systems. ..
  2. Structure and Assembly Dynamics of FtsZ
    HAROLD ERICKSON; Fiscal Year: 2007
    ..We will use high concentrations of the independently folding N-and C-terminal domains, to determine how they poison pf assembly and dynamics. We will also attempt to re-create the dimer nucleus from these domains. ..
  3. EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINS
    HAROLD ERICKSON; Fiscal Year: 2007
    ..After our initial applications and testing in FN, these sensors should be widely applicable to determine the tension in other ECM and cytoskeletal systems. ..
  4. EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINS
    HAROLD ERICKSON; Fiscal Year: 2009
    ..After our initial applications and testing in FN, these sensors should be widely applicable to determine the tension in other ECM and cytoskeletal systems. ..
  5. Structure and Assembly Dynamics of FtsZ
    HAROLD ERICKSON; Fiscal Year: 2009
    ..We will use high concentrations of the independently folding N-and C-terminal domains, to determine how they poison pf assembly and dynamics. We will also attempt to re-create the dimer nucleus from these domains. ..
  6. EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINS
    Harold P Erickson; Fiscal Year: 2010
    ..After our initial applications and testing in FN, these sensors should be widely applicable to determine the tension in other ECM and cytoskeletal systems. ..
  7. Structure and Assembly Dynamics of FtsZ
    Harold P Erickson; Fiscal Year: 2010
    ..It also has potential clinical relevance. FtsZ is highly conserved in bacteria, and is an attractive target for new antibiotics. Several lead compounds targeting FtsZ are already being studied and developed. ..
  8. Structure and Assembly Dynamics of FtsZ
    HAROLD ERICKSON; Fiscal Year: 2009
    ..We will use high concentrations of the independently folding N-and C-terminal domains, to determine how they poison pf assembly and dynamics. We will also attempt to re-create the dimer nucleus from these domains. ..
  9. Structure and Assembly Dynamics of FtsZ
    HAROLD ERICKSON; Fiscal Year: 2009
    ..We will use high concentrations of the independently folding N-and C-terminal domains, to determine how they poison pf assembly and dynamics. We will also attempt to re-create the dimer nucleus from these domains. ..
  10. Structure and Assembly Dynamics of FtsZ
    HAROLD ERICKSON; Fiscal Year: 2006
    ..We will use high concentrations of the independently folding N-and C-terminal domains, to determine how they poison pf assembly and dynamics. We will also attempt to re-create the dimer nucleus from these domains. ..
  11. Structure and Assembly Dynamics of FtsZ
    HAROLD ERICKSON; Fiscal Year: 2005
    ..Overall, we are aiming for a complete characterization of the biophysics of FtsZ protofilament assembly in vitro, and complementary analysis by FRAP of assembly dynamics and function in vivo. ..
  12. EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINS
    HAROLD ERICKSON; Fiscal Year: 2005
    ..5 if the knockout is from the beginning). FN is expressed during the development of many organs after E10, so our timed knockout should demonstrate where and how FN is important in organ development. ..
  13. EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINS
    HAROLD ERICKSON; Fiscal Year: 1990
    ..We will use a combination light scattering and electron microscopy to characterize small polymers of these two proteins, and especially to investigate the question of nucleation of polymerization...
  14. EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINS
    HAROLD ERICKSON; Fiscal Year: 1991
    ..We will use a combination light scattering and electron microscopy to characterize small polymers of these two proteins, and especially to investigate the question of nucleation of polymerization...
  15. EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINS
    HAROLD ERICKSON; Fiscal Year: 1992
    ..We will use a combination light scattering and electron microscopy to characterize small polymers of these two proteins, and especially to investigate the question of nucleation of polymerization...
  16. EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINS
    HAROLD ERICKSON; Fiscal Year: 2001
    ..5 if the knockout is from the beginning). FN is expressed during the development of many organs after E10, so our timed knockout should demonstrate where and how FN is important in organ development. ..
  17. EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINS
    HAROLD ERICKSON; Fiscal Year: 2002
    ..5 if the knockout is from the beginning). FN is expressed during the development of many organs after E10, so our timed knockout should demonstrate where and how FN is important in organ development. ..
  18. Structure and Assembly Dynamics of FtsZ
    HAROLD ERICKSON; Fiscal Year: 2002
    ..Overall, we are aiming for a complete characterization of the biophysics of FtsZ protofilament assembly in vitro, and complementary analysis by FRAP of assembly dynamics and function in vivo. ..
  19. Zeiss LSM510 META confocal-fluorescence spectroscopy
    HAROLD ERICKSON; Fiscal Year: 2003
    ..Projects for this module are proposed by two faculty from Cell Biology and two from Biochemistry. This will be the only FCS facility at Duke University, and we expect additional projects from across the campus. ..
  20. Structure and Assembly Dynamics of FtsZ
    HAROLD ERICKSON; Fiscal Year: 2003
    ..Overall, we are aiming for a complete characterization of the biophysics of FtsZ protofilament assembly in vitro, and complementary analysis by FRAP of assembly dynamics and function in vivo. ..
  21. EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINS
    HAROLD ERICKSON; Fiscal Year: 2003
    ..5 if the knockout is from the beginning). FN is expressed during the development of many organs after E10, so our timed knockout should demonstrate where and how FN is important in organ development. ..
  22. EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINS
    HAROLD ERICKSON; Fiscal Year: 2004
    ..5 if the knockout is from the beginning). FN is expressed during the development of many organs after E10, so our timed knockout should demonstrate where and how FN is important in organ development. ..
  23. Structure and Assembly Dynamics of FtsZ
    HAROLD ERICKSON; Fiscal Year: 2004
    ..Overall, we are aiming for a complete characterization of the biophysics of FtsZ protofilament assembly in vitro, and complementary analysis by FRAP of assembly dynamics and function in vivo. ..
  24. Structure and Assembly Dynamics of FtsZ
    Harold P Erickson; Fiscal Year: 2010
    ..It also has potential clinical relevance. FtsZ is highly conserved in bacteria, and is an attractive target for new antibiotics. Several lead compounds targeting FtsZ are already being studied and developed. ..