Helen Saibil
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British molecular biologist
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Why Is Helen Saibil Influential?
(Suggest an Edit or Addition)According to Wikipedia, Helen Ruth Saibil FRS FMedSci is a Canadian-British molecular biologist and Professor of Structural Biology at the Department of Crystallography of Birkbeck, University of London. Her research is largely focuses on molecular chaperones and protein misfolding.
Helen Saibil's Published Works
Number of citations in a given year to any of this author's works
Total number of citations to an author for the works they published in a given year. This highlights publication of the most important work(s) by the author
Published Works
- The protofilament structure of insulin amyloid fibrils (2002) (801)
- Chaperone machines for protein folding, unfolding and disaggregation (2013) (777)
- A small heat shock protein stably binds heat‐denatured model substrates and can maintain a substrate in a folding‐competent state (1997) (749)
- Cryo‐electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing (1999) (492)
- Hsp26: a temperature‐regulated chaperone (1999) (453)
- Atomic structure and hierarchical assembly of a cross-β amyloid fibril (2013) (453)
- Structural Basis of Pore Formation by the Bacterial Toxin Pneumolysin (2005) (421)
- Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes (1995) (418)
- The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL (1996) (387)
- Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations. (1999) (373)
- Structural basis for the regulated protease and chaperone function of DegP (2008) (360)
- The structural basis for membrane binding and pore formation by lymphocyte perforin (2010) (359)
- Structure of a Type IV Secretion System Core Complex (2009) (343)
- Location of a folding protein and shape changes in GroELGroES complexes imaged by cryo-electron microscopy (1994) (331)
- GroEL-GroES Cycling ATP and Nonnative Polypeptide Direct Alternation of Folding-Active Rings (1999) (303)
- The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter. (2005) (295)
- Structure of an Hsp90-Cdc37-Cdk4 complex. (2006) (292)
- Human Hsp70 Disaggregase Reverses Parkinson's-Linked α-Synuclein Amyloid Fibrils. (2015) (292)
- ATP-Bound States of GroEL Captured by Cryo-Electron Microscopy (2001) (287)
- T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol (1992) (279)
- Interaction between prion protein and toxic amyloid β assemblies can be therapeutically targeted at multiple sites (2011) (278)
- Secretin PulD: association with pilot PulS, structure, and ion-conducting channel formation. (1999) (215)
- ATP induces large quaternary rearrangements in a cage-like chaperonin structure (1993) (200)
- A Liquid to Solid Phase Transition Underlying Pathological Huntingtin Exon1 Aggregation (2018) (195)
- Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain. (2001) (194)
- Perforin forms transient pores on the target cell plasma membrane to facilitate rapid access of granzymes during killer cell attack. (2013) (193)
- Two Structural Transitions in Membrane Pore Formation by Pneumolysin, the Pore-Forming Toxin of Streptococcus pneumoniae (1999) (188)
- Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL (2000) (185)
- Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure. (2001) (174)
- Structural Analysis of Macromolecular Assemblies by Electron Microscopy (2011) (171)
- Chaperone machines in action. (2008) (169)
- Direct three-dimensional visualization of membrane disruption by amyloid fibrils (2012) (165)
- Outcome of the First wwPDB Hybrid/Integrative Methods Task Force Workshop. (2015) (163)
- ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin (2012) (160)
- Allosteric signaling of ATP hydrolysis in GroEL–GroES complexes (2006) (158)
- Visualization of macromolecular structures (2010) (150)
- Structure and allostery of the chaperonin GroEL. (2013) (145)
- The Calcium Channel α2δ-2 Subunit Partitions with CaV2.1 into Lipid Rafts in Cerebellum: Implications for Localization and Function (2006) (142)
- The mechanism of pore formation by bacterial toxins. (2006) (141)
- Processing of Plasmodium falciparum Merozoite Surface Protein MSP1 Activates a Spectrin-Binding Function Enabling Parasite Egress from RBCs (2015) (139)
- Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin (2014) (138)
- Atypical AAA+ Subunit Packing Creates an Expanded Cavity for Disaggregation by the Protein-Remodeling Factor Hsp104 (2007) (132)
- The molecular basis for perforin oligomerization and transmembrane pore assembly. (2009) (129)
- The chaperonin folding machine. (2002) (126)
- Neutron diffraction studies of retinal rod outer segment membranes (1976) (125)
- Amyloid-β nanotubes are associated with prion protein-dependent synaptotoxicity (2013) (120)
- Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins. (2000) (120)
- Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex. (2007) (115)
- Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF (2013) (113)
- Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation (2014) (112)
- Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy. (2001) (108)
- Motor Mechanism for Protein Threading through Hsp104 (2009) (107)
- Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system (2009) (107)
- Structure of the poly-C9 component of the complement membrane attack complex (2016) (107)
- Conformational Changes during Pore Formation by the Perforin-Related Protein Pleurotolysin (2015) (105)
- Molecular cloning and primary structure of squid (Loligo forbesi) rhodopsin, a phospholipase C-directed G-protein-linked receptor. (1991) (104)
- Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase (2017) (102)
- Topologies of a Substrate Protein Bound to the Chaperonin GroEL (2007) (102)
- A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization. (2004) (102)
- Conformational changes studied by cryo-electron microscopy (2000) (93)
- Chaperonin complex with a newly folded protein encapsulated in the folding chamber (2009) (93)
- Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. (2006) (92)
- Structure of a bacterial type III secretion system in contact with a host membrane in situ (2015) (85)
- Chlamydiae Assemble a Pathogen Synapse to Hijack the Host Endoplasmic Reticulum (2012) (84)
- Light- and GTP-activated hydrolysis of phosphatidylinositol bisphosphate in squid photoreceptor membranes. (1988) (83)
- An ordered membrane-cytoskeleton network in squid photoreceptor microvilli. (1982) (82)
- Detection and separation of heterogeneity in molecular complexes by statistical analysis of their two-dimensional projections. (2008) (81)
- Three conformations of an archaeal chaperonin, TF55 from Sulfolobus shibatae. (2000) (77)
- ATP-Driven Molecular Chaperone Machines (2013) (77)
- Binding of chaperonins (1991) (77)
- Globular Tetramers of β2-Microglobulin Assemble into Elaborate Amyloid Fibrils (2009) (75)
- RNA channelling by the eukaryotic exosome (2010) (75)
- A protease cascade regulates release of the human malaria parasite Plasmodium falciparum from host red blood cells (2018) (74)
- Cryo electron microscopy to determine the structure of macromolecular complexes (2016) (72)
- Folding with and without encapsulation by cis‐ and trans‐only GroEL–GroES complexes (2003) (71)
- Parasitophorous vacuole poration precedes its rupture and rapid host erythrocyte cytoskeleton collapse in Plasmodium falciparum egress (2017) (71)
- Real-time visualization of perforin nanopore assembly. (2017) (71)
- Cryo-EM of amyloid fibrils and cellular aggregates. (2019) (70)
- Biophysics (communication arising): Is rhodopsin dimeric in native retinal rods? (2003) (69)
- Molecular chaperones and folding catalysts (1999) (69)
- The calcium channel alpha2delta-2 subunit partitions with CaV2.1 into lipid rafts in cerebellum: implications for localization and function. (2006) (68)
- Three-dimensional structure of an invertebrate rhodopsin and basis for ordered alignment in the photoreceptor membrane. (2001) (68)
- Macromolecular structure determination by cryo-electron microscopy. (2000) (68)
- Elongated oligomers assemble into mammalian PrP amyloid fibrils. (2006) (66)
- Subunit organisation and symmetry of pore‐forming, oligomeric pneumolysin (1995) (64)
- Recognition and separation of single particles with size variation by statistical analysis of their images. (2004) (64)
- Projection structure of an invertebrate rhodopsin. (1996) (62)
- Structure determination of macromolecular assemblies by single-particle analysis of cryo-electron micrographs. (2004) (61)
- Domain rotations between open, closed and bullet-shaped forms of the thermosome, an archaeal chaperonin. (2000) (60)
- Separating and visualising protein assemblies by means of preparative mass spectrometry and microscopy. (2010) (60)
- Biophysics: is rhodopsin dimeric in native retinal rods? (2003) (60)
- Outcome of a workshop on archiving structural models of biological macromolecules. (2006) (59)
- A light‐stimulated increase of cyclic GMP in squid photoreceptors (1984) (57)
- Squid rhodopsin and GTP-binding protein crossreact with vertebrate photoreceptor enzymes. (1984) (55)
- Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ (2011) (55)
- A spiral scaffold underlies cytoadherent knobs in Plasmodium falciparum-infected erythrocytes. (2016) (54)
- Ex vivo mammalian prions are formed of paired double helical prion protein fibrils (2016) (53)
- Structural basis of allosteric changes in the GroEL mutant Arg197→Ala (1997) (52)
- Orientation of rhodopsin alpha-helices in in retinal rod outer segment membranes studied by infrared linear dichroism. (1979) (50)
- A novel and rapid method for obtaining high titre intact prion strains from mammalian brain (2015) (50)
- A 3D cellular context for the macromolecular world (2014) (48)
- GroEL/GroES‐mediated protein folding (2006) (46)
- 2.7 Å cryo-EM structure of ex vivo RML prion fibrils (2021) (45)
- Go hybrid: EM, crystallography, and beyond. (2012) (44)
- A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation (2004) (44)
- Methods for three-dimensional reconstruction of heterogeneous assemblies. (2010) (43)
- The membrane attack complex, perforin and cholesterol-dependent cytolysin superfamily of pore-forming proteins (2016) (43)
- Structures of unliganded and ATP-bound states of the Escherichia coli chaperonin GroEL by cryoelectron microscopy. (2001) (43)
- Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding. (2001) (43)
- Pathogen–host reorganization during Chlamydia invasion revealed by cryo-electron tomography (2014) (42)
- Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures (2012) (40)
- REMBI: Recommended Metadata for Biological Images—enabling reuse of microscopy data in biology (2021) (39)
- Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor (2019) (38)
- Yeast Ty retrotransposons assemble into virus-like particles whose T-numbers depend on the C-terminal length of the capsid protein. (1999) (36)
- Ordered transmembrane and extracellular structure in squid photoreceptor microvilli (1987) (36)
- Challenges at the frontiers of structural biology (2002) (35)
- Multiple states of a nucleotide-bound group 2 chaperonin. (2008) (35)
- The thermosome: chaperonin with a built-in lid (1998) (33)
- Structural features distinguishing infectious ex vivo mammalian prions from non-infectious fibrillar assemblies generated in vitro (2019) (32)
- Building bridges between cellular and molecular structural biology (2017) (31)
- Location of auxilin within a clathrin cage. (2004) (30)
- Cryo-electron microscopy structure of yeast Ty retrotransposon virus-like particles (1997) (29)
- An expanded protein folding cage in the GroEL-gp31 complex. (2006) (28)
- An expanded and flexible form of the vacuolar ATPase membrane sector. (2006) (28)
- Activation of the GTP-binding protein Gq by rhodopsin in squid photoreceptors. (1992) (28)
- Visualization of cyclic nucleotide binding sites in the vertebrate retina by fluorescence microscopy (1989) (27)
- Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery (2015) (26)
- The lid that shapes the pot: structure and function of the chaperonin GroES. (1996) (24)
- A national facility for biological cryo-electron microscopy (2015) (22)
- Cryo electron microscopy structures of Hsp100 proteins: crowbars in or out? (2010) (21)
- N-terminal Domain of Prion Protein Directs Its Oligomeric Association* (2014) (21)
- Structure and Function of the Squid Eye (1990) (20)
- Friend or foe: the same fold for attack and defense. (2008) (19)
- Effect of the C‐terminal proline repeats on ordered packing of squid rhodopsin and its mobility in membranes (1995) (19)
- Electron Bio-Imaging Centre (eBIC): the UK national research facility for biological electron microscopy (2017) (19)
- Atomic force microscopy of membrane pore formation by cholesterol dependent cytolysins. (2016) (17)
- Rhodopsin, Gq and phospholipase C activation in cephalopod photoreceptors. (1996) (15)
- Structure of an Hsp 90-Cdc 37-Cdk 4 complex (2017) (14)
- Cryo-EM in molecular and cellular biology (2022) (14)
- Rhodopsin mobility, structure, and lipid-protein interaction in squid photoreceptor membranes. (1993) (14)
- Structural basis of pore formation by cholesterol-binding toxins. (2000) (14)
- Making connections: snapshots of chlamydial type III secretion systems in contact with host membranes. (2015) (13)
- The black widow's versatile venom (2000) (12)
- Machinery to Reverse Irreversible Aggregates (2013) (11)
- Physical analysis of light-scattering changes in bovine photoreceptor membrane suspensions. (1984) (11)
- Malaria Parasite Schizont Egress Antigen-1 Plays an Essential Role in Nuclear Segregation during Schizogony (2021) (10)
- How chaperones tell wrong from right (1994) (9)
- A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin (2018) (9)
- Effects of calcium on light-activated GTP-binding proteins in squid photoreceptor membranes. (1991) (9)
- A structural basis for prion strain diversity (2022) (9)
- Neutron diffraction studies of oriented retinal rods. (1976) (7)
- Electron microscopy of chaperonins. (1998) (7)
- The pore conformation of lymphocyte perforin (2021) (6)
- The PDB and protein homeostasis: From chaperones to degradation and disaggregase machines (2021) (6)
- Blob-ology and biology of cryo-EM: an interview with Helen Saibil (2017) (5)
- Correlative light and electron microscopy suggests that mutant huntingtin dysregulates the endolysosomal pathway in presymptomatic Huntington’s disease (2021) (5)
- Pathogen-host reorganisation during Chlamydia invasion revealed by cryo-electron tomography 1 (2014) (5)
- Cooperative amyloid fibre binding and disassembly by the Hsp70 disaggregase (2021) (5)
- Linear dichroism studies in the visible, UV, and IR on oriented rod suspensions. (1982) (5)
- Perforin proteostasis is regulated through its C2 domain: supra-physiological cell death mediated by T431D-perforin (2018) (4)
- What can electron microscopy tell us about chaperoned protein folding? (1996) (4)
- Triggering and Amplification (1986) (4)
- Rival transmitters in visual transduction (1982) (3)
- Chaperonin Structure and Conformational Changes (1996) (3)
- Three-Dimensional Structural Analysis of Amyloid Fibrils by Electron Microscopy (2006) (2)
- Molecular Machines in Biology: The GroEL/GroES Chaperonin Machine (2011) (2)
- THE RELATIONSHIP BETWEEN CHAPERONIN STRUCTURE AND FUNCTION (1999) (2)
- Structural basis of ubiquitin-independent PP1 complex disassembly by p97 (2022) (2)
- Publisher Correction: A protease cascade regulates release of the human malaria parasite Plasmodium falciparum from host red blood cells (2018) (2)
- Recent advances in biological imaging (1989) (2)
- Birefringence and vision (1974) (1)
- Prion 2016 Poster Abstracts (2016) (1)
- Low-resolution phasing (2000) (1)
- Corrigendum to “Elongated Oligomers Assemble into Mammalian PrP Amyloid Fibrils” [J. Mol. Biol. 357 (2006) 975–985] (2006) (1)
- The prepore structure of pneumolysin, obtained by fitting the alpha carbon trace of perfringolysin O into a cryo-EM map (2005) (1)
- Cryo-Electron Microscopy of Vitreous Sections (CEMOVIS) of Yeast (2016) (1)
- Processing of Plasmodium falciparum Merozoite Surface Protein MSP 1 Activates a Spectrin-Binding Function Enabling Parasite Egress from RBCs Graphical (2015) (1)
- ATOMIC-RESOLUTION STRUCTURE OF A CROSS-BETA QUADRUPLET AMYLOID FIBRIL DETERMINED BY SOLID-STATE MAGIC ANGLE SPINNING NMR AND CRYO-EM (2013) (1)
- ATP-triggered molecular mechanics of the chaperonin GroEL (2012) (1)
- facilitate rapid access of granzymes during killer cell attack Perforin forms transient pores on the target cell plasma membrane to (2013) (1)
- Membrane embedded pleurotolysin pore with 13 fold symmetry (2015) (0)
- Molecular studies of prion propagation (2000) (0)
- Atomic-resolution structure of a doublet cross-beta amyloid fibril (2013) (0)
- Dumoux, Maud and Nans, Andrea and Saibil, Helen R. and Hayward, Richard D. (2015) Making connections: snapshots of chlamydial type III (2021) (0)
- REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)-ATP7 CRYO-EM MAP (EMD 1047) (2006) (0)
- ATP-bound states of GroEL and GroEL-GroES captured by cryo-EM and single particle image processing (2002) (0)
- Symmetrized cryo-EM reconstruction of E. coli DegQ 12-mer in complex with lysozymes (2012) (0)
- Solution Structure of GroEL(D398A)+ 250uM ATP by Cryo-Electron microscopy (2002) (0)
- Title Amyloid-b nanotubes are associated with prion protein-dependent synaptotoxicity (0)
- Atomic-resolution structure of a quadruplet cross-beta amyloid fibril (2013) (0)
- Structural characterization of ex vivo mammalian prions isolated from multiple strains (2016) (0)
- Rival transmitter in visual transduction. (1982) (0)
- Blob-ology and biology of cryo-EM: an interview with Helen Saibil (2017) (0)
- Electron Microscopy of Macromolecular Machines (2012) (0)
- Publisher Correction: A protease cascade regulates release of the human malaria parasite Plasmodium falciparum from host red blood cells (2018) (0)
- Symmetrized cryo-EM reconstruction of E. coli DegQ 12-mer in complex with a binding peptide (2012) (0)
- 1 1 A protease cascade regulates release of the human malaria parasite Plasmodium falciparum from host 2 red blood cells 3 4 5 (2018) (0)
- Asymmetric cryo-EM reconstruction of E. coli DegQ 12-mer in complex with lysozyme (2011) (0)
- DegP dodecamer with bound OMP (2012) (0)
- ClpB (DWB mutant) bound to casein in presence of ATPgammaS - state WT-1 (2019) (0)
- Signal and noise. Biological signal transduction (1991). Edited by E. M. Ross and K. W. A. Wirtz. Springer Verlag, Berlin. 540pp. DM 260. ISBN 3-4 540-51773-1 (1992) (0)
- P117 3D cryo-electron microscopic analysis of the disease mechanism of α1-antitrypsin deficiency (2011) (0)
- A protease cascade regulates release of the human malaria parasite Plasmodium falciparum from host red blood cells (2018) (0)
- Chaperones and protein folding (2012) (0)
- Negative-stain electron microscopy of E. coli ClpB (BAP form bound to ClpP) (2014) (0)
- Machines and networks (2002) (0)
- Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein (2012) (0)
- Cells in distress (1997) (0)
- Structural changes in the bacterial toxin pneumolysin during pore formation (2005) (0)
- Perforin proteostasis is regulated through its C2 domain: supra-physiological cell death mediated by T431D-perforin (2018) (0)
- The relationship between chaperonin structure and function. Chapter 23 (1999) (0)
- Cryo electron-micrscopy of chaperonin-assisted protein folding (1995) (0)
- Author response: Building bridges between cellular and molecular structural biology (2017) (0)
- Calcium Inhibits GTP-Binding Proteins in Squid Photoreceptors (1989) (0)
- BIROn - Birkbeck Institutional Research Online coiled-coil domains regulate ClpB cooperation in disaggregation. (2021) (0)
- ClpB (DWB and K476C mutant) bound to casein in presence of ATPgammaS - state KC-1 (2019) (0)
- Spiers Memorial Lecture: Challenges in cryo electron microscopy. (2022) (0)
- Structure and mechanism of the bacterial protein toxin, pneumolysin (1999) (0)
- Cryo electron microscopy structures of Hsp 100 proteins : crowbars in or out ? 1 (2009) (0)
- Atomic-resolution structure of a cross-beta protofilament (2013) (0)
- 86. Principles and application of cryo electron microscopy to macromolecular and cellular structures (2010) (0)
- Negative stain EM reconstruction of M.tuberculosis Acr1(Hsp 16.3) fitted with wheat sHSP dimer (2005) (0)
- Cryo EM structure of the E. coli disaggregase ClpB (BAP form, DWB mutant), in the ATPgammaS state (2017) (0)
- Negative-stain electron microscopy of E. coli ClpB mutant E432A (BAP form bound to ClpP) (2014) (0)
- Atomic-resolution structure of a triplet cross-beta amyloid fibril (2013) (0)
- Photoexcited rhodopsin (R*) and GTP-binding protein (G) cross-react in squid and bovine photoreceptors (1984) (0)
- Sample preparation in single particle cryo-EM: general discussion. (2022) (0)
- Dodecameric structure of the small heat shock protein Acr1 from Mycobacterium tuberculosis. VOLUME 280 (2005) PAGES 33419-33425 (2005) (0)
- Chaperonin structure and function (2000) (0)
- SOLUTION STRUCTURE OF GROES-ADP7-GROEL-ATP7 COMPLEX BY CRYO-EM (2002) (0)
- Pushing the limits in single particle cryo-EM: general discussion. (2022) (0)
- Biophysical analysis of the insulin amyloid assembly process (2000) (0)
- RED CELLS , IRON , AND ERYTHROPOIESIS A spiral scaffold underlies cytoadherent knobs in Plasmodium falciparum – infected erythrocytes (2015) (0)
- Correlative light and electron microscopy suggests that mutant huntingtin dysregulates the endolysosomal pathway in presymptomatic Huntington’s disease (2021) (0)
- Solution Structure of apo GroEL by Cryo-Electron microscopy (2002) (0)
- Molecular chaperone structure and function (2000) (0)
- Crystal structure of DegP24 (2008) (0)
- Fitted coordinates for GroEL-ADP7-GroES Cryo-EM complex (EMD-1181) (2006) (0)
- 3.10 Chaperones and Protein Folding (2012) (0)
- Correction: Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin (2015) (0)
- Map/model validation and machine learning in EM: general discussion. (2022) (0)
- Structural features distinguishing infectious ex vivo mammalian prions from non-infectious fibrillar assemblies generated in vitro (2019) (0)
- Erratum: Dodecameric structure of the small heat shock protein Acr1 from Mycobacterium tuberculosis (Journal of Biological Chemistry (2005) 280 (33419-33425)) (2005) (0)
- Cryo-EM structure of DegP12/OMP (2008) (0)
- Cryo EM structure of the E. coli disaggregase ClpB (BAP form, DWB mutant), in the ATPgammaS state, bound to the model substrate casein (2017) (0)
- Membrane bound pleurotolysin prepore (TMH2 strand lock) trapped with engineered disulphide cross-link (2015) (0)
- Structural journey of an insecticidal pore-forming protein targeting western corn rootworm (2022) (0)
- Sequential roles for red blood cell binding proteins enable phased commitment to invasion for malaria parasites (2022) (0)
- Macromolecular assemblies: Editorial overview (2009) (0)
- Author response: Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation (2014) (0)
- Negative-stain electron microscopy of E. coli ClpB of Y503D hyperactive mutant (BAP form bound to ClpP) (2014) (0)
- Correlative light and electron microscopy reveals that mutant huntingtin dysregulates the endolysosomal pathway in presymptomatic Huntington’s disease (2021) (0)
- Cryo-EM studies of protein aggregation and disaggregation (2017) (0)
- Macromolecular assemblies. (2009) (0)
- 39. Cryo-preparation techniques in Transmission Electron Microscopy (2010) (0)
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