USC-F1.2-k0.15 - NanoWorld®

Type: USC-F1.2-k0.15

Ultra-Short Cantilevers (for High-Speed AFM)

Cantilever Data	Value	Range*
Resonance Frequency	1200 kHz	800 - 1600 kHz
Force Constant	0.15 N/m	0.06 - 0.3 N/m
Length	7 µm	6 - 8 µm
Mean Width	2 µm	1.5 - 2.5 µm
Thickness	0.08 µm	0.06 - 0.1 µm

*Typical values

How to optimize AFM scan parameters

This AFM probe has alignment grooves on the back side of the support chip.

USC cantilever 3D view More images

Product Description

NanoWorld® Ultra-Short Cantilevers (USC) for High-Speed AFM (HS-AFM) combine very small AFM cantilevers capable of resonating in the MHz regime and a very sharp and wear resistant AFM tip.

The AFM cantilever of the USC series is rectangular and made of a quartz-like material. A gold layer is deposited on both sides of the AFM cantilever in order to enhance the reflectance of the laser beam, but the AFM tip remains uncoated.

The wear resistant AFM tip has been developed together with nanotools GmbH and sustains high velocity scans over long distances. It is made of High Density Carbon/Diamond Like Carbon (HDC/DLC) material which is hard and wear resistant. It has a height of 2.5 microns and a radius of curvature smaller than 10 nm. The aspect ratio is in the order of 5 : 1 and the tilt compensation is 8° ensuring more symmetric AFM images.

The silicon support chip is of standard dimensions (1.6 mm x 3.4 mm x 0.3 mm). Additionally, it has etched and lowered corners in order to avoid contact between the support chip and the sample when scanning. Moreover it features alignment grooves on the back side of the silicon support chip which ensure replacement of the AFM probes without major adjustment of the laser beam when used in conjunction with the alignment chip.

The type USC-F1.2-k0.15 is mainly designed for High-Speed AFM applications in liquid but can also be used for applications in air (depending on the application).

Tip shape: Cone Shaped

Coating: Reflective Gold

Gold Reflex Coating

The gold reflex coating consists of a 20 nm thick gold layer deposited on both sides of the AFM cantilevers which enhances the reflectance of the laser beam. Furthermore it prevents light from interfering within the AFM cantilever. As the coating is almost stress-free the bending of the AFM cantilevers due to stress is less than 2 degrees.

The AFM tip remains uncoated.

Order Codes

Order Code	Quantity	Data Sheet
USC-F1.2-k0.15-10	10	Nominal values

System limitations: Due to their small AFM cantilever sizes and their very high resonance frequencies USC probes currently cannot be used in all commercially available SPMs and AFMs. Only AFMs with a sufficiently small laser spot and electronics that are capable of dealing with high resonance frequencies of up to 5 MHz are able to work with the USC probes. If in doubt whether these AFM probes can be used in your AFM please check back with us or with your AFM manufacturer.

Product Screencast NanoWorld® Ultra-Short Cantilevers (USC) for High Speed Scanning

Subscribe to NanoWorld® Youtube Channel

Guaranteed values

Scientific publications mentioning use of this AFM probe

Daniel J. Barrero, Sithara S. Wijeratne, Xiaowei Zhao, Grace F. Cunningham, Rui Yan, Christian R. Nelson, Yasuhiro Arimura, Hironori Funabiki, Charles L. Asbury, Zhiheng Yu, Radhika Subramanian and Sue Biggins
Architecture of native kinetochores revealed by structural studies utilizing a thermophilic yeast
Current Biology 34, 1–13 September 9, 2024
DOI: https://doi.org/10.1016/j.cub.2024.07.036

Shehrazade Jekhmane, Maik G. N. Derks, Sourav Maity, Cornelis J. Slingerland, Kamaleddin H. M. E. Tehrani, João Medeiros-Silva, Vicky Charitou, Danique Ammerlaan, Céline Fetz, Naomi A. Consoli, Rachel V. K. Cochrane, Eilidh J. Matheson, Mick van der Weijde, Barend O. W. Elenbaas, Francesca Lavore, Ruud Cox, Joseph H. Lorent, Marc Baldus, Markus Künzler, Moreno Lelli, Stephen A. Cochrane, Nathaniel I. Martin, Wouter H. Roos, Eefjan Breukink and Markus Weingarth
Host defence peptide plectasin targets bacterial cell wall precursor lipid II by a calcium-sensitive supramolecular mechanism
Nature Microbiology volume 9, pages 1778–1791 (2024)
DOI: https://doi.org/10.1038/s41564-024-01696-9

Clara Garcia-Sacristan, Victor G. Gisbert, Kevin Klein, Anđela Šarić and Ricardo Garcia
In Operando Imaging Electrostatic-Driven Disassembly and Reassembly of Collagen Nanostructure
ACS Nano 2024, 18, 28, 18485–18492
DOI: https://doi.org/10.1021/acsnano.4c03839

Kai Liu, Alex Blokhuis, Chris van Ewijk, Armin Kiani, Juntian Wu, Wouter H. Roos and Sijbren Otto
Light-driven eco-evolutionary dynamics in a synthetic replicator system
Nature Chemistry volume 16, pages 79–88 (2024)
DOI: https://doi.org/10.1038/s41557-023-01301-2

Tereza Kadavá, Johannes F Hevler, Sofia Kalaidopoulou Nteak, Victor C Yin, Juergen Strasser, Johannes Preiner, and Albert JR Heck
Higher-order structure and proteoforms of co-occurring C4b-binding protein assemblies in human serum
The EMBO Journal (2024) 43: 3009 – 3026
DOI: https://doi.org/10.1038/s44318-024-00128-y

Miloš Tišma, Richard Janissen, Hammam Antar, Alejandro Martin-Gonzalez, Roman Barth, Twan Beekman, Jaco van der Torre, Davide Michieletto, Stephan Gruber and Cees Dekker
Dynamic ParB–DNA interactions initiate and maintain a partition condensate for bacterial chromosome segregation
Nucleic Acids Research, Volume 51, Issue 21, 27 November 2023, Pages 11856–11875
DOI: https://doi.org/10.1093/nar/gkad868

Mst. Ayesha Siddika, Hiroki Oi, Kumi Hidaka, Hiroshi Sugiyama, Masayuki Endo, Shigeyoshi Matsumura and Yoshiya Ikawa
Structural Expansion of Catalytic RNA Nanostructures through Oligomerization of a Cyclic Trimer of Engineered Ribozymes
Molecules 2023, 28(18), 6465
DOI: https://doi.org/10.3390/molecules28186465

Hayden Burdett, Martina Foglizzo, Laura J Musgrove, Dhananjay Kumar, Gillian Clifford, Lisa J Campbell, George R Heath, Elton Zeqiraj and Marcus D Wilson
BRCA1–BARD1 combines multiple chromatin recognition modules to bridge nascent nucleosomes
Nucleic Acids Research, Volume 51, Issue 20, 10 November 2023, Pages 11080–11103
DOI: https://doi.org/10.1093/nar/gkad793

Shifra Lansky, John Michael Betancourt, Jingying Zhang, Yining Jiang, Elizabeth D Kim, Navid Paknejad, Crina M Nimigean, Peng Yuan and Simon Scheuring
A pentameric TRPV3 channel with a dilated pore
Nature. 2023 Sep; 621(7977): 206–214.
DOI: https://doi.org/10.1038/s41586-023-06470-1

Bibiana Onoa, César Díaz-Celis, Cristhian Cañari-Chumpitaz, Antony Lee and Carlos Bustamante
Real-Time Multistep Asymmetrical Disassembly of Nucleosomes and Chromatosomes Visualized by High-Speed Atomic Force Microscopy
ACS Central Science 2024, 10, 1, 122–137
DOI: https://doi.org/10.1021/acscentsci.3c00735

Eiji Nakata , Khongorzul Gerelbaatar, Mashal Asif, Hiroaki Konishi, Yuya Shibano, Peng Lin and Takashi Morii
A Ratiometric Fluorescent Probe for pH Measurement over a Wide Range Composed of Three Types of Fluorophores Assembled on a DNA Scaffold
Chemistry 2023, 5, 1832–1842.
DOI: https://doi.org/10.3390/chemistry5030125

Aline Cisse, Ambroise Desfosses, Sarah Stainer, Eaazhisai Kandiah, Daouda A.K. Traore, Armel Bezault, Anna-Laurence Schachner-Nedherer, Gerd Leitinger, Gerd Hoerl, Peter Hinterdorfer, Irina Gutsche, Ruth Prassl, Judith Peters and Karin Kornmueller
Targeting structural flexibility in low density lipoprotein by integrating cryo-electron microscopy and high-speed atomic force microscopy
International Journal of Biological Macromolecules, Volume 252, 1 December 2023, 126345
DOI: https://doi.org/10.1016/j.ijbiomac.2023.126345

Raghavendar R. Sanganna Gari, Grigory Tagiltsev, Ruth A. Pumroy, Yining Jiang, Martin Blackledge, Vera Y. Moiseenkova-Bell and Simon Scheuring
Intrinsically disordered regions in TRPV2 mediate protein-protein interactions
Nature Communications Biology volume 6, Article number: 966 (2023)
DOI: https://doi.org/10.1038/s42003-023-05343-7

Daisuke Noshiro and Nobuo N. Noda
Immobilization of lipid nanorods onto two-dimensional crystals of protein tamavidin 2 for high-speed atomic force microscopy
STAR Protocols, Volume 4, Issue 4, 15 December 2023, 102633
DOI: https://doi.org/10.1016/j.xpro.2023.102633

Tomoyuki Fukuda, Kentaro Furukawa, Tatsuro Maruyama, Shun-ichi Yamashita, Daisuke Noshiro, Chihong Song, Yuta Ogasawara, Kentaro Okuyama, Jahangir Md Alam, Manabu Hayatsu, Tetsu Saigusa, Keiichi Inoue, Kazuho Ikeda, Akira Takai, Lin Chen, Vikramjit Lahiri, Yasushi Okada, Shinsuke Shibata, Kazuyoshi Murata, Daniel J. Klionsky, Nobuo N. Noda and Tomotake Kanki
The mitochondrial intermembrane space protein mitofissin drives mitochondrial fission required for mitophagy
Molecular Cell 83, 2045–2058
DOI: https://doi.org/10.1016/j.molcel.2023.04.022

Adéla Melcrová, Sourav Maity, Josef Melcr, Niels A. W. de Kok, Mariella Gabler, Jonne van der Eyden, Wenche Stensen, John S. M. Svendsen, Arnold J. M. Driessen, Siewert J. Marrink and Wouter H. Roos
Lateral membrane organization as target of an antimicrobial peptidomimetic compound
Nature Communications volume 14, Article number: 4038 (2023)
DOI: https://doi.org/10.1038/s41467-023-39726-5

Ryo Ikeda, Daisuke Noshiro, Hideaki Morishita, Shuhei Takada, Shun Kageyama, Yuko Fujioka, Tomoko Funakoshi, Satoko Komatsu-Hirota, Ritsuko Arai, Elena Ryzhii, Manabu Abe, Tomoaki Koga, Hozumi Motohashi, Mitsuyoshi Nakao, Kenji Sakimura, Arata Horii, Satoshi Waguri, Yoshinobu Ichimura, Nobuo N Noda and Masaaki Komatsu
Phosphorylation of phase-separated p62 bodies by ULK1 activates a redox-independent stress response
The EMBO Journal (2023)42:e113349
DOI: https://doi.org/10.15252/embj.2022113349

Yanggang Pan, Emmi Pohjolainen, Philip A.M. Schmidpeter, Andrea C. Vaiana, Crina M. Mimigcan, Helmut Grubmüller and Simon Scheuring
Discrimination between cyclic nucleotides in a cyclic nucleotide-gate ion channel
Nature Structural & Molecular Biology, (2023) Volume 30, 512–520
https://www.nature.com/articles/s41594-023-00955-3.epdf?sharing_token=6O8iL4P9MuwM5lLYJ_9_c9RgN0jAjWel9jnR3ZoTv0MyC3dYzcGyXgCH2gWU83BtW0gKD4eEH0uFpEFFSMfTc4dgA7sKkEIDAXbCkasoprprf29Dv0p45esvx-WNiNsrAWObBmfCCvfdgPRbvnrnfPdDjYGhkxnA-Mr_dykJUHw%3D

Kimi Azad, Delphine Guilligay, Cecile Boscheron, Sourav Maity, Nicola De Franceschi, Guidenn Sulbaran, Gregory Effantin, Haiyan Wang, Jean-Philippe Kleman, Patricia Bassereau, Guy Schoehn, Wouter H. Roos, Ambroise Desfosses and Winfried Weissenhorn
Structural basis of CHMP2A–CHMP3 ESCRT-III polymer assembly and membrane cleavage
Nature Structural & Molecular Biology volume 30, pages 81–90 (2023)
DOI: https://doi.org/10.1038/s41594-022-00867-8

Rei Esaki, Yohei Yasuda, Norito Kotani, Hisayoshi Matsushima and Mikito Ueda
High Speed Atomic Force Microscope Observation of Polyethylene Glycol Adsorption on Au(100)
Journal of The Electrochemical Society, 2022 169 082512
DOI: 10.1149/1945-7111/ac876c

Izabela Stupka, Yusuke Azuma, Artur P. Biela, Motonori Imamura, Simon Scheuring, Elżbieta Pyza, Olga Woźnicka, Daniel P. Maskell and Jonathan G. Heddle
Chemically induced protein cage assembly with programmable opening and cargo release
Science Advances, (2022), Vol 8, Issue 1
DOI: 10.1126/sciadv.abj9424

Shuai Zhang, Robbie Sadre, Benjamin A. Legg, Harley Pyles, Talita Perciano, E. Wes Bethel, David Baker, Oliver Rübel and James J. De Yoreo
Rotational dynamics and transition mechanisms of surface-adsorbed proteins
PNAS (2022) 119 (16) e2020242119
DOI: https://doi.org/10.1073/pnas.2020242119

Carmen M. Domínguez, Miguel García-Chamé, Ulrike Müller, Andreas Kraus, Klavdiya Gordiyenko, Ahmad Itani, Heiko Haschke, Peter Lanzerstorfer, Kersten S. Rabe and Christof M. Niemeyer
Linker Engineering of Ligand-Decorated DNA Origami Nanostructures Affects Biological Activity
Small, (2022), Volume 18, Issue 35
DOI: https://doi.org/10.1002/smll.202202704

Ken-ichi Shinohara, Yuu Makida, Takashi Oohashi and Ryoga Hori
Single-Molecule Unidirectional Processive Movement along a Helical Polymer Chain in Non-aqueous Medium
Langmuir 2022, 38, 40, 12173–12178
DOI: https://doi.org/10.1021/acs.langmuir.2c01704

Fang Jiao, François Dehez, Tao Ni, Xiulian Yu, Jeremy S. Dittman, Robert Gilbert, Christophe Chipot and Simon Scheuring
Perforin-2 clockwise hand-over-hand pre-pore to pore transition mechanism
Nature Communications volume 13, Article number: 5039 (2022)
DOI: https://doi.org/10.1038/s41467-022-32757-4

Rhythm Shukla, Francesca Lavore, Sourav Maity, Maik G. N. Derks, Chelsea R. Jones, Bram J. A. Vermeulen, Adéla Melcrová, Michael A. Morris, Lea Marie Becker, Xiaoqi Wang, Raj Kumar, João Medeiros-Silva, Roy A. M. van Beekveld, Alexandre M. J. J. Bonvin, Joseph H. Lorent, Moreno Lelli, James S. Nowick, Harold D. MacGillavry, Aaron J. Peoples, Amy L. Spoering, Losee L. Ling, Dallas E. Hughes, Wouter H. Roos, Eefjan Breukink, Kim Lewis and Markus Weingarth
Teixobactin kills bacteria by a two-pronged attack on the cell envelope
Nature volume 608, pages 390–396 (2022)
DOI: https://doi.org/10.1038/s41586-022-05019-y

Yining Jiang, Batiste Thienpont, Vinay Sapuru, Richard K. Hite, Jeremy S. Dittman, James N. Sturgis and Simon Scheuring
Membrane-mediated protein interactions drive membrane protein organization
Nature Communications volume 13, Article number: 7373 (2022)
DOI: https://doi.org/10.1038/s41467-022-35202-8

Karin Strohmeier, Martina Hofmann, Fabian Hauser, Dmitry Sivun, Sujitha Puthukodan, Andreas Karner, Georg Sandner, Pol-Edern Le Renard, Jaroslaw Jacak, and Mario Mairhofer
CRISPR/Cas9 Genome Editing vs. Over-Expression for Fluorescent Extracellular Vesicle-Labeling: A Quantitative Analysis
International Journal of Molecular Sciences 2022, 23(1), 282
DOI: https://doi.org/10.3390/ijms23010282

Jasper Fuk Woo Chan, Yoo Jin Oh, Shuofeng Yuan, Hin Chu, Man-Lung Yeung, Daniel Canena, Chris Chung-Sing Chan, Vincent Kwok-Man Poon, Chris Chun-Yiu Chan, Anna Jinxia Zhang, Jian-Piao Cai, Zi-Wei Ye, Lei Wen, Terrence Tsz-Tai Yuen, Kenn Ka-Heng Chik, Huiping Shuai, Yixin Wang, Yuxin Hou, Cuiting Luo, Wan-Mui Chan, Zhenzhi Qin, Ko-Yung Sit, Wing-Kuk Au, Maureen Legendre, Rong Zhu, Lisa Hain, Hannah Seferovic, Robert Tampé, Kelvin Kai-Wang To, Kwok-Hung Chan, Dafydd Gareth Thomas, Miriam Klausberger, Cheng Xu, James J. Moon, Johannes Stadlmann, Josef M. Penninger, Chris Oostenbrink, Peter Hinterdorfer, Kwok-Yung Yuen and David M. Markovitz
A molecularly engineered, broad-spectrum anti-coronavirus lectin inhibits SARS-CoV-2 and MERS-CoV infection in vivo
Cell Reports Medicine, Volume 3, Issue 10, 18 October 2022, 100774
DOI: https://doi.org/10.1016/j.xcrm.2022.100774

Nebojsa Jukic, Alma P. Perrino, Frédéric Humbert, Aurélien Roux and Simon Scheuring
Snf7 spirals sense and alter membrane curvature
Nature Communications volume 13, Article number: 2174 (2022)
DOI: https://doi.org/10.1038/s41467-022-29850-z

Rong Zhu, Daniel Canena, Mateusz Sikora, Miriam Klausberger, Hannah Seferovic, Ahmad Reza Mehdipour, Lisa Hain, Elisabeth Laurent, Vanessa Monteil, Gerald Wirnsberger, Ralph Wieneke, Robert Tampé, Nikolaus F. Kienzl, Lukas Mach, Ali Mirazimi, Yoo Jin Oh, Josef M. Penninger, Gerhard Hummer and Peter Hinterdorfer
Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level
Nature Communications volume 13, Article number: 7926 (2022)
DOI : https://doi.org/10.1038/s41467-022-35641-3

Ryosuke Ishimura, Afnan H. El-Gowily, Daisuke Noshiro, Satoko Komatsu-Hirota, Yasuko Ono, Mayumi Shindo, Tomohisa Hatta, Manabu Abe, Takefumi Uemura, Hyeon-Cheol Lee-Okada, Tarek M. Mohamed, Takehiko Yokomizo, Takashi Ueno, Kenji Sakimura, Tohru Natsume, Hiroyuki Sorimachi, Toshifumi Inada, Satoshi Waguri, Nobuo N. Noda and Masaaki Komatsu
The UFM1 system regulates ER-phagy through the ufmylation of CYB5R3
Nature Communications volume 13, Article number: 7857 (2022)
DOI: https://doi.org/10.1038/s41467-022-35501-0

Mohit Sharma, Artur P. Biela, Agnieszka Kowalczyk, Kinga Borzęcka-Solarz, Bernard M. A. G. Piette, Szymon Gaweł, Joshua Bishop, Philipp Kukura, Justin L. P. Benesch, Motonori Imamura, Simon Scheuring and Jonathan G. Heddle
Shape-Morphing of an Artificial Protein Cage with Unusual Geometry Induced by a Single Amino Acid Change
ACS Nanoscience Au 2022, 2, 5, 404–413
DOI: https://doi.org/10.1021/acsnanoscienceau.2c00019

Cindy Dirscherl, Sara Löchte, Zeynep Hein, Janine-Denise Kopicki, Antonia Regina Harders, Noemi Linden, Andreas Karner, Johannes Preiner, Julian Weghuber, Maria Garcia-Alai, Charlotte Uetrecht, Martin Zacharias, Jacob Piehler, Peter Lanzerstorfer and Sebastian Springer
Dissociation of β2m from MHC class I triggers formation of noncovalent transient heavy chain dimers
Journal of Cell Science, (2022) 135 (9): jcs259489.
DOI: https://doi.org/10.1242/jcs.259498

Raghavendar Reddy Sanganna Gari, Joel José Montalvo‐Acosta, George R. Heath, Yining Jiang, Xiaolong Gao, Crina M. Nimigean, Christophe Chipot and Simon Scheuring
Correlation of membrane protein conformational and functional dynamics
Nature Communications volume 12, Article number: 4363 (2021)
DOI: https://doi.org/10.1038/s41467-021-24660-1

Michaela Wenzel, Ilkay N. Celik Gulsoy, Yongqiang Gao, Zihao Teng, Joost Willemse, Martijn Middelkamp, Mariska G. M. van Rosmalen, Per W. B. Larsen, Nicole N. van der Wel, Gijs J. L. Wuite, Wouter H. Roos, and Leendert W. Hamoen
Control of septum thickness by the curvature of SepF polymers
PNAS, 118 (2) e20026351
DOI: https://doi.org/10.1073/pnas.2002635118

Sergei V. Kalinin, Shuai Zhang, Mani Valleti, Harley Pyles, David Baker, James J. De Yoreo, and Maxim Ziatdinov
Disentangling Rotational Dynamics and Ordering Transitions in a System of Self-Organizing Protein Nanorods via Rotationally Invariant Latent Representations
ACS Nano 2021, 15, 4, 6471–6480
DOI: https://doi.org/10.1021/acsnano.0c08914

Alma P. Perrino, Atsushi Miyagi and Simon Scheuring
Single molecule kinetics of bacteriorhodopsin by HS-AFM
Nature Communications volume 12, Article number: 7225 (2021)
DOI: https://doi.org/10.1038/s41467-021-27580-2

Ana Rita Cruz, Maurits A. den Boer, Jürgen Strasser, Seline A. Zwarthoff, Frank J. Beurskens, Carla J. C. de Haas, Piet C. Aerts, Guanbo Wang, Rob N. de Jong, Fabio Bagnoli, Jos A. G. van Strijp, Kok P. M. van Kessel, Janine Schuurman, Johannes Preiner, Albert J. R. Heck, and Suzan H. M. Rooijakkers
Staphylococcal protein A inhibits complement activation by interfering with IgG hexamer formation
PNAS February 16, 2021 118 (7) e2016772118
DOI: https://doi.org/10.1073/pnas.2016772118
https://www.pnas.org/content/pnas/118/7/e2016772118.full.pdf

Joschka Hellmeier, Rene Platzer, Alexandra S. Eklund, Thomas Schlichthaerle, Andreas Karner, Viktoria Motsch, Magdalena C. Schneider, Elke Kurz, Victor Bamieh, Mario Brameshuber, Johannes Preiner, Ralf Jungmann, Hannes Stockinger, Gerhard J. Schütz,
Johannes B. Huppa and Eva Sevcsik
DNA origami demonstrate the unique stimulatory power of single pMHCs as T cell antigens
PNAS, (2021), 118 (4) e2016857118
DOI: https://doi.org/10.1073/pnas.2016857118

George R. Heath, Ekaterina Kots, Janice L. Robertson, Shifra Lansky, George Khelashvili, Harel Weinstein and Simon Scheuring
Localization atomic force microscopy
Nature volume 594, pages 385–390 (2021)
DOI: https://doi.org/10.1038/s41586-021-03551-x

Pedro Buzón, Sourav Maity, Panagiotis Christodoulis, Monique J. Wiertsema, Steven Dunkelbarger, Christine Kim, Gijs J.L. Wuite, Adam Zlotnick and Wouter H. Roos
Virus self-assembly proceeds through contact-rich energy minima
Science Advances (2021), Vol 7, Issue 45
DOI: 10.1126/sciadv.abg0811

Seline A. Zwarthoff, Kevin Widmer, Annemarie Kuipers, Jürgen Strasser, Maartje Ruyken, Piet C. Aerts, Carla J. C. de Haas, Deniz Ugurlar, Maurits A. den Boer, Gestur Vidarsson, Jos A. G. van Strijp, Piet Gros, Paul W. H. I. Parren, Kok P. M. van Kessel, Johannes Preiner, Frank J. Beurskens, Janine Schuurman, Daniel Ricklin and Suzan H. M. Rooijakkers
C1q binding to surface-bound IgG is stabilized by C1r2s2 proteases
PNAS (2021), 118 (26) e21027871
DOI: https://doi.org/10.1073/pnas.2102787118

David Hoffmann, Stefan Mereiter, Yoo Jin Oh, Vanessa Monteil, Elizabeth Elder, Rong Zhu, Daniel Canena, Lisa Hain, Elisabeth Laurent, Clemens Grünwald-Gruber, Miriam Klausberger, Gustav Jonsson, Max J Kellner, Maria Novatchkova, Melita Ticevic, Antoine Chabloz, Gerald Wirnsberger, Astrid Hagelkruys, Friedrich Altmann, Lukas Mach, Johannes Stadlmann, Chris Oostenbrink, Ali Mirazimi, Peter Hinterdorfer and Josef M Penninger
Identification of lectin receptors for conserved SARS-CoV-2 glycosylation sites
The EMBO Journal (2021)40:e108375
DOI: https://doi.org/10.15252/embj.2021108375

Hiroko Tadokoro, Akiyoshi Hirayama, Ryuhei Kudo, Masako Hasebe, Yusuke Yoshioka, Juntaro Matsuzaki, Yusuke Yamamoto, Masahiro Sugimoto, Tomoyoshi Soga, Takahiro Ochiya
Adenosine leakage from perforin-burst extracellular vesicles inhibits perforin secretion by cytotoxic T-lymphocytes
PLoS ONE 15(4): e0231430
DOI: https://doi.org/10.1371/journal.pone.0231430

Kylee Sullivan, Yuliang Zhang, Joseph Lopez, Mary Lowe and Aleksandr Noy
Carbon nanotube porin diffusion in mixed composition supported lipid bilayers
Nature Scientific Reports volume 10, Article number: 11908 (2020)
DOI: https://doi.org/10.1038/s41598-020-68059-2

Je-Kyung Ryu, Allard J. Katan, Eli O. van der Sluis, Thomas Wisse, Ralph de Groot, Christian H. Haering and Cees Dekker
The condensin holocomplex cycles dynamically between open and collapsed states
Nature Structural & Molecular Biology volume 27, pages1134–1141(2020)
DOI: https://doi.org/10.1038/s41594-020-0508-3

Alejandro Valbuena, Sourav Maity, Mauricio G. Mateu and Wouter H. Roos
Visualization of Single Molecules Building a Viral Capsid Protein Lattice through Stochastic Pathways
ACS Nano 2020, 14, 7, 8724–8734
DOI: https://doi.org/10.1021/acsnano.0c03207

Sourav Maity, Jim Ottelé, Guillermo Monreal Santiago, Pim W. J. M. Frederix, Peter Kroon, Omer Markovitch, Marc C. A. Stuart, Siewert J. Marrink*, Sijbren Otto and Wouter H. Roos
Caught in the Act: Mechanistic Insight into Supramolecular Polymerization-Driven Self-Replication from Real-Time Visualization
Journal of the American Chemical Society 2020, 142, 32, 13709–13717
DOI: https://doi.org/10.1021/jacs.0c02635

Klemens Winkler, Andreas Karner, Andreas Horner, Christof Hannesschlaeger, Denis Knyazev, Christine Siligan, Mirjam Zimmermann, Roland Kuttner, Peter Pohl and Johannes Preiner
Interaction of the motor protein SecA and the bacterial protein translocation channel SecYEG in the absence of ATP
Nanoscale Advances, 2020, 2, 3431-3443
DOI: 10.1039/d0na00427h

Aurélie Bertin, Nicola de Franceschi, Eugenio de la Mora, Sourav Maity, Maryam Alqabandi, Nolwen Miguet, Aurélie di Cicco, Wouter H. Roos, Stéphanie Mangenot, Winfried Weissenhorn and Patricia Bassereau
Human ESCRT-III polymers assemble on positively curved membranes and induce helical membrane tube formation
Nature Communications volume 11, Article number: 2663 (2020)
DOI: https://doi.org/10.1038/s41467-020-16368-5

Tina R. Matin, George R. Heath, Gerard H. M. Huysmans, Olga Boudker and Simon Scheuring
Millisecond dynamics of an unlabeled amino acid transporter
Nature Communications volume 11, Article number: 5016 (2020)
DOI: https://doi.org/10.1038/s41467-020-18811-z

Xu Xu, Toshiaki Nakano, Masataka Tsuda, Ryota Kanamoto, Ryoichi Hirayama, Akiko Uzawa, Hiroshi Ide
Direct observation of damage clustering in irradiated DNA with atomic force microscopy
Nucleic Acids Research, Volume 48, Issue 3, 20 February 2020, Page e18,
DOI: https://doi.org/10.1093/nar/gkz1159

Francesca Zuttion, Adai Colom, Stefan Matile, Denes Farago, Frédérique Pompeo, Janos Kokavecz, Anne Galinier, James Sturgis and Ignacio Casuso
High-speed atomic force microscopy highlights new molecular mechanism of daptomycin action
Nature Communications volume 11, Article number: 6312 (2020
DOI: https://doi.org/10.1038/s41467-020-19710-z

Sourav Maity, Christophe Caillat, Nolwenn Miguet, Guidenn Sulbaran, Gregory Effantin, Guy Schoehn, Wouter H.Roos, Winfried Weissenhorn
VPS4 triggers constriction and cleavage of ESCRT-III helical filaments
Science Advances 10 Apr 2019: Vol. 5, no. 4, eaau7198
DOI: 10.1126/sciadv.aau7198
https://advances.sciencemag.org/content/advances/5/4/eaau7198.full.pdf

Alison O. Nwokeoji, Sandip Kumar, Peter M. Kilby, David E. Portwood, Jamie K. Hobbs and Mark J. Dickman
Analysis of long dsRNA produced in vitro and in vivo using atomic force microscopy in conjunction with ion-pair reverse-phase HPLC
Analyst, 2019,144, 4985-4994
DOI: https://doi.org/10.1039/C9AN00954J
https://pubs.rsc.org/en/content/articlepdf/2019/an/c9an00954j

Shinji Saito, Kaori Sano, Tadaki Suzuki, Akira Ainai, Yuki Taga, Tomonori Ueno, Koshiro Tabata, Kumpei Saito, Yuji Wada, Yuki Ohara, Haruko Takeyama, Takato Odagiri, Tsutomu Kageyama, Kiyoko Ogawa-Goto, Pretty Multihartina, Vivi Setiawaty, Krisna Nur Andriana Pangesti, Hideki Hasegawa
IgA tetramerization improves target breadth but not peak potency of functionality of anti-influenza virus broadly neutralizing antibody
PLoS Pathogens 15(1):e1007427
DOI: https://doi.org/10.1371/journal.ppat.1007427

Ken-ichi Shinohara, Masahiro Yanagisawa and Yuu Makida
Direct Observation of Long-Chain Branches in a Low-Density Polyethylene
Nature Scientific Reports volume 9, Article number: 9791 (2019)
DOI: https://doi.org/10.1038/s41598-019-46035-9

Michael C. Owen, Andreas Karner, Radek Šachl, Johannes Preiner, Mariana Amaro and Robert Vácha
Force Field Comparison of GM1 in a DOPC Bilayer Validated with AFM and FRET Experiments
Journal of Physical Chemistry, B 2019, 123, 35, 7504–7517
DOI: https://doi.org/10.1021/acs.jpcb.9b05095
https://d1wqtxts1xzle7.cloudfront.net/63935681/Owen_et_al._2019.pdf?1594887925=&response-content-disposition=inline%3B+filename%3DForce_Field_Comparison_of_GM1_in_a_DOPC.pdf&Expires=1618506116&Signature=IA0sg5fdmkgsL-YZha7VX-c31mJ6yI~yd1x~xdoOhTtTDUtHmH~EiDk4gCGrtaLG45nX9atyEa2NGrw~D95hdz7qImEPiYRLg~wIuj4ww~H9Ys9eClCUAm0pFn6BSKV-R0k1rA-DgmRhyvEbSWnVxuLL5UsbBacnoXk5k6k7tG6QmLMtri0hQho9z2rBKoUR0SnK6SKLe1cUA4m8rYxRGWI33RoUHtTi9fU9S2ggS703sUxWA4OG6IaPZW~rdqpxf7BGF4lFT01npXxfyj8-y9x15r-4aVhxD1I~PpC30icMbPcqc9Vodt2v1izkp4WMjsPIl3MLerjz6DdnOzBTvg__&Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA

Takashi Mino, Noriki Iwai, Masayuki Endo, Kentaro Inoue, Kotaro Akaki, Fabian Hia, Takuya Uehata, Tomoko Emura, Kumi Hidaka, Yutaka Suzuki, Daron M Standley, Mariko Okada-Hatakeyama, Shigeo Ohno, Hiroshi Sugiyama, Akio Yamashita, Osamu Takeuchi
Translation-dependent unwinding of stem–loops by UPF1 licenses Regnase-1 to degrade inflammatory mRNAs
Nucleic Acids Research, Volume 47, Issue 16, 19 September 2019, Pages 8838–8859
DOI: https://doi.org/10.1093/nar/gkz628

Ramya H. Tunuguntla, Andrew Y. Hu,a Yuliang Zhanga and Aleksandr Noy
Impact of PEG additives and pore rim functionalization on water transport through sub-1 nm carbon nanotube porins
Faraday Discussions, 2018,209, 359-369
DOI: https://doi.org/10.1039/C8FD00068A
https://pubs.rsc.org/fa/content/getauthorversionpdf/C8FD00068A

Fidan Sumbul, Arin Marchesi, Hirohide Takahashi,Simon Scheuring, and Felix Rico
High-Speed Force Spectroscopy for Single Protein Unfolding
Lyubchenko Y. (eds) Nanoscale Imaging. Methods in Molecular Biology, vol 1814. Humana Press, New York, NY 2018
DOI: https://doi.org/10.1007/978-1-4939-8591-3_15
https://www.researchgate.net/profile/Fidan-Sumbul/publication/326404578_High-Speed_Force_Spectroscopy_for_Single_Protein_Unfolding/links/5b51d28eaca27217ffa71881/High-Speed-Force-Spectroscopy-for-Single-Protein-Unfolding.pdf

Ken-ichi Shinohara and Yuu Makida
Direct observation of dynamic interaction between a functional group in a single SBR chain and an inorganic matter surface
Nature Scientific Reports volume 8, Article number: 13982 (2018)
DOI: https://doi.org/10.1038/s41598-018-32382-6

Markus Axmann, Sabine M. Meier, Andreas Karner, Witta Strobl, Herbert Stangl, and Birgit Plochberger
Serum and Lipoprotein Particle miRNA Profile in Uremia Patients
Genes 2018, 9(11), 533
DOI: https://doi.org/10.3390/genes9110533

Jeremy R. Sanborn, Xi Chen, Yun‐Chiao Yao, Joshua A. Hammons, Ramya H. Tunuguntla, Yuliang Zhang, Christina C. Newcomb, Jennifer A. Soltis, James J. De Yoreo, Anthony Van Buuren, Atul N. Parikh, Aleksandr Noy
Carbon Nanotube Porins in Amphiphilic Block Copolymers as Fully Synthetic Mimics of Biological Membranes
Advanced Materials, Volume 30, Issue 51 (2018), 1803355
DOI: https://doi.org/10.1002/adma.201803355
https://escholarship.org/content/qt5h4562fc/qt5h4562fc.pdf

George R. Heath and Simon Scheuring
High-speed AFM height spectroscopy reveals µs-dynamics of unlabeled biomolecules
Nature Communications volume 9, Article number: 4983 (2018)
DOI: https://doi.org/10.1038/s41467-018-07512-3

Annafrancesca Rigato, Atsushi Miyagi, Simon Scheuring and Felix Rico
High-frequency microrheology reveals cytoskeleton dynamics in living cells
Nature Physics volume 13, pages771–775(2017)
DOI: https://doi.org/10.1038/nphys4104

Yuliang Zhang, Ramya H. Tunuguntla, Pyung-On Choi and Aleksandr Noy
Real-time dynamics of carbon nanotube porins in supported lipid membranes visualized by high-speed atomic force microscopy
Philosophical Transaction of the Royal Society B372 20160226 20160226
DOI: https://doi.org/10.1098/rstb.2016.0226

Kenji Suda, Tatsuya Murakami, Norimoto Gotoh, Ryosuke Fukuda, Yasuhiko Hashida, Mitsuru Hashida, Akitaka Tsujikawa, Nagahisa Yoshimura
High-density lipoprotein mutant eye drops for the treatment of posterior eye diseases
Journal of Controlled Release, Volume 266, 28 November 2017, Pages 301-309
DOI: https://doi.org/10.1016/j.jconrel.2017.09.036
https://repository.kulib.kyoto-u.ac.jp/dspace/bitstream/2433/231013/2/digak04310.pdf

Andreas Karner, Benedikt Nimmervoll, Birgit Plochberger, Enrico Klotzsch, Andreas Horner, Denis G. Knyazev, Roland Kuttner, Klemens Winkler, Lukas Winter, Christine Siligan, Nicole Ollinger, Peter Pohl and Johannes Preiner
Tuning membrane protein mobility by confinement into nanodomains
Nature Nanotechnology volume 12, pages260–266(2017)
DOI: https://doi.org/10.1038/nnano.2016.236
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5734611/

Xiang Ma, Shuai Zhang, Fang Jiao, Christina J. Newcomb, Yuliang Zhang, Arushi Prakash, Zhihao Liao, Marcel D. Baer, Christopher J. Mundy, James Pfaendtner, Aleksandr Noy, Chun-Long Chen and James J. De Yoreo
Tuning crystallization pathways through sequence engineering of biomimetic polymers
Nature Materials volume 16, pages767–774(2017)
DOI: https://doi.org/10.1038/nmat4891
https://www.osti.gov/pages/servlets/purl/1513103

Jorine M.Eeftens, Allard J. Katan, Marc Kschonsak, Markus Hassler, Lizade Wilde, Essam M.Dief, Christian H.Haering, Cees Dekker
Condensin Smc2-Smc4 Dimers Are Flexible and Dynamic
Cell Reports, Volume 14, Issue 8, 1 March 2016, Pages 1813-1818
DOI: https://doi.org/10.1016/j.celrep.2016.01.063
https://www.sciencedirect.com/science/article/pii/S2211124716300560

Hirohide Takahashi, Atsushi Miyagi, Lorena Redondo‐Morata, Simon Scheuring
Temperature‐Controlled High‐Speed AFM: Real‐Time Observation of Ripple Phase Transitions
Small Nano Micro, Volume12, Issue 44, November 23, 2016, Pages 6106-6113
DOI: https://doi.org/10.1002/smll.201601549
https://www.hal.inserm.fr/inserm-01653778/document

Tomoyuki Ikai, Yugaku Takagi, Ken-ichi Shinohara, Katsuhiro Maeda and Shigeyoshi Kanoh
Synthesis of polyisocyanides bearing oligothiophene pendants: higher-order structural control through pendant framework design
Polymer Journal volume 47, pages625–630 (2015)
DOI: https://doi.org/10.1038/pj.2015.42

Print

For more information contact: info@nanoworld.com

Pointprobe® is a registered trademark of NanoWorld AG

All data are subject to change without notice.

NanoWorld AG
Rue des Saars 10
CH-2000 Neuchâtel,
Switzerland
www.nanoworld.com