Interactions between mannose-binding lectin and MASPs during complement activation by the lectin pathway

по Wallis, Russell
Опубликовано 2007

Carbohydrate recognition and complement activation by rat ficolin-B

по Girija, Umakhanth Venkatraman, Mitchell, Daniel A, Roscher, Silke, Wallis, Russell
Опубликовано 2011

Simultaneous Activation of Complement and Coagulation by MBL-Associated Serine Protease 2

по Krarup, Anders, Wallis, Russell, Presanis, Julia S., Gál, Péter, Sim, Robert B.
Опубликовано 2007

Near-planar Solution Structures of Mannose-binding Lectin Oligomers Provide Insight on Activation of Lectin Pathway of Complement

по Miller, Ami, Phillips, Anna, Gor, Jayesh, Wallis, Russell, Perkins, Stephen J.
Опубликовано 2012

Paths reunited: initiation of the classical and lectin pathways of complement activation

по Wallis, Russell, Mitchell, Daniel A., Schmid, Ralf, Schwaeble, Wilhelm W., Keeble, Anthony H.
Опубликовано 2009

Lysyl Hydroxylase 3 Modifies Lysine Residues to Facilitate Oligomerization of Mannan-Binding Lectin

по Risteli, Maija, Ruotsalainen, Heli, Bergmann, Ulrich, Venkatraman Girija, Umakhanth, Wallis, Russell, Myllylä, Raili
Опубликовано в: PLoS One (2014)

Localization and Characterisation of the MASP-2 binding site in rat ficolin-A: Equivalent binding sites within the collagenous domains of Mannose-binding Lectins and Ficolins

по Girija, Umakhanth Venkatraman, Dodds, Alister W., Roscher, Silke, Reid, Kenneth B. M., Wallis, Russell
Опубликовано 2007

C1q, the recognition subcomponent of the classical pathway of complement, drives microglial activation

по Färber, Katrin, Cheung, Giselle, Mitchell, Daniel, Wallis, Russell, Weihe, Eberhard, Schwaeble, Wilhelm, Kettenmann, Helmut
Опубликовано 2009

l‐Fucose prevention of renal ischaemia/reperfusion injury in Mice

по Howard, Mark C., Nauser, Christopher L., Farrar, Conrad A., Wallis, Russell, Sacks, Steven H.
Опубликовано в: FASEB J (2019)

Flexibility in Mannan-Binding Lectin-Associated Serine Proteases-1 and -2 Provides Insight on Lectin Pathway Activation

по Nan, Ruodan, Furze, Christopher M., Wright, David W., Gor, Jayesh, Wallis, Russell, Perkins, Stephen J.
Опубликовано в: Structure (2017)

Crystal structure of the CUB1-EGF-CUB2 region of mannose-binding protein associated serine protease-2

по Feinberg, Hadar, Uitdehaag, Joost C.M., Davies, Jason M., Wallis, Russell, Drickamer, Kurt, Weis, William I.
Опубликовано 2003

Rationale for targeting complement in COVID‐19

по Polycarpou, Anastasia, Howard, Mark, Farrar, Conrad A, Greenlaw, Roseanna, Fanelli, Giorgia, Wallis, Russell, Klavinskis, Linda S, Sacks, Steven
Опубликовано в: EMBO Mol Med (2020)

Engineering Novel Complement Activity into a Pulmonary Surfactant Protein

по Venkatraman Girija, Umakhanth, Furze, Christopher, Toth, Julia, Schwaeble, Wilhelm J., Mitchell, Daniel A., Keeble, Anthony H., Wallis, Russell
Опубликовано 2010

High-Affinity Glycopolymer Binding to Human DC-SIGN and Disruption of DC-SIGN Interactions with HIV Envelope Glycoprotein

по Becer, C. Remzi, Gibson, Matthew I., Geng, Jin, Ilyas, Rebecca, Wallis, Russell, Mitchell, Daniel A., Haddleton, David M.
Опубликовано 2010

Identification of the minimal binding region of a Plasmodium falciparum IgM binding PfEMP1 domain

по Semblat, Jean-Philippe, Ghumra, Ashfaq, Czajkowsky, Daniel M., Wallis, Russell, Mitchell, Daniel A., Raza, Ahmed, Rowe, J.Alexandra
Опубликовано в: Mol Biochem Parasitol (2015)

H-ficolin binds Aspergillus fumigatus leading to activation of the lectin complement pathway and modulation of lung epithelial immune responses

по Bidula, Stefan, Sexton, Darren W, Yates, Matthew, Abdolrasouli, Alireza, Shah, Anand, Wallis, Russell, Reed, Anna, Armstrong-James, Darius, Schelenz, Silke
Опубликовано в: Immunology (2015)

Light Scattering By Optically-Trapped Vesicles Affords Unprecedented Temporal Resolution Of Lipid-Raft Dynamics

по Collard, Liam, Perez-Guaita, David, Faraj, Bayan H. A., Wood, Bayden R., Wallis, Russell, Andrew, Peter W., Hudson, Andrew J.
Опубликовано в: Sci Rep (2017)

The Recognition Unit of FIBCD1 Organizes into a Noncovalently Linked Tetrameric Structure and Uses a Hydrophobic Funnel (S1) for Acetyl Group Recognition

по Thomsen, Theresa, Moeller, Jesper B., Schlosser, Anders, Sorensen, Grith L., Moestrup, Soren K., Palaniyar, Nades, Wallis, Russell, Mollenhauer, Jan, Holmskov, Uffe
Опубликовано 2010

Formation of pre-pore complexes of pneumolysin is accompanied by a decrease in short-range order of lipid molecules throughout vesicle bilayers

по Faraj, Bayan H. A., Collard, Liam, Cliffe, Rachel, Blount, Leanne A., Lonnen, Rana, Wallis, Russell, Andrew, Peter W., Hudson, Andrew J.
Опубликовано в: Sci Rep (2020)

Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97

по Yuan, Xuemei, Simpson, Peter, Mckeown, Ciaran, Kondo, Hisao, Uchiyama, Keiji, Wallis, Russell, Dreveny, Ingrid, Keetch, Catherine, Zhang, Xiaodong, Robinson, Carol, Freemont, Paul, Matthews, Stephen
Опубликовано 2004