A citation-based method for searching scientific literature

Cristina Puchades, Bojian Ding, Albert Song, R Luke Wiseman, Gabriel C Lander, Steven E Glynn. Mol Cell 2019
Times Cited: 29







List of co-cited articles
494 articles co-cited >1



Times Cited
  Times     Co-cited
Similarity


Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing.
Cristina Puchades, Anthony J Rampello, Mia Shin, Christopher J Giuliano, R Luke Wiseman, Steven E Glynn, Gabriel C Lander. Science 2017
107
65

Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104.
Stephanie N Gates, Adam L Yokom, JiaBei Lin, Meredith E Jackrel, Alexandrea N Rizo, Nathan M Kendsersky, Courtney E Buell, Elizabeth A Sweeny, Korrie L Mack, Edward Chuang,[...]. Science 2017
151
41

Evolutionary relationships and structural mechanisms of AAA+ proteins.
Jan P Erzberger, James M Berger. Annu Rev Biophys Biomol Struct 2006
516
34

Substrate-engaged 26S proteasome structures reveal mechanisms for ATP-hydrolysis-driven translocation.
Andres H de la Peña, Ellen A Goodall, Stephanie N Gates, Gabriel C Lander, Andreas Martin. Science 2018
121
34

Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding.
Edward C Twomey, Zhejian Ji, Thomas E Wales, Nicholas O Bodnar, Scott B Ficarro, Jarrod A Marto, John R Engen, Tom A Rapoport. Science 2019
93
34

Structural basis of protein translocation by the Vps4-Vta1 AAA ATPase.
Nicole Monroe, Han Han, Peter S Shen, Wesley I Sundquist, Christopher P Hill. Elife 2017
74
31

Evolutionary history and higher order classification of AAA+ ATPases.
Lakshminarayan M Iyer, Detlef D Leipe, Eugene V Koonin, L Aravind. J Struct Biol 2004
556
31

Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome.
Yuanchen Dong, Shuwen Zhang, Zhaolong Wu, Xuemei Li, Wei Li Wang, Yanan Zhu, Svetla Stoilova-McPhie, Ying Lu, Daniel Finley, Youdong Mao. Nature 2019
116
31

Structure of the Cdc48 segregase in the act of unfolding an authentic substrate.
Ian Cooney, Han Han, Michael G Stewart, Richard H Carson, Daniel T Hansen, Janet H Iwasa, John C Price, Christopher P Hill, Peter S Shen. Science 2019
60
31

AAA+ proteins: have engine, will work.
Phyllis I Hanson, Sidney W Whiteheart. Nat Rev Mol Cell Biol 2005
803
27

The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets.
Han Han, Nicole Monroe, Wesley I Sundquist, Peter S Shen, Christopher P Hill. Elife 2017
49
27

AAA+ proteases: ATP-fueled machines of protein destruction.
Robert T Sauer, Tania A Baker. Annu Rev Biochem 2011
467
27

The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission.
Ruchika Anand, Timothy Wai, Michael J Baker, Nikolay Kladt, Astrid C Schauss, Elena Rugarli, Thomas Langer. J Cell Biol 2014
385
27

Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28.
Daniela Di Bella, Federico Lazzaro, Alfredo Brusco, Massimo Plumari, Giorgio Battaglia, Annalisa Pastore, Adele Finardi, Claudia Cagnoli, Filippo Tempia, Marina Frontali,[...]. Nat Genet 2010
210
27

Reciprocal Degradation of YME1L and OMA1 Adapts Mitochondrial Proteolytic Activity during Stress.
T Kelly Rainbolt, Justine Lebeau, Cristina Puchades, R Luke Wiseman. Cell Rep 2016
87
24

Structure of a AAA+ unfoldase in the process of unfolding substrate.
Zev A Ripstein, Rui Huang, Rafal Augustyniak, Lewis E Kay, John L Rubinstein. Elife 2017
82
24

New roles for mitochondrial proteases in health, ageing and disease.
Pedro M Quirós, Thomas Langer, Carlos López-Otín. Nat Rev Mol Cell Biol 2015
284
24

The molecular principles governing the activity and functional diversity of AAA+ proteins.
Cristina Puchades, Colby R Sandate, Gabriel C Lander. Nat Rev Mol Cell Biol 2020
50
24

A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery.
Zev A Ripstein, Siavash Vahidi, Walid A Houry, John L Rubinstein, Lewis E Kay. Elife 2020
37
24

Homozygous YME1L1 mutation causes mitochondriopathy with optic atrophy and mitochondrial network fragmentation.
Bianca Hartmann, Timothy Wai, Hao Hu, Thomas MacVicar, Luciana Musante, Björn Fischer-Zirnsak, Werner Stenzel, Ralph Gräf, Lambert van den Heuvel, Hans-Hilger Ropers,[...]. Elife 2016
62
20

YME1L degradation reduces mitochondrial proteolytic capacity during oxidative stress.
T Kelly Rainbolt, Jaclyn M Saunders, R Luke Wiseman. EMBO Rep 2015
47
20

Substrate-translocating loops regulate mechanochemical coupling and power production in AAA+ protease ClpXP.
Piere Rodriguez-Aliaga, Luis Ramirez, Frank Kim, Carlos Bustamante, Andreas Martin. Nat Struct Mol Biol 2016
31
20

Structural principles of SNARE complex recognition by the AAA+ protein NSF.
K Ian White, Minglei Zhao, Ucheor B Choi, Richard A Pfuetzner, Axel T Brunger. Elife 2018
38
20

Structure and function of the AAA+ nucleotide binding pocket.
Petra Wendler, Susanne Ciniawsky, Malte Kock, Sebastian Kube. Biochim Biophys Acta 2012
179
20

ATP hydrolysis-coupled peptide translocation mechanism of Mycobacterium tuberculosis ClpB.
Hongjun Yu, Tania J Lupoli, Amanda Kovach, Xing Meng, Gongpu Zhao, Carl F Nathan, Huilin Li. Proc Natl Acad Sci U S A 2018
41
20

The conserved AAA-ATPase Msp1 confers organelle specificity to tail-anchored proteins.
Voytek Okreglak, Peter Walter. Proc Natl Acad Sci U S A 2014
113
20

OPA1 processing in cell death and disease - the long and short of it.
Thomas MacVicar, Thomas Langer. J Cell Sci 2016
231
20

Whole-exome sequencing identifies homozygous AFG3L2 mutations in a spastic ataxia-neuropathy syndrome linked to mitochondrial m-AAA proteases.
Tyler Mark Pierson, David Adams, Florian Bonn, Paola Martinelli, Praveen F Cherukuri, Jamie K Teer, Nancy F Hansen, Pedro Cruz, James C Mullikin For The Nisc Comparative Sequencing Program, Robert W Blakesley,[...]. PLoS Genet 2011
137
20

Lipid signalling drives proteolytic rewiring of mitochondria by YME1L.
Thomas MacVicar, Yohsuke Ohba, Hendrik Nolte, Fiona Carola Mayer, Takashi Tatsuta, Hans-Georg Sprenger, Barbara Lindner, Yue Zhao, Jiahui Li, Christiane Bruns,[...]. Nature 2019
51
20

Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor.
Célia Deville, Kamila Franke, Axel Mogk, Bernd Bukau, Helen R Saibil. Cell Rep 2019
25
20

UCSF Chimera--a visualization system for exploratory research and analysis.
Eric F Pettersen, Thomas D Goddard, Conrad C Huang, Gregory S Couch, Daniel M Greenblatt, Elaine C Meng, Thomas E Ferrin. J Comput Chem 2004
17

Malaria parasite translocon structure and mechanism of effector export.
Chi-Min Ho, Josh R Beck, Mason Lai, Yanxiang Cui, Daniel E Goldberg, Pascal F Egea, Z Hong Zhou. Nature 2018
83
17


Mechanism of DNA translocation in a replicative hexameric helicase.
Eric J Enemark, Leemor Joshua-Tor. Nature 2006
380
17

Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation.
Jörg Hinnerwisch, Wayne A Fenton, Krystyna J Furtak, George W Farr, Arthur L Horwich. Cell 2005
189
17


An allosteric network in spastin couples multiple activities required for microtubule severing.
Colby R Sandate, Agnieszka Szyk, Elena A Zehr, Gabriel C Lander, Antonina Roll-Mecak. Nat Struct Mol Biol 2019
20
25

Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding.
Andreas Martin, Tania A Baker, Robert T Sauer. Nat Struct Mol Biol 2008
192
17

An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases.
Steffen Augustin, Florian Gerdes, Sukyeong Lee, Francis T F Tsai, Thomas Langer, Takashi Tatsuta. Mol Cell 2009
74
17

Conformational switching of the 26S proteasome enables substrate degradation.
Mary E Matyskiela, Gabriel C Lander, Andreas Martin. Nat Struct Mol Biol 2013
169
17

Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle.
Parijat Majumder, Till Rudack, Florian Beck, Radostin Danev, Günter Pfeifer, István Nagy, Wolfgang Baumeister. Proc Natl Acad Sci U S A 2019
36
17

Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.
Steven E Glynn, Andreas Martin, Andrew R Nager, Tania A Baker, Robert T Sauer. Cell 2009
197
17


Cryo-EM structure of the ClpXP protein degradation machinery.
Christos Gatsogiannis, Dora Balogh, Felipe Merino, Stephan A Sieber, Stefan Raunser. Nat Struct Mol Biol 2019
28
17

Msp1/ATAD1 maintains mitochondrial function by facilitating the degradation of mislocalized tail-anchored proteins.
Yu-Chan Chen, George K E Umanah, Noah Dephoure, Shaida A Andrabi, Steven P Gygi, Ted M Dawson, Valina L Dawson, Jared Rutter. EMBO J 2014
107
17

Metalloproteases of the Inner Mitochondrial Membrane.
Roman M Levytskyy, Iryna Bohovych, Oleh Khalimonchuk. Biochemistry 2017
26
19

Imbalanced OPA1 processing and mitochondrial fragmentation cause heart failure in mice.
Timothy Wai, Jaime García-Prieto, Michael J Baker, Carsten Merkwirth, Paule Benit, Pierre Rustin, Francisco Javier Rupérez, Coral Barbas, Borja Ibañez, Thomas Langer. Science 2015
238
17

m-AAA proteases, mitochondrial calcium homeostasis and neurodegeneration.
Maria Patron, Hans-Georg Sprenger, Thomas Langer. Cell Res 2018
45
17

Molecular basis of selective mitochondrial fusion by heterotypic action between OPA1 and cardiolipin.
Tadato Ban, Takaya Ishihara, Hiroto Kohno, Shotaro Saita, Ayaka Ichimura, Katsumi Maenaka, Toshihiko Oka, Katsuyoshi Mihara, Naotada Ishihara. Nat Cell Biol 2017
152
17

Stress-induced OMA1 activation and autocatalytic turnover regulate OPA1-dependent mitochondrial dynamics.
Michael J Baker, Philipp A Lampe, Diana Stojanovski, Anne Korwitz, Ruchika Anand, Takashi Tatsuta, Thomas Langer. EMBO J 2014
165
17


Co-cited is the co-citation frequency, indicating how many articles cite the article together with the query article. Similarity is the co-citation as percentage of the times cited of the query article or the article in the search results, whichever is the lowest. These numbers are calculated for the last 100 citations when articles are cited more than 100 times.