Manajit Hayer-Hartl
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Explore the profile of Manajit Hayer-Hartl including associated specialties, affiliations and a list of published articles.
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72
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7985
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Recent Articles
1.
Cairo L, Hong X, Muller M, Yuste-Checa P, Jagadeesan C, Bracher A, et al.
Cell
. 2024 Jun;
187(17):4656-4673.e28.
PMID: 38942013
The ability of proteins and RNA to coalesce into phase-separated assemblies, such as the nucleolus and stress granules, is a basic principle in organizing membraneless cellular compartments. While the constituents...
2.
Gionfriddo M, Zang K, Hayer-Hartl M
FEBS Lett
. 2023 Jun;
597(13):1679-1680.
PMID: 37334940
Photosynthesis uses the energy of sunlight to convert water and atmospheric CO into sugars, providing food and oxygen for life. The fixation of atmospheric CO in this crucial biological process...
3.
Wang H, Hayer-Hartl M
Methods Mol Biol
. 2022 Oct;
2563:269-296.
PMID: 36227479
Carboxysomes are large, cytosolic bodies present in all cyanobacteria and many proteobacteria that function as the sites of photosynthetic CO fixation by the enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). The carboxysome lumen...
4.
Zang K, Wang H, Hartl F, Hayer-Hartl M
Nat Struct Mol Biol
. 2021 Nov;
28(11):909-922.
PMID: 34759380
Carboxysomes in cyanobacteria enclose the enzymes Rubisco and carbonic anhydrase to optimize photosynthetic carbon fixation. Understanding carboxysome assembly has implications in agricultural biotechnology. Here we analyzed the role of the...
5.
Zhao L, Castanie-Cornet M, Kumar S, Genevaux P, Hayer-Hartl M, Hartl F
Mol Cell
. 2021 Jun;
81(14):2914-2928.e7.
PMID: 34107307
Molecular chaperones assist with protein folding by interacting with nascent polypeptide chains (NCs) during translation. Whether the ribosome can sense chaperone defects and, in response, abort translation of misfolding NCs...
6.
Flecken M, Wang H, Popilka L, Hartl F, Bracher A, Hayer-Hartl M
Cell
. 2020 Sep;
183(2):457-473.e20.
PMID: 32979320
Rubisco, the key enzyme of CO fixation in photosynthesis, is prone to inactivation by inhibitory sugar phosphates. Inhibited Rubisco undergoes conformational repair by the hexameric AAA+ chaperone Rubisco activase (Rca)...
7.
Hayer-Hartl M, Hartl F
Trends Biochem Sci
. 2020 May;
45(9):748-763.
PMID: 32471779
A major challenge faced by human civilization is to ensure that agricultural productivity keeps pace with population growth and a changing climate. All food supply is generated, directly or indirectly,...
8.
Balchin D, Hayer-Hartl M, Hartl F
FEBS Lett
. 2020 May;
594(17):2770-2781.
PMID: 32446288
Molecular chaperones are highly conserved proteins that promote proper folding of other proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking, the assembly of oligomeric complexes,...
9.
Bracher A, Paul S, Wang H, Wischnewski N, Hartl F, Hayer-Hartl M
PLoS One
. 2020 Apr;
15(4):e0230090.
PMID: 32339190
Chaperonins are ubiquitous molecular chaperones found in all domains of life. They form ring-shaped complexes that assist in the folding of substrate proteins in an ATP-dependent reaction cycle. Key to...
10.
Singh A, Balchin D, Imamoglu R, Hayer-Hartl M, Hartl F
J Mol Biol
. 2020 Mar;
432(7):2304-2318.
PMID: 32135190
The cylindrical chaperonin GroEL and its cofactor GroES mediate ATP-dependent protein folding in Escherichia coli by transiently encapsulating non-native substrate in a nano-cage formed by the GroEL ring cavity and...