In vitro studies of maleidride-forming enzymes

to related objects

Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource

Language: Englisch

Bibliographic citation: In: Yin, S.; Friedrich, S.; Hrupinsa, V.; Cox, R.J.: In vitro studies of maleidride-forming enzymes. In: RSC Advances 11 (2021), Nr. 25, S. 14922-14931. DOI: https://doi.org/10.1039/D1RA02118D

Event: Veröffentlichung

(where): Hannover

(who): Gottfried Wilhelm Leibniz Universität Hannover

(when): 2021

Event: Veröffentlichung

(where): Hannover

(who): Technische Informationsbibliothek (TIB)

(when): 2021

Creator: Yin, Sen
Friedrich, Steffen
Hrupinsa, Vjaceslavs
Cox, Russell

DOI: 10.15488/11185

URN: urn:nbn:de:101:1-2021082006281452407727

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:53 AM CEST

Data provider

This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.

Show original at data provider

Associated

Yin, Sen
Friedrich, Steffen
Hrupinsa, Vjaceslavs
Cox, Russell
Gottfried Wilhelm Leibniz Universität Hannover
Technische Informationsbibliothek (TIB)

Time of origin

2021

Other Objects (12)

Curiouser and curiouser: progress in understanding the programming of iterative highly-reducing polyketide synthases

Oxidative rearrangements during fungal biosynthesis

Investigating and engineering fungal tropolone meroterpenoid biosynthesis

Reductive Release from a Hybrid PKS‐NRPS during the Biosynthesis of Pyrichalasin H

Three previously unrecognised classes of biosynthetic enzymes revealed during the production of xenovulene A

The molecular steps of citrinin biosynthesis in fungi

Classic fungal natural products in the genomic age: The molecular legacy of Harold Raistrick

Reengineering the programming of a functional domain of an iterative highly reducing polyketide synthase

Oxidative steps during the biosynthesis of squalestatin S1

Stereochemical and Biosynthetic Rationalisation of the Tropolone Sesquiterpenoids

Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme

Curiouser and curiouser: progress in understanding the programming of iterative highly-reducing polyketide synthases

Oxidative rearrangements during fungal biosynthesis

Investigating and engineering fungal tropolone meroterpenoid biosynthesis

Reductive Release from a Hybrid PKS‐NRPS during the Biosynthesis of Pyrichalasin H

Three previously unrecognised classes of biosynthetic enzymes revealed during the production of xenovulene A

The molecular steps of citrinin biosynthesis in fungi

Classic fungal natural products in the genomic age: The molecular legacy of Harold Raistrick

Reengineering the programming of a functional domain of an iterative highly reducing polyketide synthase

Oxidative steps during the biosynthesis of squalestatin S1

Stereochemical and Biosynthetic Rationalisation of the Tropolone Sesquiterpenoids

Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme

Curiouser and curiouser: progress in understanding the programming of iterative highly-reducing polyketide synthases

Oxidative rearrangements during fungal biosynthesis

Investigating and engineering fungal tropolone meroterpenoid biosynthesis

Reductive Release from a Hybrid PKS‐NRPS during the Biosynthesis of Pyrichalasin H

Three previously unrecognised classes of biosynthetic enzymes revealed during the production of xenovulene A

The molecular steps of citrinin biosynthesis in fungi

Classic fungal natural products in the genomic age: The molecular legacy of Harold Raistrick

Reengineering the programming of a functional domain of an iterative highly reducing polyketide synthase

Oxidative steps during the biosynthesis of squalestatin S1

Stereochemical and Biosynthetic Rationalisation of the Tropolone Sesquiterpenoids

Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme

Cultural heritage institutions wishing to register will find more information here.

Fields marked * need to be filled in.

Username*

Please enter your username

Email*

Please enter your email address

Please do not fill this field

First name

Last name

Password*

Please enter your password

Confirm password*

Please enter the same password

I have read the terms of use and the privacy policy for the collection of personal data and accept them. *

This field is required.

I would like to subscribe to the newsletter of the Deutsche Digitale Bibliothek. See newsletter subscription info.

Account created

Your "My DDB" account has been successfully created. Before you can log in to your account, you must click the confirmation link in the message we just sent to the email address you provided.

In vitro studies of maleidride-forming enzymes

Object Details

References and Relationships

Contributors, Places and Time

Further information

Data provider

Associated

Time of origin

Other Objects (12)

Curiouser and curiouser: progress in understanding the programming of iterative highly-reducing polyketide synthases

Oxidative rearrangements during fungal biosynthesis

Investigating and engineering fungal tropolone meroterpenoid biosynthesis

Reductive Release from a Hybrid PKS‐NRPS during the Biosynthesis of Pyrichalasin H

Three previously unrecognised classes of biosynthetic enzymes revealed during the production of xenovulene A

The molecular steps of citrinin biosynthesis in fungi

Classic fungal natural products in the genomic age: The molecular legacy of Harold Raistrick

Reengineering the programming of a functional domain of an iterative highly reducing polyketide synthase

Oxidative steps during the biosynthesis of squalestatin S1

Stereochemical and Biosynthetic Rationalisation of the Tropolone Sesquiterpenoids

Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme

Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme

Curiouser and curiouser: progress in understanding the programming of iterative highly-reducing polyketide synthases

Oxidative rearrangements during fungal biosynthesis

Investigating and engineering fungal tropolone meroterpenoid biosynthesis

Reductive Release from a Hybrid PKS‐NRPS during the Biosynthesis of Pyrichalasin H

Three previously unrecognised classes of biosynthetic enzymes revealed during the production of xenovulene A

The molecular steps of citrinin biosynthesis in fungi

Classic fungal natural products in the genomic age: The molecular legacy of Harold Raistrick

Reengineering the programming of a functional domain of an iterative highly reducing polyketide synthase

Oxidative steps during the biosynthesis of squalestatin S1

Stereochemical and Biosynthetic Rationalisation of the Tropolone Sesquiterpenoids

Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme

Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme

Curiouser and curiouser: progress in understanding the programming of iterative highly-reducing polyketide synthases

Oxidative rearrangements during fungal biosynthesis

Investigating and engineering fungal tropolone meroterpenoid biosynthesis

Reductive Release from a Hybrid PKS‐NRPS during the Biosynthesis of Pyrichalasin H

Three previously unrecognised classes of biosynthetic enzymes revealed during the production of xenovulene A

The molecular steps of citrinin biosynthesis in fungi

Classic fungal natural products in the genomic age: The molecular legacy of Harold Raistrick

Reengineering the programming of a functional domain of an iterative highly reducing polyketide synthase

Oxidative steps during the biosynthesis of squalestatin S1

Stereochemical and Biosynthetic Rationalisation of the Tropolone Sesquiterpenoids

Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme

Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme

Related objects

Reset password